EP2054513A1 - Nouvelle protéase alcaline issue de bacillus gibsonii et détergents et nettoyants contenant cette nouvelle protéase alcaline - Google Patents

Nouvelle protéase alcaline issue de bacillus gibsonii et détergents et nettoyants contenant cette nouvelle protéase alcaline

Info

Publication number
EP2054513A1
EP2054513A1 EP07847839A EP07847839A EP2054513A1 EP 2054513 A1 EP2054513 A1 EP 2054513A1 EP 07847839 A EP07847839 A EP 07847839A EP 07847839 A EP07847839 A EP 07847839A EP 2054513 A1 EP2054513 A1 EP 2054513A1
Authority
EP
European Patent Office
Prior art keywords
polypeptide
polynucleotide
acid sequence
amino acid
seq
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP07847839A
Other languages
German (de)
English (en)
Inventor
Petra Siegert
Susanne Wieland
Julia Engelskirchen
Marion Merkel
Karl-Heinz Maurer
Cornelius Bessler
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Henkel AG and Co KGaA
Original Assignee
Henkel AG and Co KGaA
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Publication of EP2054513A1 publication Critical patent/EP2054513A1/fr
Withdrawn legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A61K8/66—Enzymes
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q11/00—Preparations for care of the teeth, of the oral cavity or of dentures; Dentifrices, e.g. toothpastes; Mouth rinses
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A61Q19/10—Washing or bathing preparations
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q5/00—Preparations for care of the hair
    • A61Q5/02—Preparations for cleaning the hair
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
    • C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus

Definitions

  • the present invention relates to a novel subtilisin-type alkaline protease from Bacillus gibsonii and to sufficiently related proteins and their derivatives. It also relates to detergents and cleaners with this new Subtilisin-type alkaline protease, sufficiently related proteins and their derivatives, corresponding washing and cleaning processes and their use in detergents and cleaners, and other technical uses.
  • Enzymes are well-established active ingredients in detergents and cleaners. Proteases cause the degradation of protein-containing stains on the cleaning material, such as textiles or hard surfaces. At best, there are synergies between the enzymes and the remaining components of the funds concerned.
  • the development of detergent proteases is based on naturally, preferably microbially formed enzymes. Such are optimized by per se known mutagenesis method, for example, point mutagenesis, deletion, insertion or fusion with other proteins or protein parts or other modifications for use in detergents and cleaners.
  • subtilisins occupy an outstanding position due to their favorable enzymatic properties such as stability or pH optimum.
  • subtilisins are attributed to the serine proteases due to the catalytically active amino acids. They are naturally formed and secreted by microorganisms, especially Bacillus species. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range. An overview of this family is provided, for example, by the article "Subtilases: Subtilisin-like Proteases" by R. Siezen, pages 75-95 in “Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996. Subtilisins are suitable for a variety of technical uses, as components of cosmetics and especially as active ingredients of detergents or cleaners.
  • subtilisin BPN ' which from Bacillus amyloliquefaciens, or ß. subtilis is from the work of Vasantha et al. (1984) in J. Bacteriol., Volume 159, pp. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume V ⁇ _, pp. 7911-7925.
  • Subtilisin BPN ' serves as a reference enzyme of the subtilisins, in particular with regard to the numbering of the positions.
  • the protease subtilisin Carlsberg is described in the publications of EL Smith et al. (1968) in J. Biol. Chem., Volume 243, pp.
  • subtilisins 147 and 309 are sold under the trade names Esperase ®, or Savinase ® from Novozymes. They are originally from Bac / 7 / ⁇ / s strains, which are disclosed in the application GB 1243784.
  • subtilisin DY is originally from Nedkov et al. Chem., 1985, in Biol. Chem. Hoppe-Seyler, Vol. 366, pp. 421-430.
  • subtilisin-type proteases isolated from Bacillus strains are described in the recent patent applications WO03 / 054185 and WO03 / 054184 and in the unpublished patent application DE102006022216.
  • a strategy to improve the washing performance of the subtilisins is to substitute statistically or specifically in the known molecules individual amino acids against others and to check the variants obtained for their contributions to the washing performance.
  • the enzymes can also be improved with regard to their allergenicity with certain amino acid exchanges or deletions.
  • subtilisins In order to improve the washing performance of subtilisins, numerous applications have followed the strategy of inserting additional amino acids into the active loops. This strategy should, in principle, be applicable to all subtilisins belonging to one of subgroups I-S1 (true subtilisins) or I-S2 (highly alkaline subtilisins).
  • Another strategy of performance improvement is to change the surface charges and / or the isoelectric point of the molecules and, above that, their interactions with the substrate. Furthermore, point mutants with reduced pH dependent molecular charge variation have been described. From this principle, a method was also derived for the identification of variants, which should be suitable for use in detergents and cleaners; All disclosed variants have at least one exchange in position 103. Generally, variations in the literature are very often described as having an exchange at position 103, optionally combined with a variety of other possible substitutions.
  • An alternative way of improving the performance of detergents and cleaners is to increase the hydrophobicity of the molecules, which may affect the stability of the enzyme. Another way to modulate the performance of proteases is by forming fusion proteins.
  • fusion proteins from proteases and an inhibitor such as the Streptomyces subtilisin inhibitor are disclosed in the literature.
  • Another possibility is, for example, the coupling to the cellulase-derived cellulose binding domain (CBD) to increase the concentration of active enzyme in the immediate vicinity of the substrate or the coupling of a peptide linker and therefrom polymers to reduce the allergenicity or immunogenicity.
  • CBD cellulase-derived cellulose binding domain
  • methods for generating statistical amino acid replacements can be based on the phage display.
  • a modern direction of enzyme development is to combine elements from known, related proteins via statistical methods into new enzymes that have previously unattainable properties. Such methods are also summarized under the generic term recombination. These include, for example, the following methods: the StEP method (Zhao et al., 1998, Nat. Biotechnol., Vol. 6, pp. 258-261), random priming recombination (Shao et al., (1998), Nucleic Acids Res., Vol. 26, pp. 681-683), DNA shuffling (Stemmer, WPC (1994), Nature, Vol. 370, pp.
  • Another, and in particular complementary, strategy is to increase the stability of the proteases in question and thereby increase their effectiveness.
  • Stabilization via coupling to a polymer has been described, for example, for proteases used in cosmetics; As a result, a better skin compatibility could be achieved.
  • stabilizers by point mutations are more common, especially for detergents and cleaners.
  • proteases can be stabilized, in particular also with regard to use at elevated temperatures, by exchanging certain tyrosine residues for others.
  • Other described possibilities for stabilization via point mutagenesis are, for example:
  • proteases are used to improve the washing or cleaning performance together with ⁇ -amylases and other detergent enzymes, in particular lipases can be.
  • lipases can be used in detergents in combination with other active ingredients such as bleaching agents or soil release agents.
  • proteases established for use in detergents are also suitable for cosmetic purposes or for organic-chemical synthesis.
  • proteases with different properties, such as the reaction conditions, the stability or the substrate specificity.
  • the technical utility of the proteases depends on other factors such as stability of the enzyme to high temperatures, oxidizing agents, denaturation by surfactants, folding effects, or desired synergies with other ingredients.
  • the present invention therefore an object of the invention to find another, not yet known protease.
  • the wild-type enzyme should preferably be characterized as being at least close to the enzymes established for this purpose when used in an appropriate composition. In particular, the contribution to the performance of a detergent or cleaning agent was of interest.
  • proteases in particular of the subtilisin type, which have improved stability with respect to the prior art to temperature influences, pH fluctuations, denaturing or oxidizing agents, proteolytic degradation, high temperatures, acidic or alkaline conditions or to a change in the redox ratios.
  • Other tasks can be seen in a reduced immunogenicity or reduced allergenic effect.
  • Another particular object of the present invention was to find proteases which at temperatures of 20 to 60 0 C, a good washing performance, preferably an improved washing performance in comparison to the disclosed in the prior art proteases, in particular those of the subtilisin type have ,
  • Another particular object of the present invention has been to find proteases which have improved detergency relative to at least one soiling, preferably with respect to multiple soils, with respect to the homologous proteases known in the art.
  • proteases Other subtasks have been to provide nucleic acids encoding such proteases, and to provide vectors, host cells, and methods of production that can be used to obtain such proteases. Furthermore, appropriate means, in particular washing and cleaning agents, appropriate washing and cleaning methods and corresponding uses for such proteases should be made available. Finally, technical applications for the proteases found should be defined.
  • subtilisin-type alkaline proteases having amino acid sequences which are as described in the sequence listing under SEQ ID NO. 2 amino acid sequence given from position 115 to 383 are at least 97.5% identical and / or differ in relation to this amino acid sequence at most in 6 amino acid positions.
  • the subtilisin type naturally occurring alkaline protease underlying the present invention is obtainable from the culture supernatant of a new Bacillus gibsonii strain obtained from DSMZ (Deutsche Collection of microorganisms and cell cultures) has been identified as such. A deposit of this strain did not take place. Instead, for the purpose of reworkability according to the Budapest Treaty, a plasmid containing the nucleic acid sequence of the enzyme according to the invention, with DSMZ (German Collection of Microorganisms and Cell Cultures, Braunschweig) with the accession number DSM 18912 deposited.
  • DSMZ German Collection of Microorganisms and Cell Cultures, Braunschweig
  • the present patent application pursued the strategy of finding from a natural habitat a protease-producing microorganism and thus a naturally formed enzyme that meets the requirements as completely as possible.
  • the nucleotide sequence of the novel alkaline protease from Bacillus gibsonii according to the invention is shown in the sequence listing of the present application under SEQ ID NO. 1 indicated. It includes 1152 bp.
  • the deduced amino acid sequence is shown in SEQ ID NO. 2 indicated. It comprises 383 amino acids, followed by a stop codon. Of these, the first 114 amino acids are unlikely to be present in the mature protein, so the mature protein is expected to be 269 amino acids in length.
  • the measure of homology is a percentage of identity, such as may be determined, for example, according to the method given by D. J. Lipman and W. R. Pearson in Science 227 (1985), pp. 1435-1441. This indication may refer to the entire protein or to the respective region to be assigned.
  • a broad homology term, similarity also includes conserved variations, that is, amino acids with similar chemical activity, as these usually perform similar chemical activities within the protein. With nucleic acids one knows only the percentage of identity.
  • subtilisin HP302 from Bacillus gibsonii (described in DE 102006022216) with 88% identity
  • subtilisin TI-1 from Bacillus gibsonii (described in WO03 / 054184) with 88% identity
  • Subtilisin TII-5 from Bacillus gibsonii (described in WO03 / 054185) with 86% identity.
  • subtilisin HP302 from Bacillus gibsonii (described in DE 102006022216) with 87% identity
  • subtilisin TI-1 from Bacillus gibsonii (described in WO03 / 054184) with 86% identity
  • Subtilisin TII-5 from Bacillus gibsonii (described in WO03 / 054185) with 84% identity.
  • Subtilisin HP302 from Bacillus gibsonii (described in DE 102006022216) with 96% identity
  • Subtilisin TI-1 from Bacillus gibsonii (described in WO03 / 054184 ) with 95% identity
  • Subtilisin TII-5 from Bacillus gibsonii (described in WO03 / 054185) with 92% identity.
  • subtilisin HP302 from Bacillus gibsonii (described in DE 102006022216) with 97% identity
  • subtilisin TI-1 from Bacillus gibsonii (described in WO03 / 054184 ) with 96% identity
  • Subtilisin TII-5 from Bacillus gibsonii (described in WO03 / 054185) with 91% identity.
  • this alkaline protease is to be regarded as a subtilisin.
  • An object of the present invention is thus any polypeptide, in particular any hydrolase, especially any subtilisin-type alkaline protease, having an amino acid sequence which is at least 96.5% identical to the amino acid sequence given in SEQ ID NO: 2 and / or with respect to the amino acid sequence given in SEQ ID NO: 2 deviates at most in 14 amino acid positions.
  • those polypeptides whose amino acid sequence to the amino acid sequence given in SEQ ID NO: 2 is more preferably at least 97% or 97.5%, more preferably at least 98% or 98.5%, especially at least 99% or 99, 5% identical and / or those whose amino acid sequence in relation to the amino acid sequence given in SEQ ID NO: 2 at most in 13, 12, 11, 10, 9, 8 or 7, in particular at most in 6, 5, 4, 3 or 2 amino acid positions, more preferably at most deviates in one amino acid position.
  • Very particular preference is given to a protein having an amino acid sequence according to SEQ ID NO: 2.
  • amino acids 1 to 14 are to be regarded as leader peptide, wherein amino acids 1 to 27 presumably represent the signal peptide, and the mature protein is expected to extend from positions 115 to 383 according to SEQ ID NO: 2.
  • the position 384 is thus occupied by a stop codon, so actually corresponds to no amino acid.
  • this position is included according to the invention in the region corresponding to the mature protein.
  • a further subject of the present invention is thus any polypeptide, in particular any hydrolase, in particular any subtilisin-type alkaline protease having an amino acid sequence which is at least 97.5 to the amino acid sequence given in SEQ ID NO: 2 from position 115 to position 383 % is identical and / or deviates in relation to this amino acid sequence at most in 6 amino acid positions.
  • polypeptides whose amino acid sequence is identical to the amino acid sequence given in SEQ ID NO: 2 from position 115 to position 383 at least 98% or 98.5%, more preferably at least 99% or 99.5%, and / or those whose amino acid sequence differs at most in 5 or 4, in particular at most in 3 or 2 amino acid positions, particularly preferably at most in an amino acid position with respect to the amino acid sequence given in SEQ ID NO: 2 from position 115 to 383.
  • Very particular preference is given here to a protein having an amino acid sequence from position 115 to 383 according to SEQ ID NO: 2.
  • cleavage site is not located between the 114th and the 115th amino acids of SEQ ID NO: 2 but at a different location this information refers to the actual cleavage site or to the actual mature protein.
  • Another object of the present invention are also fragments, in particular the mature protein, provided that they are new compared to the prior art.
  • a further subject of the present invention are therefore also polypeptides which have an amino acid sequence with at least 81, preferably at least 90, 100 or 120, particularly preferably at least 150, 175 or 200, in particular at least 225 or 250, consecutive amino acids of the amino acid sequence according to SEQ ID NO: 2, in particular the amino acid sequence of position 115 to 383 according to SEQ ID NO: 2.
  • Another object of the present invention are therefore also polypeptides having an amino acid sequence with at least 127, preferably at least 140, 160 or 170, more preferably at least 180, 190 or 200, especially at least 220, 240 or 250 consecutive amino acids of the amino acid sequence of SEQ ID NO : 2, in particular the amino acid sequence of position 115 to 383 according to SEQ ID NO: 2, or at most differ in an amino acid position thereof.
  • Another object of the present invention are therefore also polypeptides having an amino acid sequence with at least 171, preferably at least 180, 190 or 200, more preferably at least 210, 220 or 230, especially at least 240, 250 or 260 consecutive amino acids of the amino acid sequence of SEQ ID NO : 2, in particular the amino acid sequence from position 115 to 383 according to SEQ ID NO: 2, or at most in two amino acid positions, preferably at most in one amino acid position, deviate therefrom.
  • Another object of the present invention are therefore also polypeptides having an amino acid sequence having at least 192, preferably at least 200, 210 or 220, more preferably at least 230, 240 or 250 consecutive amino acids of the amino acid sequence of SEQ ID NO: 2, in particular the amino acid sequence of position 115th to 383 according to SEQ ID NO. 2, or at most in three, preferably at most in two, more preferably at most in one position, deviate therefrom.
  • Another object of the present invention are therefore also polypeptides having an amino acid sequence from position 164 to position 382 of the in SEQ ID NO. 2 or at most in six or five, preferably at most in four or three, more preferably at most in two positions, especially at most in one position, deviate therefrom.
  • amino acids 1 to 114 are likely to be the leader peptide, with amino acids 1 to 27 believed to represent the signal peptide and amino acids 28 to 114 corresponding to the propeptide.
  • a further subject of the present invention are therefore polypeptides having an amino acid sequence from position 1 to 114 and from position 28 to 114 according to SEQ ID NO: 2 as well as polypeptides starting from these amino acid sequences in at most 4, preferably in at most 3 or 2 amino acid positions differ in exactly one amino acid position.
  • Another object of the present invention are polypeptides which are encoded by the polynucleotides according to the invention, mentioned below.
  • polypeptides which are derived from a nucleotide sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 nucleotide sequence is as similar as possible, in particular over the portion of the positions 1 15 to 384 of the polypeptide according to SEQ ID NO. 2 corresponds.
  • these nucleic acids encode proteins whose properties are increasingly similar to those of the alkaline protease according to the invention from Bacillus gibsonii, in particular the mature protein. Again, as for all subsequent embodiments, it again applies that these details refer to the actual mature protein, if it should turn out that the cleavage site of the protein is at a different site than indicated above.
  • subtilisin HP302 from Bacillus gibsonii (described in DE 102006022216), subtilisin TI-1 from Bacillus gibsonii (described in WO03 / 054184) and subtilisin TII-5 from Bacillus gibsonii (described in WO 03/054185) preferably those polypeptides according to the invention which, compared with this closest prior art, have an improved washing performance with respect to at least one soiling, preferably with respect to at least two soils, in particular selected from grass on cotton, milk / oil on cotton, Whole / carbon black on cotton, chocolate milk / carbon black on cotton and blood / milk on cotton, in particular at a washing temperature of 20 to 60 0 C, preferably 30 0 C, and preferably when used in a liquid detergent.
  • the most preferred embodiment of the invention is any subtilisin-type alkaline protease whose amino acid sequence is identical to that shown in SEQ ID NO. 2 overall amino acid sequence, preferably in the positions 1 15 to 383 is identical and / or their amino acid sequence of the in SEQ ID NO. 1 nucleotide sequence, preferably from positions 343 to 1 152, can be derived.
  • protease not yet known in the prior art. It is, as indicated in the examples, isolatable, manufacturable and usable. It is also characterized, as also documented in the examples, by the fact that, when used in an appropriate agent, it at least approximates, or even exceeds, the performance of enzymes established for this purpose.
  • the polypeptides according to the invention are preferably enzymes, particularly preferably hydrolases, in particular proteases, particularly preferably endo-peptidases, in particular proteases of the subtilisin type, or parts thereof.
  • the polypeptides according to the invention are therefore preferably able to hydrolyze acid amide bonds of proteins, in particular those which are located inside the proteins.
  • the parts of the polypeptides may, in particular, be protein domains which may be suitable, for example, for the formation of functional chimeric enzymes.
  • proteases which can be used in particular in detergents, it can serve as a naturally occurring, microbially formed enzyme as a starting point for mutagenesis methods known per se, for example point mutagenesis, fragmentation, deletion, insertion or fusion with other proteins or protein parts or Other modifications for the desired use to be optimized.
  • Such optimizations can be, for example, adjustments to temperature influences, pH fluctuations, redox ratios and / or other influences that are relevant for the technical fields of application. For example, an improvement in oxidation resistance, stability to denaturing agents or proteolytic degradation, high temperatures, acidic or strongly alkaline conditions, a change in sensitivity to calcium ions or other cofactors, a reduction in immunogenicity or allergenic activity are desired.
  • the surface charges or the loops involved in the catalysis or substrate binding can be changed.
  • One starting point for this is an alignment with known proteases. This makes it possible to locate positions which, if necessary, could lead to an improvement in the properties of the protein.
  • mutagenesis methods are based on the associated nucleotide sequence shown in SEQ ID NO. 1, or for this purpose sufficiently similar nucleotide sequences, the further below be presented as a separate subject of the invention.
  • Corresponding molecular biology methods are described in the prior art, for example in manuals such as those of Fritsch, Sambrook and Maniatis "Molecular cloning: a laboratory manual", CoId Spring Harbor Laboratory Press, New York, 1989.
  • polypeptides according to the invention are those protein variants which have one or more amino acid exchanges in the positions 3, 4, 36, 42, 47, 56, 61, 69, 87, 96, 99, 101, 102, 104, 114, 118, 120, 130, 139, 141, 142, 154, 157, 188, 193, 199, 205, 211, 224, 229, 236, 237, 242, 243, 255 and 268 in the count of the alkaline Protease from Bacillus lentus.
  • Chimeric proteins according to the invention have in the broadest sense a proteolytic activity. This may be exercised or modified by a moiety derived from a polypeptide of the invention.
  • the chimeric proteins can therefore also lie outside the range claimed above over their entire length.
  • the purpose of such a fusion is to introduce or modify a particular function or partial function using the fused protein portion of the invention.
  • it is irrelevant whether such a chimeric protein consists of a single polypeptide chain or several subunits.
  • a polypeptide according to the invention or parts thereof via peptidic linkers or directly as a fusion protein with binding domains from other proteins, for example the cellulose-binding domain, thereby making the hydrolysis of the substrate more effective.
  • binding domain could also be derived from a protease, such as to enhance the binding of the protein of the invention to a protease substrate. This increases the local protease concentration, which may be advantageous in individual applications, for example in the treatment of raw materials.
  • proteins according to the invention can also be linked with amylases or cellulases, for example, in order to perform a dual function.
  • polypeptides according to the invention obtainable by insertion mutation are to be assigned to their basic similarity because of the chimeric proteins according to the invention.
  • This subheading also includes substitution variants, ie those in which individual regions of the molecule have been replaced by elements from other proteins.
  • the purpose of insertion and suppression mechanisms is to combine individual properties, functions or partial functions of proteins according to the invention with those of other proteins.
  • This also includes, for example, variants to be obtained via shuffling or recombination of partial sequences from different proteases.
  • proteins can be obtained which have not previously been described. Such techniques allow drastic effects to very subtle activity modulations.
  • such mutations are random priming recombinations according to a statistical method attributable to the Directed Evolution field, such as StEP (Zhao et al., 1998, Nat. Biotechnol., Vol. 16, pp. 258-261) (Shao et al., (1998) Nucleic Acids Res., Vol. 26, pp. 681-683), DNA shuffling (Stemmer, WP, C. (1994), Nature, Vol. 370, pp. 389-391) or recursive sequence recombination (RSR; 27230, WO 97/20078, WO 95/22625) or the method RACHITT (Coco, WM et al. (2001), Nat.
  • Inversion mutagenesis ie a partial sequence reversal, can be regarded as a special form of both the deletion and the insertion. Such variants can also be generated purposefully or randomly.
  • subtilisins are preferred.
  • endopeptidases especially of the groups 3.4.21 serine proteinases, 3.4.22 cysteine proteinases, 3.4.23 aspartate proteinases and 3.4.24 metalloproteinases.
  • serine proteinases 3.4.21
  • subtilisins see “Subtilases: Subtilisin-like Proteases” by R. Siezen, pages 75-95 in “Subtilisin enzymes", issued by R. Bott and C. Betzel, New York, 1996).
  • subtilisins of group IS-2 the highly alkaline subtilisins, are preferred.
  • active molecules are preferred to inactive ones, since, for example, the proteolysis carried out is of importance, for example, in the fields of application set out below.
  • the above-mentioned fragments also have a proteolytic activity in the broadest sense, for example for complexing a substrate or for forming a structural element required for the hydrolysis. They are preferred if, taken alone, they can already be used for the hydrolysis of another protein without the need for further protease components to be present. This refers to the activity that can be exerted by a protease per se; the possibly simultaneously necessary presence of buffer substances, cofactors etc. remains unaffected.
  • deletion variants proteins of the invention, as in the case of the fusion proteins.
  • Preferred representatives of this subject invention include those which per se are capable of hydrolyzing a protein substrate without the need for further protease components to be present.
  • a preferred embodiment are all such polypeptides according to the invention carried out so far, which are characterized in that they are additionally stabilized.
  • proteases according to the invention can be increased, for example, by coupling to polymers. It requires that the proteins be linked to such polymers via a chemical coupling step prior to their use in appropriate agents.
  • Another way to stabilize against elevated temperature and the action of surfactants would be the stabilization via the exchange of amino acids that are close to the N-terminus, against those that come into contact with the rest of the molecule via non-covalent interactions and thus a Contribute to the maintenance of the globular structure.
  • a preferred embodiment are all such polypeptides according to the invention carried out so far, which are characterized in that they are additionally derivatized.
  • Derivatives are understood as meaning proteins which are derived from the exported proteins by an additional modification. Such modifications may include, for example, stability, substrate specificity or binding strength to the substrate or enzymatic activity influence. They can also serve to reduce the allergenicity and / or immunogenicity of the protein and thus, for example, increase its skin compatibility.
  • Such derivatizations can be carried out, for example, biologically, for example in connection with the protein biosynthesis by the producing host organism.
  • Particularly noteworthy here are couplings of low-molecular compounds such as lipids or oligosaccharides.
  • derivatizations can also be carried out chemically, for example by the chemical transformation of a side chain or by covalent bonding of another, for example macromolecular, compound to the protein.
  • another, for example macromolecular, compound for example, such a coupling of amines to carboxyl groups of the enzyme to change the isoelectric point done.
  • macromolecules such as proteins, for example via bifunctional chemical compounds, can be bound to proteins according to the invention. Such a macromolecule may be a binding domain, for example.
  • Such derivatives are particularly suitable for use in detergents or cleaners.
  • protease inhibitors can also be linked to the proteins according to the invention via linkers, in particular amino acid linkers. Couplings with other macromolecular compounds such as polyethylene glycol improve the molecule for other properties such as stability or skin compatibility.
  • Derivatives of proteins according to the invention can in the broadest sense also be understood to mean preparations of these enzymes.
  • a protein may be associated with various other substances, for example from the culture of the producing microorganisms.
  • a protein may also have been deliberately added to certain other substances, for example to increase its storage stability. Therefore, all preparations of a protein according to the invention are also according to the invention. This is also independent of whether or not it actually exhibits this enzymatic activity in a particular preparation. Because it may be desired that it has no or only low activity during storage, and unfolds its proteolytic function only at the time of use. This can be controlled, for example, via appropriate accompanying substances such as protease inhibitors.
  • a preferred embodiment is any of those proteins, protein fragments, fusion proteins or derivatives characterized by having at least one antigenic determinant in common with one of the polypeptides of the invention described above.
  • a preferred embodiment are all such polypeptides according to the invention which have hitherto been carried out and which are characterized in that they are obtainable from a natural source, in particular from a microorganism.
  • These may be, for example, unicellular fungi or bacteria. Because they are usually easier to win and handle as multicellular organisms or cell cultures derived from multicellular organisms; although these may represent useful options for specific embodiments and thus are not excluded in principle from the subject invention.
  • Particularly preferred among these are those from gram-positive bacteria. Because they have no outer membrane and thus release secreted proteins directly into the surrounding medium.
  • Very particularly preferred are those from gram-positive bacteria of the genus Bacillus.
  • Bacillus proteases have from the outset favorable properties for various technical applications. These include some stability to elevated temperature, oxidizing or denaturing agents.
  • microbial proteases have the greatest experience in terms of their biotechnological production, for example the construction of favorable cloning vectors, the selection of host cells and growth conditions or the estimation of risks, such as allergenicity.
  • Bacilli are also established as production organisms with a particularly high production output in technical processes. The wealth of experience that has been acquired for the production and use of these proteases also benefits further developments of these enzymes according to the invention. This concerns, for example, their compatibility with other chemical compounds, such as the ingredients of detergents or cleaners.
  • Bacillus gibsonii in particular from the strain of Bacillus gibsonii used according to the invention, are preferred.
  • the embodiment of the enzyme according to the invention was originally obtained. Its associated sequences are given in the Sequence Listing. From this or related strains, the variants described above can be prepared in particular using standard molecular biological methods, such as PCR and / or per se known point mutagenesis method.
  • a further solution of the problem and thus a separate subject of the invention are the nucleic acids which serve to realize the invention.
  • a person skilled in the art will be able to prepare complete genes by known DNA and / or amino acid sequences via methods that are generally known today, such as, for example, chemical synthesis or the polymerase chain reaction (PCR) in conjunction with molecular biological and / or proteinchemical standard methods.
  • PCR polymerase chain reaction
  • Such methods are known for example from the "Encyclopaedia of Biochemistry", Spektrum Akademischer Verlag, Berlin, 1999, Volume 1, pp. 267-271 and Volume 2, pp. 227-229. This is possible in particular if it is possible to fall back on a strain deposited in a master collection.
  • PCR primers which can be synthesized by means of a known sequence and / or isolated mRNA molecules, the relevant genes can be synthesized from such strains, cloned and, if desired, further processed, for example mutagenized.
  • Nucleic acids form the starting point of almost all molecular biological investigations and further developments as well as the production of proteins. These include, in particular, the sequencing of the genes and the derivation of the associated amino acid sequence, any type of mutagenesis (see above) and the expression of the proteins.
  • Mutagenesis for the development of proteins with specific properties is also referred to as "protein engineering”. Properties to be optimized have already been exemplified above. Such mutagenesis may be targeted or by random methods, for example, with subsequent activity-directed recognition and / or selection (screening and selection) on the cloned genes, such as hybridization with nucleic acid probes, or on the gene products, the proteins, be done about their activity.
  • the further development of the proteases according to the invention can also be carried out in particular in the "Protein engineering” publication by PNBryan (2000) in Biochim. Biophys. Ada, vol. 1543, pp. 203-222, are presented.
  • Another object of the present invention are therefore also polynucleotides encoding polypeptides according to the invention, in particular hydrolases, especially subtilisin-type alkaline proteases.
  • the present invention therefore relates in particular to polynucleotides selected from the group consisting of: a) polynucleotide having a nucleic acid sequence according to SEQ ID NO: 1, b) polynucleotide having a nucleic acid sequence from position 1 to 342 according to SEQ ID NO: 1, c) polynucleotide with a nucleic acid sequence from position 1 to 81 according to SEQ ID NO: 1, d) polynucleotide having a nucleic acid sequence from position 82 to 342 according to SEQ ID NO: 1, e) polynucleotide having a nucleic acid sequence from position 343 to 1152 according to SEQ ID NO: 1, f) polynucleotide encoding a polypeptide having an amino acid sequence according to
  • polynucleotide according to (b) or (d) with up to 25, preferably up to 22, 20, 18, 16 or 15, particularly preferably up to 14, 13, 12, 11 or 10, especially up to 9, 8, 7, 6, 5, 4, 3 or 2 mutations, most preferably with exactly one mutation, m) polynucleotides having a sequence homology or identity of at least 90%, preferably at least 91, 92, 93, 94 or 95%, more preferably at least 96, 97, 98 or 99%, with respect to a polynucleotide according to (a) or (e), n) polynucleotides having a sequence homology or identity of at least 93 %, preferably at least 94, 95 or 96%, particularly preferably at least 97, 98 or 99%, with respect to a polynucleotide according to (d), o) under stringent conditions with a polynucleotide according to (d), o) under stringent conditions with a polynucleotide according to
  • the polynucleotides may be present as a single strand or as a double strand.
  • Subject matter of the invention are, besides the deoxyribonucleic acids, also the homologous and complementary ribonucleic acids.
  • the present invention also relates, in particular, to those polynucleotides in which certain regions have been replaced by other regions, taking account of the differing codon usage of a host organism used for the expression, in order to enable the expression of the polypeptide according to the invention.
  • nucleic acids according to the invention described above are increasingly preferred among the nucleic acids according to the invention described above:
  • microorganism is a Gram-positive bacterium
  • Gram-positive bacterium is one of the genus Bacillus
  • Bacillus species Bacillus gibsonii in particular the strain used in the invention.
  • a separate subject of the invention are vectors which contain one of the previously described nucleic acid regions according to the invention, in particular one which codes for one of the polypeptides according to the invention designated above.
  • vectors are in great numbers and variation, both for the Cloning and for expression commercially available. These include, for example, vectors derived from bacterial plasmids, bacteriophages or viruses, or predominantly synthetic vectors. Furthermore, they are differentiated according to the type of cell types in which they are able to establish themselves, for example vectors for gram-negative, gram-positive bacteria, yeast or higher eukaryotes. They form suitable starting points for example for molecular biological and biochemical investigations and for the expression of the relevant gene or associated protein.
  • vectors of the invention are cloning vectors.
  • cloning vectors are suitable in addition to the storage, the biological amplification or the selection of the gene of interest for its molecular biological characterization. At the same time they represent transportable and storable forms of the claimed nucleic acids and are also starting points for molecular biological techniques that are not bound to cells, such as the PCR or / n-wfro mutagenesis method.
  • vectors according to the invention are expression vectors.
  • expression vectors are the basis for realizing the corresponding nucleic acids in biological production systems and thus to produce the associated proteins.
  • Preferred embodiments of this subject matter of the invention are expression vectors carrying genetic elements necessary for expression, for example the natural promoter originally located in front of this gene or a promoter from another organism. These elements can be arranged for example in the form of a so-called expression cassette. Alternatively, individual or all regulatory elements may also be provided by the respective host cell. With particular preference, the expression vectors are matched to the selected expression system, in particular the host cell (see below), with regard to further properties, for example the optimal copy number.
  • the expression vector contains as far as possible only the relevant gene as an insert and no larger 5 'or 3' noncoding regions.
  • Such inserts are obtained, for example, when the fragment obtained after statistical treatment of the chromosomal DNA of the starting strain with a restriction enzyme has been cut again after sequencing before integration into the expression vector.
  • An example of an expression vector is the vector pAWA22.
  • Other vectors are available to those skilled in the art and are commercially available in large numbers.
  • a separate subject of the invention are cells which contain a polynucleotide according to the invention after genetic engineering modification.
  • these cells contain the genetic information for the synthesis of a protein according to the invention.
  • these are to be understood as meaning those cells which have been provided with the nucleic acids according to the invention by methods known per se or which are derived from such cells.
  • suitable suitable host cells are those which can be cultivated relatively easily and / or yield high product yields.
  • This genetic information can either be extrachromosomally as a separate genetic element, ie be present in bacteria in plasmidaler localization or integrated into a chromosome.
  • the choice of a suitable system depends on issues such as the nature and duration of storage of the gene, or the organism or the type of mutagenesis or selection. For example, based on bacteriophages - and their specific host cells - the prior art described mutagenesis and selection processes for the development of detergent enzymes.
  • the polynucleotide according to the invention is preferably part of one of the above-described vectors according to the invention, in particular of a cloning or expression vector.
  • those cells are preferred which express a polypeptide of the invention and preferably secrete.
  • host cells that make up the proteins enable their biotechnological production.
  • all organisms that is prokaryotes, eukaryotes or cyanophyta, are suitable as host cells for protein expression.
  • host cells which can be genetically well handled, for example, the transformation with the expression vector, its stable establishment and the regulation of expression, for example, unicellular fungi or bacteria.
  • preferred host cells are characterized by good microbiological and biotechnological handling. This concerns, for example, easy culturing, high growth rates, low demands on fermentation media and good production and Secretion rates for foreign proteins.
  • laboratory strains are selected which are aligned to the expression. Such are available commercially or via publicly available strain collections.
  • Each protein of the invention can thus be theoretically obtained from a variety of host organisms. From the abundance of various systems available in the prior art, the optimal expression systems for the individual case must be determined experimentally.
  • host cells which are themselves protease-negative and thus do not degrade proteins formed.
  • Preferred embodiments are those host cells which are regulatable in activity by virtue of corresponding genetic elements, for example by controlled addition of chemical compounds, by changing the culture conditions or depending on the respective cell density.
  • This controllable expression allows very economical production of the proteins of interest; It can be realized, for example, via a corresponding element on the relevant vector.
  • the gene, expression vector and host cell are matched to one another, which relates, for example, to the genetic elements required for expression (ribosome binding site, promoters, terminators) or the codon usage.
  • host cells which are bacteria.
  • bacteria are characterized by short generation times and low demands on the cultivation conditions. As a result, inexpensive methods can be established. In addition, bacteria have a wealth of experience in fermentation technology. For a specific production gram-negative or gram-positive bacteria may be suitable for a variety of reasons to be determined experimentally in individual cases, such as nutrient sources, product formation rate, time requirement, etc.
  • it is a gram-negative bacterium, in particular one of the genera Escherichia coli or Klebsiella, in particular strains of E. coli K12, E. coli B or Klebsiella planticola, and more particularly derivatives of the strains Escherichia coli BL21 (DE3 ) E. coli RV308, E. coli DH5 ⁇ , E. coli JM109, E coli XL-1 or Klebsiella planticola (Rf).
  • Gram-negative bacteria such as E. coli
  • a variety of proteins are secreted into the periplasmic space. This can be advantageous for special applications.
  • WO 01/81597 A1 discloses a method according to which it is achieved that gram-negative bacteria also eject the expressed proteins. Such a system is also suitable for the production of proteins according to the invention.
  • the Gram-negative bacteria which are mentioned as preferred are generally light, that is to say commercially or accessible via public strain collections and, in conjunction with other components which are likewise available in large numbers, such as vectors, can be optimized for specific production conditions.
  • it is a Gram-positive bacterium, in particular one of the genera Bacillus, Staphylococcus or Corynebacteria, more particularly of the species Bacillus lentus, B. licheniformis, B. amyloliquefaciens, B. subtilis, B. globigii, B gibsonii, B. pumilus or ß. alcalophilus, Staphylococcus carnosus or Corynebacterium glutamicum.
  • gram-positive bacteria have the gram-negative compared to the fundamental difference, secreted proteins readily deliver into the nutrient medium surrounding the cells, from which, if desired, the expressed proteins according to the invention can be purified directly from the nutrient medium.
  • they are related or identical to most of the organisms of origin for technically important subtilisins and usually form even comparable subtilisins, so that they have a similar codon Usage and their protein synthesizer is naturally aligned accordingly.
  • a further advantage may be that a mixture of proteins according to the invention with the subtilisins formed endogenously by the host strains can be obtained by this process. Such a co-expression is also apparent from the application WO 91/02792. Should it not be desired, the protease genes naturally present in the host cell would have to be permanently or temporarily inactivated.
  • host cells which are eukaryotic cells, preferably of the genus Saccharomyces.
  • fungi such as Actinomycetes or even yeasts such as Saccharomyces or Kluyveromyces.
  • Thermophilic fungal expression systems are presented, for example, in WO 96/02653 A1. Such are particularly suitable for the expression of temperature-resistant variants.
  • Modifications that eukaryotic systems perform, especially in connection with protein synthesis include, for example, the binding of low molecular weight compounds such as membrane anchors or oligosaccharides. Such oligosaccharide modifications may be desirable, for example, to reduce allergenicity.
  • coexpression with the enzymes naturally produced by such cells, such as cellulases may be advantageous.
  • An independent subject of the invention are processes for the preparation of a polypeptide according to the invention. This includes any method for producing a polypeptide of the invention described above, for example, chemical synthesis methods.
  • Embodiments of the present invention may also be cell-free expression systems in which protein biosynthesis is understood in vitro. All of the elements already described above can also be combined to form new methods for producing proteins according to the invention. It is conceivable for each protein according to the invention a variety of possible combinations of process steps, so that optimal procedures must be determined experimentally for each specific case.
  • nucleotide sequence has been adapted in one, preferably a plurality of codons to the codon usage of the host strain.
  • a separate subject of the invention are agents which contain the abovementioned polypeptides according to the invention.
  • compositions especially mixtures, formulations, solutions, etc., the utility of which is improved by addition of a protein of the invention described above, within the scope of the present invention.
  • these may be, for example, solid mixtures, for example powders with freeze-dried or encapsulated proteins, or gel or liquid agents.
  • Preferred formulations contain, for example, buffer substances, stabilizers, reaction partners and / or cofactors of the proteases and / or other ingredients synergistic with the proteases.
  • this appropriation is to be understood as the areas of application set out below. Further fields of application emerge from the prior art and are described, for example, in US Pat Handbook "Industrial Enzymes and their Applications" by H. UhNg, Wiley-Verlag, New York, 1998.
  • Possible fields of use here are, in particular, the use for obtaining or treating raw materials or intermediates in textile production, in particular for removing protective layers on fabrics, in particular wool or silk, and the use for the care of textiles, the natural fibers, in particular wool or silk, contain.
  • natural fibers such as wool or silk
  • the natural raw materials are treated with agents according to the invention which, for example, help to smooth the shingled surface structure based on protein structures and thus counteract entanglement.
  • the invention also relates to processes for the treatment of textile raw materials and for textile care, in which polypeptides according to the invention are used in at least one of the process steps.
  • processes for textile raw materials, fibers or textiles with natural constituents, in particular those with wool or silk may be, for example, processes in which materials for processing in textiles are prepared, for example for anti-fungal finishing, or, for example, for processes which enrich the cleaning of worn textiles with a nourishing component.
  • Another use according to the invention is the use of the polypeptides according to the invention in cosmetic agents.
  • This is understood to mean all types of cleansing and conditioning agents for human skin or hair, in particular cleansing agents.
  • the agent may also be a pharmaceutical agent depending on the purpose of use.
  • proteases also play a crucial role in the cell renewal process of the human skin (desquamation) (T. Egelrud et al., Acta Derm. Venera /, Volume 71 (1991), pp. 471-474). Accordingly, proteases are also used as bioactive components in skin care agents to aid in the breakdown of desmosome structures that are increased in dry skin.
  • the use of subtilisin proteases with amino acid substitutions in the positions R99G / A / S, S154D / E and / or L211 D / E for cosmetic purposes is described, for example, in WO 97/07770 A1.
  • proteases according to the invention can be further developed via the corresponding point mutations.
  • proteases according to the invention in particular those which are controlled in their activity, for example after mutagenesis or by addition of corresponding substances interacting with them, are also suitable as active components in skin or hair cleansing or care preparations.
  • compositions according to the invention are shampoos, soaps, washing lotions, creams, peels and oral, dental or denture care agents mentioned.
  • these compositions may also contain constituents, as mentioned below for detergents and cleaners.
  • proteolytic enzymes for cosmetic purposes are also included in this subject matter, in particular in appropriate agents, such as shampoos, soaps or washing lotions, or in care products that are offered, for example in the form of creams. Also, the use in a peeling drug, or the use for its production is included in this article.
  • a particularly preferred subject according to the invention are detergents and cleaners containing polypeptides according to the invention. Because as in the embodiments of In the case of detergents and cleaners containing a protease which is preferred according to the invention, surprisingly, an increase in the washing power compared to agents with conventionally employed proteases could be ascertained.
  • the washing performance or the cleaning performance of a washing or cleaning agent is to be understood as meaning the effect which the agent in question has on the soiled articles, for example textiles or objects with hard surfaces.
  • Individual components of such agents, in particular the enzymes according to the invention are assessed with regard to their contribution to the washing or cleaning performance of the entire detergent or cleaning agent. It should be noted in particular that from the enzymatic properties of an enzyme can not be readily deduced to its contribution to the washing performance of an agent. Rather, in addition to the enzymatic activity, factors such as stability, substrate binding, binding to the items to be cleaned or interactions with other ingredients of the detergents or cleaning agents, in particular possible synergy effects in the removal of the contaminants, also play a role here.
  • Another object of the present invention are therefore detergents and cleaning agents, in particular surfactant and / or bleach-containing, containing a polypeptide of the invention.
  • the detergents and cleaning agents according to the invention may be any conceivable type of cleaning agent, both concentrates and agents to be used undiluted, for use on a commercial scale, in the washing machine or in hand washing or cleaning.
  • These include, for example, detergents for textiles, carpets, or natural fibers, for which according to the present invention the term laundry detergent is used.
  • laundry detergent includes, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather; for such according to the present invention, the term cleaning agent is used.
  • sterilizing and disinfecting agents are to be regarded as detergents and cleaners in the sense of the invention.
  • Embodiments of the present invention include all of the prior art and / or all suitable administration forms of the washing or cleaning agents according to the invention. These include, for example, solid, powdery, liquid, gelatinous or pasty agents, optionally also of several phases, compressed or uncompressed; further include, for example: extrudates, granules, tablets or pouches, packed both in large containers and in portions.
  • the detergents or cleaners according to the invention contain the above-described polypeptides according to the invention, in particular alkaline subtilisin-type proteases, in an amount of from 2 ⁇ g to 20 mg, preferably from 5 ⁇ g to 17.5 mg, particularly preferably 20 ⁇ g to 15 mg, most preferably from 50 ⁇ g to 10 mg per gram of the agent. Included are all integer and non-integer values lying between these numbers.
  • protease activity in such agents can be determined by the method described in Tenside, Vol. 7 (1970), pp. 125-132. It is accordingly stated in PE (protease units).
  • a washing or cleaning agent according to the invention optionally contains further ingredients such as further enzymes, enzyme stabilizers, surfactants, for.
  • further ingredients such as further enzymes, enzyme stabilizers, surfactants, for.
  • surfactants for.
  • the nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular primary, alcohols having preferably 8 to 18 carbon atoms and on average 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical is linear or preferably methyl-branched in the 2-position can, or may contain linear and methyl-branched radicals in the mixture, as they are usually present in Oxoalkoholresten.
  • alcohol ethoxylates with linear radicals of alcohols of native origin having 12 to 18 carbon atoms, for example of coconut, palm, tallow or oleyl alcohol, and on average 2 to 8 EO per mole of alcohol are preferred.
  • Preferred ethoxylated alcohols include, for example, C 2 - 14 alcohols with 3 EO or 4 EO, C 9 n-alcohol with 7 EO, C-ms alcohols containing 3 EO, 5 EO, 7 EO or 8 EO, C 12 -i 8 -alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C 12 -i 4 -alcohol with 3 EO and C 12 -i 8 -alcohol with 5 EO.
  • the specified degrees of ethoxylation represent statistical averages that can be a whole or a fractional number for a particular product.
  • Preferred alcohol ethoxylates have a narrow homolog distribution (narrow rank ethoxylates, NRE).
  • NRE narrow rank ethoxylates
  • fatty alcohols with more than 12 EO can also be used. Examples of these are tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO.
  • nonionic surfactants used either as the sole nonionic surfactant or in combination with other nonionic surfactants are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably having from 1 to 4 carbon atoms in the alkyl chain, especially fatty acid methyl esters.
  • alkyl polyglycosides Another class of nonionic surfactants that can be used to advantage are the alkyl polyglycosides (APG).
  • APG alkyl polyglycosides
  • Usable Alkypolyglycoside meet the general formula RO (G) Z , in which R is a linear or branched, especially in the 2-position methyl-branched, saturated or unsaturated, aliphatic radical having 8 to 22, preferably 12 to 18 carbon atoms and G is the symbol which is a glycose unit having 5 or 6 C atoms, preferably glucose.
  • the degree of glycosylation z is between 1, 0 and 4.0, preferably between 1, 0 and 2.0 and in particular between 1, 1 and 1, 4.
  • Preference is given to using linear alkyl polyglucosides that is to say alkyl polyglycosides in which the polyglycosyl radical is a glucose radical and the alkyl radical is an n-alkyl radical.
  • Nonionic surfactants of the amine oxide type for example N-cocoalkyl N, N-dimethylamine oxide and N-tallow alkyl N, N-dihydroxyethyl amine oxide, and the fatty acid alkanolamides may also be suitable.
  • the proportion of these nonionic surfactants is preferably not higher than that of the ethoxylated fatty alcohols, especially not more than half of them.
  • surfactants are polyhydroxy fatty acid amides of the formula (I)
  • RCO is an aliphatic acyl radical having 6 to 22 carbon atoms
  • R ⁇ is hydrogen
  • [Z] is a linear or branched polyhydroxyalkyl radical having 3 to 10 carbon atoms and 3 to 10 hydroxyl groups.
  • the polyhydroxy fatty acid amides are known substances which can usually be obtained by reductive amination of a reducing sugar with ammonia, an alkylamine or an alkanolamine and subsequent acylation with a fatty acid, a fatty acid alkyl ester or a fatty acid chloride.
  • the group of polyhydroxy fatty acid amides also includes compounds of the formula (II) R 1 -OR 2 R-CO-N- [Z] (II)
  • R is a linear or branched alkyl or alkenyl radical having 7 to 12 carbon atoms
  • R 1 is a linear, branched or cyclic alkyl radical or an aryl radical having 2 to 8 carbon atoms
  • R 2 is a linear, branched or cyclic alkyl radical or an aryl radical or an oxy-alkyl radical having 1 to 8 carbon atoms
  • Ci_ 4 alkyl or phenyl radicals are preferred
  • [Z] is a linear polyhydroxyalkyl radical whose alkyl chain is substituted with at least two hydroxyl groups, or alkoxylated, preferably ethoxylated or propoxylated derivatives thereof residue.
  • [Z] is preferably obtained by reductive amination of a reducing sugar, for example glucose, fructose, maltose, lactose, galactose, mannose or xylose.
  • a reducing sugar for example glucose, fructose, maltose, lactose, galactose, mannose or xylose.
  • the N-alkoxy- or N-aryloxy-substituted compounds can be converted into the desired polyhydroxy fatty acid amides, for example, by reaction with fatty acid methyl esters in the presence of an alkoxide as catalyst.
  • anionic surfactants for example, those of the sulfonate type and sulfates are used.
  • surfactants of the sulfonate type are preferably C 9 - 13 alkylbenzenesulfonates, olefin sulfonates, that is, mixtures of alkene and hydroxyalkanesulfonates and disulfonates, as they are for example from C
  • alkanesulfonates from C 2 - 18 are obtained, for example, alkanes by sulfochlorination or sulfoxidation and subsequent hydrolysis or neutralization.
  • the esters of CC are preferably C 9 - 13 alkylbenzenesulfonates, olefin sulfonates, that is, mixtures
  • Sulfo fatty acids for example the CC-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.
  • sulfated fatty acid glycerol esters are to be understood as meaning the mono-, di- and triesters and mixtures thereof, as obtained in the preparation by esterification of a monoglycerol with 1 to 3 moles of fatty acid or in the transesterification of triglycerides with 0.3 to 2 moles of glycerol.
  • Preferred sulfated fatty acid glycerol esters are the sulfonation products of saturated fatty acids having 6 to 22 carbon atoms, for example caproic acid, caprylic acid, capric acid, myristic acid, lauric acid, palmitic acid, stearic acid or behenic acid.
  • Alk (en) yl sulfates are the alkali and especially the sodium salts of the Schwefelhoffreraumester C 2 -C 8 fatty alcohols, for example coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol, or d 0 -C 2 o Oxo alcohols and those half esters secondary alcohols of these chain lengths are preferred. Also preferred are alk (en) ylsulfates of said chain length, which contain a synthetic, produced on a petrochemical basis straight-chain alkyl radical, which have an analogous degradation behavior as the adequate compounds based on oleochemical raw materials.
  • Ci 2 -Ci 6 alkyl sulfates and Ci 2 -Ci 5 alkyl sulfates and Ci 4 -Ci 5 alkyl sulfates are preferred.
  • 2,3-alkyl sulfates are also suitable anionic surfactants.
  • the sulfuric acid monoesters of straight-chain or branched C 7 ethoxylated with 1 to 6 moles of ethylene oxide are suitable.
  • 2 i-alcohols such as 2-methyl-branched Cg-n-alcohols having on average 3.5 mol of ethylene oxide (EO) or C 12 -i 8 -fatty alcohols having 1 to 4 EO, are suitable. Due to their high foaming behavior, they are only used in detergents in relatively small amounts, for example in amounts of up to 5% by weight, usually from 1 to 5% by weight.
  • Suitable anionic surfactants are also the salts of alkylsulfosuccinic acid, which are also referred to as sulfosuccinates or as sulfosuccinic acid esters and the monoesters and / or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols and in particular ethoxylated fatty alcohols.
  • alcohols preferably fatty alcohols and in particular ethoxylated fatty alcohols.
  • Preferred sulfosuccinates contain C 8 -i 8 -fatty alcohol residues or mixtures of these.
  • Particularly preferred sulfosuccinates contain a fatty alcohol radical which is derived from ethoxylated fatty alcohols, which in themselves constitute nonionic surfactants (description see above).
  • Sulfosuccinates whose fatty alcohol residues are derived from ethoxylated fatty alcohols with a narrow homolog distribution, are again particularly preferred.
  • alk (en) ylsuccinic acid having preferably 8 to 18 carbon atoms in the alk (en) yl chain or salts thereof.
  • anionic surfactants are particularly soaps into consideration.
  • Suitable are saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid and behenic acid and, in particular, soap mixtures derived from natural fatty acids, for example coconut, palm kernel or tallow fatty acids.
  • the anionic surfactants may be in the form of their sodium, potassium or ammonium salts and as soluble salts of organic bases, such as mono-, di- or triethanolamine.
  • the anionic surfactants are preferably present in the form of their sodium or potassium salts, in particular in the form of the sodium salts.
  • the surfactants may be contained in the detergents or detergents according to the invention overall in an amount of preferably from 5% by weight to 50% by weight, in particular from 8% by weight to 30% by weight, based on the finished composition ,
  • Detergents or cleaners according to the invention may contain bleaches.
  • bleaches include the compounds which serve as bleaches and deliver H 2 O 2 in water, the sodium percarbonate, the sodium perborate tetrahydrate and the sodium perborate monohydrate are of particular importance.
  • Other useful bleaching agents are, for example, peroxopyrophosphates, citrate perhydrates and H 2 O 2 -producing peracidic salts or peracids, such as persulfates or persulfuric acid.
  • the urea peroxohydrate percarbamide represented by the formula H 2 N-CO-NH 2 2 O 2 can be described H.
  • the means for cleaning hard surfaces for example in automatic dishwashing, they may, if desired, also contain bleaching agents from the group of organic bleaches, although their use is also possible in principle for laundry detergents.
  • Typical organic bleaches are the diacyl peroxides, such as dibenzoyl peroxide.
  • Other typical organic bleaches are the peroxyacids, examples of which include the alkyl peroxyacids and the aryl peroxyacids.
  • Preferred representatives are the peroxybenzoic acid and its ring-substituted derivatives, such as alkylperoxybenzoic acids, but also peroxy- ⁇ -naphthoic acid and magnesium monoperphthalate, the aliphatic or substituted aliphatic peroxyacids, such as peroxylauric acid, peroxystearic acid, ⁇ -phthalimidoperoxycaproic acid (Phthalimidoperoxyhexanoic acid, PAP), o-carboxybenzamidoperoxycaproic acid, N-nonenylamidoperadipic acid and N-nonylamidopersuccinates, and aliphatic and araliphatic peroxydicarboxylic acids, such as 1, 12-diperoxycarboxylic acid, 1, 9-diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassic acid, the diperoxyphthalic acids, 2-decyldiperoxybutane-1,4-d
  • the content of bleach detergent or cleaning agent may be from 1 to 40% by weight and in particular from 10 to 20% by weight, with perborate monohydrate or percarbonate being advantageously used.
  • the agents may also contain bleach activators.
  • bleach activators it is possible to use compounds which, under perhydrolysis conditions, give aliphatic peroxycarboxylic acids having preferably 1 to 10 C atoms, in particular 2 to 4 C atoms, and / or optionally substituted perbenzoic acid. Suitable substances are those which carry O- and / or N-acyl groups of the stated C atom number and / or optionally substituted benzoyl groups.
  • polyacylated alkylenediamines in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular 1, 3,4,6 Tetraacetylglycoluril (TAGU), N-acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates, in particular n-nonanoyl or isononanoyloxybenzenesulfonate (n- or iso-NOBS), acylated hydroxycarboxylic acids, such as triethyl-O-acetylcitrate (TEOC), Carboxylic acid anhydrides, in particular phthalic anhydride, isatoic anhydride and / or succinic
  • hydrophilic substituted acyl acetals known from the German patent application DE 196 16 769 and the acyllactams described in the German patent application DE 196 16 770 and the international patent application WO 95/14075 are also preferably used.
  • the combinations of conventional bleach activators known from German patent application DE 44 43 177 can also be used.
  • nitrile derivatives such as cyanopyridines, nitrile quats, for example N-alkylammonium acetonitriles, and / or cyanamide derivatives can be used.
  • Preferred bleach activators are sodium 4- (octanoyloxy) benzenesulfonate, n-nonanoyl or isononanoyloxybenzenesulfonate (n- or iso-NOBS), undecenoyloxybenzenesulfonate (UDOBS), sodium dodecanoyloxybenzenesulfonate (DOBS), decanoyloxybenzoic acid (DOBA, OBC 10) and / or Dodecanoyloxybenzenesulfonate (OBS 12), as well as N-methylmorpholinum acetonitrile (MMA).
  • Such bleach activators can be used in the customary amount range of from 0.01 to 20% by weight, preferably in amounts of from 0.1 to 15% by weight, in particular from 1% to 10% by weight, based on the total composition, be included.
  • bleach catalysts may also be included.
  • These substances are bleach-enhancing transition metal salts or transition metal complexes such as Mn, Fe, Co, Ru or Mo-salene complexes or carbonyl complexes.
  • Mn, Fe, Co, Ru, Mo, Ti, V and Cu complexes with N-containing tripod ligands and also Co, Fe, Cu and Ru ammine complexes are suitable as bleach catalysts, wherein such compounds are preferably used, which are described in DE 19709284 A1.
  • Detergents or cleaners according to the invention generally comprise one or more builders, in particular zeolites, silicates, carbonates, organic cobuilders and, where there are no ecological reasons against their use, also the phosphates.
  • builders in particular zeolites, silicates, carbonates, organic cobuilders and, where there are no ecological reasons against their use, also the phosphates.
  • the latter are particularly preferred builders to be used in automatic dishwashing detergents.
  • crystalline, layered sodium silicates of the general formula NaMSi x O 2x + I yH 2 O, where M is sodium or hydrogen, x is a number from 1, 6 to 4, preferably 1, 9 to 4.0 and y is a number from 0 to 20 and preferred values for x are 2, 3 or 4.
  • M sodium or hydrogen
  • x is a number from 1, 6 to 4, preferably 1, 9 to 4.0
  • y is a number from 0 to 20 and preferred values for x are 2, 3 or 4.
  • Preferred crystalline layered silicates of the formula given are those in which M is sodium and x assumes the values 2 or 3.
  • both ⁇ - and ⁇ -sodium disilicates Na 2 Si 2 O 5 YH 2 O are preferred.
  • Such compounds are commercially available, for example, under the name SKS® (Clariant company).
  • SKS-6 ® is a ⁇ -sodium having the formula Na 2 Si 2 O 5 ⁇ yH 2 O
  • SKS-7 ® is predominantly a beta-sodium disilicate.
  • acids for example citric acid or carbonic acid
  • SKS- 9® or SKS- 10® is formed from the ⁇ -sodium disilicate.
  • SKS- 10® commercially available under the name SKS- 9® or SKS- 10® (Clariant)
  • the alkalinity of the layered silicates can be suitably influenced.
  • Phyllosilicates doped with phosphate or with carbonate have altered crystal morphologies in comparison with the ⁇ -sodium disilicate, dissolve more rapidly and show an increased calcium binding capacity in comparison with ⁇ -sodium disilicate.
  • phyllosilicates of the general empirical formula x Na 2 O • y SiO 2 • z P 2 O 5 in which the ratio x to y is a number 0.35 to 0.6, the ratio x to z a number from 1, 75 to 1200 and the ratio y to z correspond to a number from 4 to 2800, described in the patent application DE 196 01 063.
  • the solubility of the layered silicates can also be increased by using particularly finely divided layered silicates.
  • compounds from the crystalline layer silicates with other ingredients can be used.
  • compounds with cellulose derivatives which have advantages in the disintegrating effect and are used in particular in detergent tablets and compounds with polycarboxylates, for example citric acid, or polymeric polycarboxylates, for example copolymers of acrylic acid, may be mentioned.
  • amorphous sodium silicates with a Na 2 O: SiO 2 modulus of from 1: 2 to 1: 3.3, preferably from 1: 2 to 1: 2.8 and in particular from 1: 2 to 1: 2.6, which Delayed and have secondary washing properties.
  • the dissolution delay compared to conventional amorphous sodium silicates may have been caused in various ways, for example by surface treatment, compounding, compacting / compacting or by overdrying.
  • the term "amorphous" is also understood to mean "X-ray amorphous”.
  • the silicates do not yield sharp X-ray reflections typical of crystalline substances in X-ray diffraction experiments, but at most one or more maxima of the scattered X-rays having a width of several degrees of diffraction angle. However, it may well even lead to particularly good builder properties if the silicate particles provide blurred or even sharp diffraction maxima in electron diffraction experiments. This is to be interpreted as meaning that the products have microcrystalline regions of size 10 to a few hundred nm, values of up to max. 50 nm and in particular up to max. 20 nm are preferred. Particularly preferred compacted / compacted amorphous silicates, compounded amorphous silicates and overdried X-ray amorphous silicates.
  • An optionally usable, finely crystalline, synthetic and bound water-containing zeolite is preferably zeolite A and / or P.
  • zeolite P zeolite MAP ® (commercial product from Crosfield) is particularly preferred.
  • zeolite X and mixtures of A, X and / or P are particularly preferred.
  • Commercially available and preferably usable in the context of the present invention is, for example, a cocrystal of zeolite X and zeolite A (about 80% by weight of zeolite X) ), which is sold by the company CONDEA Augusta SpA under the brand name VEGOBOND AX ® and by the formula
  • Suitable zeolites have an average particle size of less than 10 ⁇ m (volume distribution, measuring method: Coulter Counter) and preferably contain 18 to 22% by weight, in particular 20 to 22% by weight, of bound water.
  • phosphates as builders are possible, unless such use should not be avoided for environmental reasons.
  • alkali metal phosphates with particular preference of pentasodium or pentakalium triphosphate (sodium or potassium tripolyphosphate) in the washing and cleaning industry have the greatest importance.
  • Alkali metal phosphates is the summary term for the alkali metal (especially sodium and potassium) salts of various phosphoric acids, in which one can distinguish metaphosphoric acids (HPO 3 ) n and orthophosphoric H 3 PO 4 in addition to higher molecular weight representatives.
  • the phosphates combine several advantages: they act as alkali carriers, prevent lime deposits on machine parts or lime incrustations in fabrics and also contribute to the cleaning performance.
  • Sodium dihydrogen phosphate, NaH 2 PO 4 exists as dihydrate (density 1, 91 like 3 , melting point 60 °) and as monohydrate (density 2.04 like 3 ). Both salts are white powders which are very slightly soluble in water and which lose the water of crystallization when heated and at 200 ° C. into the weak acid diphosphate (disodium hydrogen diphosphate, Na 2 H 2 P 2 O 7 ), at higher temperature in sodium trimetaphosphate (Na 3 P 3 O 9 ) and Maddrell's salt (see below).
  • NaH 2 PO 4 is acidic; It arises when phosphoric acid is adjusted to a pH of 4.5 with sodium hydroxide solution and the mash is sprayed.
  • Potassium dihydrogen phosphate (primary or monobasic potassium phosphate, potassium biphosphate, KDP), KH 2 PO 4 , is a white salt of density 2.33, like '3 a melting point of 253 0 C [decomposition to form potassium polyphosphate (KPO 3 ) J and is readily soluble in water.
  • Disodium hydrogen phosphate (secondary sodium phosphate), Na 2 HPO 4 , is a colorless, very slightly water-soluble crystalline salt. It exists anhydrous and with 2 mol. (Density 2.066 like '3 , loss of water at 95 °), 7 mol. (Density 1, 68 like “3 , melting point 48 0 C with loss of 5 H 2 O) and 12 mol (Density 1, 52 like "3 , melting point 35 0 C with loss of 5 H 2 O), becomes anhydrous at 100 ° C and goes on stronger heating in the diphosphate Na 4 P 2 O 7 .
  • Disodium hydrogen phosphate is prepared by neutralization of phosphoric acid with soda solution using phenolphthalein as an indicator.
  • Dipotassium hydrogen phosphate (secondary or dibasic potassium phosphate), K 2 HPO 4 , is an amorphous, white salt that is readily soluble in water.
  • Triphosphate tertiary or tribasic potassium phosphate
  • K 3 PO 4 is a white, deliquescent, granular powder with a density of 2.56 '3 , has a melting point of 1340 ° and is in water with alkaline Reaction slightly soluble, for example, when heating Thomas slag with coal and potassium sulphate Despite the higher price, in the detergent industry, the more soluble, therefore highly effective, potassium phosphates often preferred over corresponding sodium compounds.
  • Tetrasodium diphosphate (sodium pyrophosphate), Na 4 P 2 O 7 , exists in anhydrous form (density 2.534 '3 , melting point 988 0 C, also indicated 88O 0 C) and as decahydrate (density 1, 815-1, 836 like "3 , melting point 94 0 C with loss of water). Both substances are colorless crystals which dissolve in water with an alkaline reaction, crystals.
  • Na 4 P 2 O 7 is formed when disodium phosphate is heated to> 200 ° C, or by reacting phosphoric acid with soda in a stoichiometric ratio and the solution
  • the decahydrate complexes heavy metal salts and hardness agents and therefore reduces the hardness of the water.
  • Kali diphosphate potassium pyrophosphate
  • K 4 P 2 O 7 exists in the form of the trihydrate and produces a colorless, hygroscopic powder with a density of 2.33 like '3 , which is soluble in water, wherein the pH of the 1% solution at 25 0 C is 10.4.
  • Condensation of the NaH 2 PO 4 or of the KH 2 PO 4 gives rise to relatively high molecular weight sodium and potassium phosphates, in which cyclic representatives, the sodium or potassium metaphosphates and chain-type, the sodium or potassium polyphosphates, can be distinguished. Especially for the latter are a variety of Names in use: Melted or calcined phosphates, Graham's salt, Kurrolsches and Maddrell's salt. All higher sodium and potassium phosphates are collectively referred to as condensed phosphates.
  • pentasodium triphosphate Na 5 P 3 Oi 0 , sodium tripolyphosphate
  • n 3.
  • 100 g of water at room temperature dissolve about 17 g, at 6O 0 C about 20 g, at 100 0 C, about 32 g of the salt water-free salt; after two hours of heating the solution to 100 0 C caused by hydrolysis about 8% orthophosphate and 15% diphosphate.
  • pentasodium triphosphate In the preparation of pentasodium triphosphate, phosphoric acid is reacted with soda solution or sodium hydroxide solution in a stoichiometric ratio and the solution is dehydrated by spraying. Similar to Graham's salt and sodium diphosphate, pentasodium triphosphate dissolves many insoluble metal compounds (including lime soaps, etc.). Pentakaliumtriphosphat, K 5 P 3 O 10 (potassium tripolyphosphate), for example, in the form of a 50 wt .-% solution (> 23% P 2 O 5 , 25% K 2 O) in the trade. The potassium polyphosphates are widely used in the washing and cleaning industry. There are also sodium potassium tripolyphosphates which can also be used in the context of the present invention. These arise, for example, when hydrolyzed sodium trimetaphosphate with KOH:
  • organic cobuilders it is possible in particular to use in the detergents and cleaners according to the invention polycarboxylates or polycarboxylic acids, polymeric polycarboxylates, polyaspartic acid, polyacetals, optionally oxidized dextrins, further organic cobuilders (see below) and phosphonates. These classes of substances are described below.
  • Useful organic builder substances are, for example, the polycarboxylic acids which can be used in the form of their sodium salts, polycarboxylic acids meaning those carboxylic acids which carry more than one acid function. These are, for example, citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids, aminocarboxylic acids, nitrilotriacetic acid (NTA), if such use can not be avoided for ecological reasons, and mixtures of these.
  • Preferred salts are the salts of polycarboxylic acids such as citric acid, adipic acid, succinic acid, glutaric acid, tartaric acid, sugar acids and mixtures thereof.
  • the acids themselves can also be used. In addition to their builder effect, they also typically have the property of an acidifying component and thus also serve to set a lower and milder pH of detergents or cleaners, unless the pH resulting from the mixture of the other components is desired.
  • system and environmentally compatible acids such as citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid, adipic acid, gluconic acid and any mixtures of these are to be mentioned.
  • mineral acids, in particular sulfuric acid or bases, in particular ammonium or alkali hydroxides can serve as pH regulators.
  • Such regulators are contained in the agents according to the invention in amounts of preferably not more than 20% by weight, in particular from 1.2% by weight to 17% by weight.
  • polymeric polycarboxylates for example the alkali metal salts of polyacrylic acid or of polymethacrylic acid, for example those having a relative molecular weight of 500 to 70,000 g / mol.
  • the molecular weights stated for polymeric polycarboxylates are weight-average molar masses M w of the particular acid form, which were determined in principle by means of gel permeation chromatography (GPC), a UV detector being used. The measurement was carried out against an external polyacrylic acid standard, which provides realistic molecular weight values due to its structural relationship with the polymers investigated. These data differ significantly from the molecular weight data, in which polystyrene sulfonic acids are used as standard. The molar masses measured against polystyrenesulfonic acids are generally significantly higher than the molecular weights specified in this document.
  • Suitable polymers are in particular polyacrylates, which preferably have a molecular weight of from 2,000 to 20,000 g / mol. Because of their superior solubility, the short-chain polyacrylates, which have molecular weights of from 2,000 to 10,000 g / mol, and particularly preferably from 3,000 to 5,000 g / mol, may again be preferred from this group.
  • copolymeric polycarboxylates in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid.
  • Copolymers of acrylic acid with maleic acid which contain 50 to 90% by weight of acrylic acid and 50 to 10% by weight of maleic acid have proven to be particularly suitable.
  • Their relative molecular weight, based on free acids, is generally from 2,000 to 70,000 g / mol, preferably from 20,000 to 50,000 g / mol and in particular from 30,000 to 40,000 g / mol.
  • the (co) polymeric polycarboxylates can be used either as a powder or used as an aqueous solution.
  • the content of the (co) polymeric polycarboxylates may be from 0.5 to 20% by weight, in particular from 1 to 10% by weight.
  • the polymers may also contain allylsulfonic acids such as allyloxybenzenesulfonic acid and methallylsulfonic acid as a monomer.
  • biodegradable polymers of more than two different monomer units for example those which contain as monomers salts of acrylic acid and maleic acid and vinyl alcohol or vinyl alcohol derivatives or as monomers salts of acrylic acid and 2-alkylallylsulfonic acid and sugar derivatives.
  • copolymers are those which have as monomers preferably acrolein and acrylic acid / acrylic acid salts or acrolein and vinyl acetate.
  • polymeric aminodicarboxylic acids their salts or their precursors.
  • polyaspartic acids or their salts and derivatives are particularly preferred.
  • polyacetals which can be obtained by reacting dialdehydes with polyolcarboxylic acids which have 5 to 7 C atoms and at least 3 hydroxyl groups.
  • Preferred polyacetals are obtained from dialdehydes such as glyoxal, glutaraldehyde, terephthalaldehyde and mixtures thereof and from polyol carboxylic acids such as gluconic acid and / or glucoheptonic acid.
  • dextrins for example oligomers or polymers of carbohydrates, which can be obtained by partial hydrolysis of starches.
  • the hydrolysis can be carried out by customary, for example acid or enzyme catalyzed processes.
  • it is hydrolysis products having average molecular weights in the range of 400 to 500 000 g / mol.
  • a polysaccharide with a dextrose equivalent (DE) in the range from 0.5 to 40, in particular from 2 to 30 is preferred, DE being a customary measure of the reducing action of a polysaccharide in comparison to dextrose, which is a DE of 100 has.
  • DE dextrose equivalent
  • Both maltodextrins with a DE of between 3 and 20 and dry glucose syrups with a DE of between 20 and 37 and also yellow dextrins and white dextrins with relatively high molecular weights in the range from 2 000 to 30 000 g / mol are useful.
  • oxidized derivatives of such dextrins are their reaction products with oxidizing agents which are capable of oxidizing at least one alcohol function of the saccharide ring to the carboxylic acid function.
  • oxidizing agents which are capable of oxidizing at least one alcohol function of the saccharide ring to the carboxylic acid function.
  • Particularly preferred organic builders for inventive Agents are oxidized starches, or their derivatives from the applications EP 472042, WO 97/25399, and EP 755944.
  • Ethylenediamine-N, N'-disuccinate is preferably used in form of its sodium or magnesium salts. Also preferred in this context are glycerol disuccinates and glycerol trisuccinates. Suitable amounts are in zeolith-, carbonate and / or silicate-containing formulations between 3 and 15 wt .-%.
  • organic cobuilders are, for example, acetylated hydroxycarboxylic acids or their salts, which may optionally also be present in lactone form and which contain at least 4 carbon atoms and at least one hydroxyl group and a maximum of two acid groups.
  • phosphonates are, in particular, hydroxyalkane or aminoalkanephosphonates.
  • hydroxyalkane phosphonates 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance as a co-builder. It is preferably used as the sodium salt, the disodium salt neutral and the tetrasodium salt alkaline (pH 9).
  • Preferred aminoalkane phosphonates are ethylenediamine tetramethylene phosphonate (EDTMP), diethylene triamine pentamethylene phosphonate (DTPMP) and their higher homologs. They are preferably in the form of neutral sodium salts, eg. B.
  • the builder used here is preferably HEDP from the class of phosphonates.
  • the aminoalkanephosphonates also have a pronounced heavy metal binding capacity. Accordingly, in particular if the agents also contain bleach, it may be preferable to use aminoalkanephosphonates, in particular DTPMP, or to use mixtures of the phosphonates mentioned.
  • Builder substances may optionally be present in the detergents or cleaners according to the invention in amounts of up to 90% by weight. They are preferably contained in amounts of up to 75% by weight. Detergents according to the invention have builder contents of, in particular, from 5% by weight to 50% by weight. In agents according to the invention for the cleaning of hard surfaces, in particular for the automated cleaning of dishes, the content of builder substances is in particular from 5% by weight to 88% by weight, wherein preferably no water-insoluble builder materials are used in such agents.
  • inventive means for the particular machine cleaning of dishes are 20 wt .-% to 40 wt .-% of water-soluble organic builder, in particular alkali, 5 wt .-% to 15 wt .-% alkali carbonate and 20 wt .-% to 40 wt .-% Alkalidisilikat included.
  • Solvents that can be used in the liquid to gelatinous compositions of detergents and cleaners for example, from the group of monohydric or polyhydric alcohols, alkanolamines or glycol ethers, provided that they are miscible in the specified concentration range with water.
  • the solvents are preferably selected from ethanol, n- or i-propanol, butanols, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, propylene glycol methyl, -ethyl or -propyl ether, dipropylene glycol monomethyl, or -ethyl ether, di-isopropylene glycol monomethyl, or -ethyl ether, methoxy, ethoxy or Butoxytriglykol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether and mixtures of these solvents.
  • Solvents may be used in the liquid to gelled detergents and cleaners according to the invention in amounts of between 0.1 and 20% by weight, but preferably below 15% by weight and in particular below 10% by weight.
  • one or more thickeners or thickening systems can be added to the composition according to the invention.
  • These high-molecular substances which are also called swelling agents, usually absorb the liquids and swell up to finally pass into viscous true or colloidal solutions.
  • Suitable thickeners are inorganic or polymeric organic compounds.
  • the inorganic thickeners include, for example, polysilicic acids, clay minerals such as montmorillonites, zeolites, silicas and bentonites.
  • the organic thickeners are derived from the groups of natural polymers, modified natural polymers and fully synthetic polymers.
  • Such naturally derived polymers include, for example, agar-agar, carrageenan, tragacanth, gum arabic, alginates, pectins, polyoses, guar gum, locust bean gum, starch, dextrins, gelatin and casein.
  • Modified natural products, which are used as thickeners come mainly from the group of modified starches and celluloses.
  • Fully synthetic thickeners are polymers such as polyacrylic and polymethacrylic compounds, vinyl polymers, polycarboxylic acids, polyethers, polyimines, polyamides and polyurethanes.
  • the thickeners may be present in an amount of up to 5% by weight, preferably from 0.05 to 2% by weight, and more preferably from 0.1 to 1.5% by weight, based on the finished composition .
  • the washing and cleaning agent according to the invention may optionally contain further conventional ingredients sequestering agent, electrolyte and other auxiliaries, such as optical brighteners, grayness inhibitors, silver corrosion inhibitors, dye transfer inhibitors, foam inhibitors, abrasives, dyes and / or fragrances, as well as microbial active ingredients, UV-absorbents and / or enzyme stabilizers.
  • Detergents according to the invention may contain, as optical brighteners, derivatives of diaminostilbenedisulfonic acid or their alkali metal salts.
  • derivatives of diaminostilbenedisulfonic acid or their alkali metal salts for example, salts of 4,4'-bis (2-anilino-4-morpholino-1, 3,5-triazinyl-6-amino) stilbene-2,2'-disulphonic acid or similarly constructed compounds which are substituted for the morpholino Group carry a diethanolamino group, a methylamino group, an anilino group or a 2-methoxyethylamino group.
  • brighteners of the substituted diphenylstyrene type may be present, for example the alkali metal salts of 4,4'-bis (2-sulfostyryl) -diphenyl, 4,4'-bis (4-chloro-3-sulfostyryl) -diphenyl, or 4- (4-chlorostyryl) -4 '- (2-sulfostyryl) -diphenyls.
  • Mixtures of the aforementioned optical brightener can be used.
  • Graying inhibitors have the task of keeping suspended from the textile fiber dirt suspended in the fleet.
  • Water-soluble colloids of mostly organic nature are suitable for this purpose, for example starch, glue, gelatin, salts of ether carboxylic acids or ether sulfonic acids of starch or of cellulose or salts of acidic sulfuric acid esters of cellulose or starch.
  • water-soluble polyamides containing acidic groups are suitable for this purpose.
  • starch derivatives can be used, for example aldehyde starches.
  • cellulose ethers such as carboxymethylcellulose (Na salt), methylcellulose, hydroxyalkylcellulose and mixed ethers, such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, methylcarboxymethylcellulose and mixtures thereof, for example in amounts of from 0.1 to 5% by weight, based on the compositions ,
  • silver corrosion inhibitors can be used in dishwashing detergents according to the invention.
  • dishwashing detergents Such are known in the art, for example benzotriazoles, iron (III) chloride or CoSO 4 .
  • benzotriazoles iron (III) chloride
  • CoSO 4 a silver corrosion inhibitor for use in conjunction with enzymes
  • particularly suitable silver corrosion inhibitors for use in conjunction with enzymes are manganese, titanium, zirconium, hafnium, vanadium, cobalt or cerium salts and / or complexes where the said metals are present in one of the oxidation states II, III, IV, V or VI.
  • Examples of such compounds are MnSO 4 , V 2 O 5 , V 2 O 4 , VO 2 , TiOSO 4 , K 2 TiF 6 , K 2 ZrF 6 , Co (NO 3 ) 2 , Co (NO 3 ) 3 , and the like mixtures.
  • soil-release or “soil repellents” are mostly polymers which impart soil repellency when used in a laundry detergent detergent and / or aid in the soil release performance of the other detergent ingredients. A similar effect can also be observed in their use in hard surface cleaners.
  • Particularly effective and long-known soil release agents are copolyesters with dicarboxylic acid, alkylene glycol and polyalkylene glycol units. Examples of these are copolymers or copolymers of polyethylene terephthalate and polyoxyethylene glycol (DT 16 17 141, or DT 22 00 911).
  • German Offenlegungsschrift DT 22 53 063 acidic agents which contain, inter alia, a copolymer of a dibasic carboxylic acid and an alkylene or cycloalkylene polyglycol.
  • Polymers of ethylene terephthalate and polyethylene oxide terephthalate and their use in detergents are described in German patents DE 28 57 292 and DE 33 24 258 and European patent EP 0 253 567.
  • European patent EP 066 944 relates to compositions containing a copolyester of ethylene glycol, polyethylene glycol, aromatic dicarboxylic acid and sulfonated aromatic dicarboxylic acid in certain molar ratios.
  • European Patent EP 0 185 427 discloses methyl or ethyl end-capped polyesters having ethylene and / or propylene terephthalate and polyethylene oxide terephthalate units and detergents containing such soil release polymer.
  • European patent EP 0 241 984 relates to a polyester which, besides oxyethylene groups and terephthalic acid units, also contains substituted ethylene units and also glycerine units.
  • European Patent EP 0 241 985 discloses polyesters which, in addition to oxyethylene groups and terephthalic acid units, contain 1, 2-propylene, 1, 2-butylene and / or 3-methoxy-1, 2-propylene groups and also glycerol units and with d - Are capped to C 4 alkyl groups.
  • European Patent EP 0 274 907 describes sulfoethyl end-capped terephthalate-containing soil release polyesters. According to the European patent application EP 0 357 280, by sulfonation of unsaturated terminal groups, soil-release polyesters containing terephthalate, alkylene glycol and poly-C 2 - 4 prepared glycol units.
  • International Patent Application WO 95/32232 relates to acidic, aromatic soil release polymers.
  • WO 97/31085 discloses non-polymeric soil repellent active ingredients for multi-functional cotton materials: a first entity, which may be cationic, for example, is capable of adsorption to the cotton surface by electrostatic interaction, and a second Unit that is hydrophobic is responsible for the retention of the drug at the water / cotton interface.
  • the color transfer inhibitors which are suitable for use in textile detergents according to the invention include in particular polyvinylpyrrolidones, polyvinylimidazoles, polymeric N-oxides such as poly (vinylpyridine-N-oxide) and copolymers of vinylpyrrolidone with vinylimidazole.
  • foam inhibitors When used in automated cleaning processes, it may be advantageous to add foam inhibitors to the agents concerned.
  • foam inhibitors are, for example, soaps of natural or synthetic origin, which have a high proportion of Ci 8 -C 24 fatty acids.
  • Suitable non-surfactant foam inhibitors are, for example, organopolysiloxanes and mixtures thereof with microfine, optionally signed silica and paraffins, waxes, microcrystalline waxes and mixtures thereof with signed silica or bistearylethylenediamide. It is also advantageous to use mixtures of various foam inhibitors, for example those of silicones, paraffins or waxes.
  • the foam inhibitors in particular silicone and / or paraffin-containing foam inhibitors, are bound to a granular, water-soluble, or dispersible carrier substance.
  • a granular, water-soluble, or dispersible carrier substance In particular, mixtures of paraffins and bistearylethylenediamides are preferred.
  • a hard surface cleaning agent according to the invention may contain abrasive constituents, in particular from the group comprising quartz flours, wood flours, plastic flours, chalks and glass microspheres and mixtures thereof.
  • Abrasives are preferably present in the detergents according to the invention in an amount of not more than 20% by weight, in particular in an amount of from 5 to 15% by weight.
  • Dyes and fragrances are added to detergents and cleaners in order to improve the aesthetic appearance of the products and to provide the consumer with a visually and sensory "typical and unmistakable" product in addition to the washing and cleaning performance.
  • perfume oils or fragrances individual perfume compounds, for example the synthetic products of the ester type, ethers, aldehydes, ketones, alcohols and hydrocarbons can be used.
  • Fragrance compounds of the ester type are, for example, benzyl acetate, phenoxyethyl isobutyrate, p-tert-butylcyclohexyl acetate, linalyl acetate, dimethylbenzylcarbinyl acetate, phenylethyl acetate, linalyl benzoate, benzyl formate, ethylmethylphenyl glycinate, allylcyclohexyl propionate, styrallyl propionate and benzyl salicylate.
  • the ethers include, for example, benzyl ethyl ether, to the aldehydes, for example, the linear alkanals having 8-18 C atoms, citral, citronellal, citronellyloxyacetaldehyde, cyclamen aldehyde, hydroxycitronellal, lilial and bourgeonal, to the ketones, for example, the ionone, ⁇ -lsomethylionon and methyl cedryl ketone, to the alcohols anethole, citronellol, eugenol, geraniol, linalool, phenylethyl alcohol and terpineol, the hydrocarbons include mainly the terpenes such as limonene and pinene.
  • fragrance oils may also contain natural fragrance mixtures such as are available from vegetable sources, for example, pine, citrus, jasmine, patchouly, rose or ylang-ylang oil. Also suitable are muscatel, sage, chamomile, clove, lemon balm, mint, cinnamon, lime, juniper, vetiver, olibanum, galbanum and labdanum, and orange blossom, neroliol, orange peel and sandalwood.
  • the content of detergents and cleaners to dyes is less than 0.01 wt .-%, while perfumes can account for up to 2 wt .-% of the total formulation.
  • the fragrances can be incorporated directly into the detergents or cleaners, but it can also be advantageous to apply the fragrances to carriers, which enhance the adhesion of the perfume to the items to be cleaned and provide a slower release of fragrance for long-lasting fragrance, especially of treated textiles.
  • carrier materials for example, cyclodextrins have been proven, the cyclodextrin-perfume complexes can be additionally coated with other excipients.
  • a further preferred carrier for fragrances is the described zeolite X, which can also absorb fragrances instead of or in mixture with surfactants. Preference is therefore given to washing and cleaning agents containing the described zeolite X and fragrances, which are preferably at least partially absorbed on the zeolite.
  • Preferred dyes the selection of which presents no difficulty to the skilled person, have a high storage stability and insensitivity to the other ingredients of the agents and to light and no pronounced substantivity to textile fibers so as not to stain them.
  • Detergents or cleaners may contain antimicrobial agents to combat microorganisms. Depending on the antimicrobial spectrum and mechanism of action, a distinction is made between bacteriostatic agents and bactericides, fungistatics and fungicides, etc. Important substances from these groups are, for example, benzalkonium chlorides, alkylarylsulfonates, halophenols and phenolmercuric acetate.
  • antimicrobial action and antimicrobial active substance have the usual meaning within the scope of the teaching according to the invention, which is described, for example, by KH Wallophen in "Praxis der Sterilisation, Disinfection - Conservation: Germ Identification - Company Hygiene” (5th edition - Stuttgart, New York: Thieme, 1995
  • Suitable antimicrobial agents are preferably selected from the groups of alcohols, amines, aldehydes, antimicrobial acids or their salts, carboxylic esters, acid amides, phenols, phenol derivatives, diphenyls, diphenylalkanes, Urea derivatives, oxygen, nitrogen acetals and formals, benzamidines, isothiazolines, phthalimide derivatives, pyridine derivatives, antimicrobial surface-active compounds, guanidines, antimicrobial amphoteric compounds, quinolines, 1, 2-dibromo-2,4-dicyanobutane, iodo-2-propyl butyl
  • the antimicrobial agent may be selected from ethanol, n-propanol, i-propanol, 1,3-butanediol, phenoxyethanol, 1,2-propylene glycol, glycerol, undecylenic acid, benzoic acid, salicylic acid, dihydracetic acid, o-phenylphenol, N-methylmorpholine.
  • acetonitrile MMA
  • 2-benzyl-4-chlorophenol 2,2'-methylenebis (6-bromo-4-chlorophenol), 4,4'-dichloro-2'-hydroxydiphenyl ether (dichlosan), 2,4 , 4'-trichloro-2'-hydroxydiphenyl ether (trichlosan), chlorhexidine, N- (4-chlorophenyl) -N- (3,4-dichlorophenyl) -urea, N, N'-1-iodo-decanediyldi-i -pyridinyl ⁇ -ylidene ⁇ to ⁇ i-octanamine ⁇ dihydrochloride, N, N'-bis (4-chlorophenyl) nyl) -3,12-diimino-2,4,11,13-tetraaza-tetradecandiimidamide, glucoprotamines, antimicrobial surface-active quaternary
  • Ethylene bis (N-butylphenylbiguanide), ethylene bis (2,5-diethoxyphenylbiguanide), ethylene bis (2,4-dimethylphenyl biguanide), ethylene bis (o-diphenylbiguanide), ethylene bis (mixed amyl naphthyl biguanide) , N-butyl-ethylene-bis (phenylbiguanide), trimethylene bis (o-tolylbiguanide), N-butyl-trimethyl-bis- (phenyl biguanide) and the corresponding salts such as acetates, gluconates, hydrochlorides, hydrobromides, citrates, bisulfites, Fluorides, polymaleates, N-cocosalkyl sarcosinates, phosphites, hypophosphites, perfluorooctanoates, silicates, sorbates, salicylates, maleates, tartrates, fumarates,
  • halogenated xylene and cresol derivatives such as p-chlorometacresol or p-chloro-meta-xylene, and natural antimicrobial agents of plant origin (for example, from spices or herbs), animal and microbial origin.
  • antimicrobial surface-active quaternary compounds a natural antimicrobial agent of plant origin and / or a natural antimicrobial agent of animal origin, most preferably at least one natural antimicrobial agent of plant origin from the group comprising caffeine, theobromine and theophylline and essential oils such as eugenol, thymol and geraniol, and / or at least one natural antimicrobial agent of animal origin from the group comprising enzymes such as protein from milk, lysozyme and lactoperoxidase, and / or at least one antimicrobial surface-active quaternary compound having an ammonium, sulfonium, phosphonium, iodonium or arsonium group, peroxo compounds and chlorine compounds become. Also substances of microbial origin, so-called bacteriocins, can be used.
  • the quaternary ammonium compounds (QAV) suitable as antimicrobial agents have the general formula (R 1 ) (R 2 ) (R 3 ) (R 4 ) N + X " , in which R 1 to R 4 are identical or different C-
  • the radicals preferably at least one of the radicals a chain length of 8 to 18, in particular 12 to 16 C-atoms.
  • QACs can be prepared by reacting tertiary amines with alkylating agents, such as, for example, methyl chloride, benzyl chloride, dimethyl sulfate, dodecyl bromide, but also ethylene oxide.
  • alkylating agents such as, for example, methyl chloride, benzyl chloride, dimethyl sulfate, dodecyl bromide, but also ethylene oxide.
  • alkylating agents such as, for example, methyl chloride, benzyl chloride, dimethyl sulfate, dodecyl bromide, but also ethylene oxide.
  • alkylating agents such as, for example, methyl chloride, benzyl chloride, dimethyl sulfate, dodecyl bromide, but also ethylene oxide.
  • the alkylation of tertiary amines with a long alkyl radical and two methyl groups succeeds particularly easily, and the quaternization of tertiary
  • Suitable QACs are, for example, benzalkonium chloride (N-alkyl-N, N-dimethylbenzylammonium chloride, CAS No. 8001-54-5), benzalkone B (m, p-dichlorobenzyldimethyl-C 12 -alkylammonium chloride, CAS No. 58390-78-6), benzoxonium chloride (benzyldodecylbis (2-hydroxyethyl) ammonium chloride), cetrimonium bromide (N-hexadecyl-N, N-trimethylammonium bromide, CAS No.
  • benzetonium chloride N, N-dimethyl-N- [2- [2- [p- (1,1,3,3-tetramethylbutyl) phenoxy] ethoxy] ethyl] benzylammonium chloride, CAS No. 121-54-0
  • dialkyldimethylammonium chlorides such as di-n-decyldimethylammonium chloride (CAS No. 7173-51-5-5), didecyldi-methylammonium bromide (CAS No. 2390-68-3 ), Dioctyl-dimethyl-ammonium chloride, 1-cetylpyridinium chloride (CAS No.
  • QUATS are the benzalkonium chlorides with C 8 -C 8 alkyl, in particular Ci ⁇ -C M -Aklyl-benzyl-dimethyl-ammonium chloride.
  • Benzalkonium halides and / or substituted benzalkonium halides are for example commercially available as Barquat ® ex Lonza, Marquat® ® ex Mason, Variquat ® ex Witco / Sherex and Hyamine ® ex Lonza and as Bardac ® ex Lonza.
  • Other commercially obtainable antimicrobial agents are hexaminium N- (3-chloroallyl) as Dowicide and Dowicil ® ® ex Dow, Benzethonium as Hyamine ® 1622 ex Rohm & Haas, methylbenzethonium as Hyamine ® 10X ex Rohm & Haas, cetylpyridinium chloride such Cepacol ex Merrell Labs.
  • the antimicrobial agents are used in amounts of 0.0001 wt .-% to 1 wt .-%, preferably from 0.001 wt .-% to 0.8 wt .-%, particularly preferably from 0.005 wt .-% to 0.3 wt .-% and in particular from 0.01 to 0.2 wt .-% used.
  • the detergents or cleaners according to the invention may contain UV absorbents (UV absorbers) which are applied to the treated textiles and improve the lightfastness of the fibers and / or the lightfastness of other formulation constituents.
  • UV absorbents UV absorbers
  • Under UV absorber are organic substances (sunscreen) to understand, which are able to absorb ultraviolet rays and the absorbed energy in the form of longer-wave radiation, for example, to give off heat.
  • Compounds having these desired properties include, for example, the non-radiative deactivating compounds and derivatives of benzophenone having substituents in the 2- and / or 4-position. Also suitable are substituted benzotriazoles, in the 3-position phenyl-substituted acrylates (cinnamic acid derivatives, optionally with cyano groups in the 2-position), salicylates, organic Ni complexes and natural substances such as umbelliferone and the body's own urocanic acid.
  • the biphenyl and, above all, stilbene derivatives as described for example in EP 0728749 A are described and commercially available as Tinosorb FD ® ® or Tinosorb FR ex Ciba.
  • UV-B absorbers may be mentioned: 3-Benzylidencampher or 3-Benzylidennorcampher and its derivatives, for example 3- (4-methylbenzylidene) camphor, as described in EP 0693471 B1; 4-aminobenzoic acid derivatives, preferably 2-ethylhexyl 4- (dimethylamino) benzoate, 2-octyl 4- (dimethylamino) benzoate and 4- (dimethylamino) benzoic acid ester; Esters of cinnamic acid, preferably 4-methoxycinnamic acid 2-ethylhexyl ester, 4-methoxycinnamic acid propyl ester, 4-methoxycinnamic acid isoamyl ester, 2-cyano-3,3-phenylcinnamic acid 2-ethylhexyl ester (octocrylene); Esters of salicylic acid, preferably 2-ethylhexyl salicylate,
  • Ketotricyclo (5.2.1.0) decane derivatives as described in EP 0694521 B1.
  • 2-phenylbenzimidazole-5-sulfonic acid and its alkali metal, alkaline earth metal, ammonium, alkylammonium, alkanolammonium and glucammonium salts Sulfonic acid derivatives of benzophenones, preferably 2-hydroxy-4-methoxybenzophenone-5-sulfonic acid and its salts
  • Sulfonic acid derivatives of 3-Benzylidencamphers such as 4- (2-oxo-3-bornylidenme- thyl) benzenesulfonic acid and 2-methyl-5- (2-oxo-3-bomylidene) sulfonic acid and salts thereof.
  • UV-A and UV-B filters can also be used in mixtures.
  • insoluble photoprotective pigments namely finely dispersed, preferably nano-metal oxides or salts, are also suitable for this purpose.
  • suitable metal oxides are in particular zinc oxide and titanium dioxide and, in addition, oxides of iron, zirconium, silicon, manganese, aluminum and cerium and mixtures thereof.
  • silicates (talc) barium sulfate or zinc stearate can be used.
  • the oxides and salts are already used in the form of the pigments for skin-care and skin-protecting emulsions and decorative cosmetics.
  • the particles should have an average diameter of less than 100 nm, preferably between 5 and 50 nm and in particular between 15 and 30 nm. They may have a spherical shape, but it is also possible to use those particles which have an ellipsoidal or otherwise deviating shape from the spherical shape.
  • the pigments may also be surface-treated, that is to say hydrophilized or hydrophobicized.
  • Typical examples are coated titanium dioxides, such as, for example, titanium dioxide T 805 (Degussa) or Eusolex® T2000 (Merck; preferred hydrophilic coating agents are silicones and particularly preferably trialkoxyoctylsilanes or simethicones.) Micronized zinc oxide is preferably used see the review by P. Finkel in S ⁇ FW Journal 122 (1996), p. 543.
  • the UV absorbents are usually used in amounts of from 0.01% by weight to 5% by weight, preferably from 0.03% by weight to 1% by weight.
  • compositions according to the invention may comprise further enzymes in addition to the proteins according to the invention for increasing the washing or cleaning performance, it being possible in principle to use all enzymes established for this purpose in the prior art.
  • These include in particular other proteases, amylases, lipases, hemicellulases, cellulases or oxidoreductases, and preferably mixtures thereof.
  • These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents and cleaners, which are preferably used accordingly.
  • Compositions according to the invention preferably contain these further enzymes in total amounts of 1 ⁇ 10 -6 to 5 percent by weight, based on active protein.
  • those of the subtilisin type are preferred.
  • subtilisins BPN 'and Carlsberg examples thereof are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and the enzymes thermitase, proteinase K and the subtilases, but not the subtilisins in the narrower sense Proteases TW3 and TW7.
  • Subtilisin Carlsberg in a developed form under the trade names Alcalase ® from Novozymes A / S, Bagsvaerd, Denmark.
  • the subtilisins 147 and 309 are sold under the trade names Esperase ®, or Savinase ® from Novozymes.
  • BLAP ® variants of the protease from Bacillus lentus DSM 5483 (WO 91/02792 A1) to derive, in particular, in WO 92/21760 A1, WO 95/23221 A1, WO 02/088340 A2 and WO 03 / 038082 A2.
  • Other useful proteases from various Bacillus sp.- and ß. g / oson / V strains are evident from the patent applications WO 03/054185, WO 03/056017, WO 03/055974 and WO 03/054184.
  • proteases are, for example, under the trade names Durazym ®, relase ®, Everlase® ®, Nafizym, Natalase ®, Kannase® ® and Ovozymes ® from Novozymes, under the trade names Purafect ®, Purafect ® OxP and Properase.RTM ® by the company Genencor, that under the trade name Protosol® ® from Advanced Biochemicals Ltd., Thane, India, under the trade name Wuxi ® from Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® ® and protease P ® by the company Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzyme available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
  • amylases which can be used according to the invention are the ⁇ -amylases from Bacillus licheniformis, from ⁇ . amyloliquefaciens or from ß. stearothermophilus and their improved for use in detergents and cleaners further developments.
  • the enzyme from ß. licheniformis is available from Novozymes under the name Termamyl ® and from Genencor under the name Purastar® ® ST.
  • Development products of this ⁇ -amylase are available from Novozymes under the trade names Duramyl ® and Termamyl ® ultra, from Genencor under the name Purastar® ® OxAm and from Daiwa Seiko Inc., Tokyo, Japan, as Keistase ®.
  • the ⁇ -amylase of ⁇ . amyloliquefaciens is sold by Novozymes under the name BAN ®, and variants derived from the ⁇ -amylase from B.. stearothermophilus under the names BSG ® and Novamyl ®, likewise from Novozymes. Further usable commercial products are, for example, the amylase LT® and Stainzyme®, the latter also from Novozymes.
  • ⁇ -amylase from Bacillus sp. Disclosed in the application WO 02/10356 A2 for this purpose.
  • a 7-7 (DSM 12368) and described in the application WO 02/44350 A2 cyclodextrin glucanotransferase (CGTase) from ß. agaradherens (DSM 9948).
  • CCTase cyclodextrin glucanotransferase
  • DSM 9948 cyclodextrin glucanotransferase
  • amylolytic enzymes which belong to the sequence space of ⁇ -amylases, which is defined in the application WO 03/002711 A2, and those which are described in the application WO 03/054177 A2 can be used.
  • fusion products of the molecules mentioned can be used, for example those from application DE 10138753 A1.
  • compositions according to the invention may contain lipases or cutinases, in particular because of their triglyceride-cleaving activities, but also in order to generate in situ peracids from suitable precursors.
  • lipases or cutinases include, for example, the lipases originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, in particular those with the amino acid exchange D96L. They are sold, for example, by Novozymes under the trade names Lipolase ®, Lipolase Ultra ®, LipoPrime® ®, Lipozyme® ® and Lipex ®.
  • the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens.
  • lipases are available from Amano under the designations Lipase CE ®, Lipase P ®, Lipase B ®, or lipase CES ®, Lipase AKG ®, Bacillis sp. Lipase® , Lipase AP® , Lipase M- AP® and Lipase AML® are available. From the company Genencor, for example, the lipases, or cutinases can be used, the initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii.
  • Detergents according to the invention may contain cellulases, depending on the purpose, as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously supplement each other in terms of their various performance aspects.
  • These performance aspects include in particular contributions to the primary washing performance, to the secondary washing performance of the agent
  • EG endoglucanase
  • Novozymes A useful fungal, endoglucanase (EG) -rich cellulase preparation, or its further developments are offered by Novozymes under the trade name Celluzyme ®.
  • Further commercial products of this company are Cellusoft® ® and Renozyme ®. The latter is based on the application WO 96/29397 A1. Performance-enhanced cellulase variants For example, see the application WO 98/12307 A1.
  • the cellulases disclosed in the application WO 97/14804 A1 can be used; For example, it revealed 20 kD EG Melanocarpus, available from AB Enzymes, Finland, under the trade names Ecostone® ® and Biotouch ®. Further commercial products from AB Enzymes are Econase® ® and ECOPULP ®. Other suitable cellulases from Bacillus sp. CBS 670.93 and CBS 669.93 are disclosed in WO 96/34092 A2, wherein those derived from Bacillus sp. CBS 670.93 from the company Genencor under the trade name Puradax ® is available. Further commercial products of the company Genencor are "Genencor detergent cellulase L" and lndiAge ® Neutra.
  • compositions according to the invention may, in particular for the removal of certain problem soiling, comprise, in addition to the polypeptides according to the invention, further enzymes which are combined under the term hemicellulases.
  • further enzymes which are combined under the term hemicellulases.
  • Suitable mannanases are available, for example under the name Gamanase ® and Pektinex AR ® from Novozymes, under the name Rohapec ® B1 L from AB Enzymes and under the name Pyrolase® ® from Diversa Corp., San Diego, CA, USA ,
  • a suitable ß-glucanase from a ß. alcalophilus results from the application WO 99/06573 A1.
  • the from ß. subtilis derived beta-glucanase is available under the name Cereflo ® from Novozymes.
  • detergents and cleaners according to the invention may be oxidoreductases, for example oxidases, oxygenases, catalases, peroxidases, such as halo, chloro, bromo, lignin, glucose or manganese peroxidases, dioxygenases or laccases (phenol oxidases, polyphenol oxidases) contain.
  • oxidases oxygenases, catalases, peroxidases, such as halo, chloro, bromo, lignin, glucose or manganese peroxidases, dioxygenases or laccases (phenol oxidases, polyphenol oxidases) contain.
  • Suitable commercial products Denilite® ® 1 and 2 from Novozymes should be mentioned.
  • organic, particularly preferably aromatic, compounds which interact with the enzymes in order to enhance the activity of the relevant oxidoreductases (enhancers) or to ensure the flow of electrons (mediators) at greatly varying redox potentials between the oxidizing enzymes and the soils.
  • the enzymes additionally employed in agents according to the invention are either originally derived from microorganisms, such as the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or are produced by biotechnological methods known per se by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or filamentous fungi.
  • the purification of the relevant enzymes is conveniently carried out by conventional methods, for example by precipitation, sedimentation, concentration, filtration of the liquid phases, microfiltration, ultrafiltration, exposure to chemicals, deodorization or suitable combinations of these steps.
  • Agents according to the invention can be added to the polypeptides according to the invention as well as the additionally used enzymes in any form established according to the prior art. These include, for example, the solid preparations obtained by granulation, extrusion or lyophilization or, especially in the case of liquid or gel-form detergents, solutions of the enzymes, advantageously as concentrated as possible, sparing in water and / or added with stabilizers.
  • these proteins can be encapsulated for both the solid and liquid dosage forms, for example, by spray-drying or extruding the enzyme solution together with a preferably natural polymer or in the form of capsules, for example those in which the enzymes are entrapped as in a solidified gel or in those of the core-shell type, in which an enzyme-containing core is coated with a water, air and / or chemical impermeable protective layer.
  • a preferably natural polymer or in the form of capsules for example those in which the enzymes are entrapped as in a solidified gel or in those of the core-shell type, in which an enzyme-containing core is coated with a water, air and / or chemical impermeable protective layer.
  • further active ingredients for example stabilizers, emulsifiers, pigments, bleaches or dyes, may additionally be applied.
  • Such capsules are applied by methods known per se, for example by shaking or rolling granulation or in fluid-bed processes.
  • such granules for example by applying
  • a protein contained in an agent according to the invention in particular also the polypeptide according to the invention, can be protected against damage, for example inactivation, denaturation or decomposition, for example by physical influences, oxidation or proteolytic cleavage, especially during storage.
  • damage for example inactivation, denaturation or decomposition, for example by physical influences, oxidation or proteolytic cleavage, especially during storage.
  • inhibition of proteolysis is particularly preferred, especially if the agents also contain proteases.
  • Preferred agents according to the invention contain stabilizers for this purpose.
  • One group of stabilizers are reversible protease inhibitors.
  • Benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters are frequently used for this purpose, including, in particular, derivatives with aromatic groups, for example ortho, meta or para-substituted phenylboronic acids, in particular 4-formylphenylboronic acid, or the salts or Esters of the compounds mentioned.
  • peptide aldehydes that is oligopeptides with a reduced C-terminus, especially those of 2 to 50 monomers are used for this purpose.
  • the peptidic reversible protease inhibitors include, among others, ovomucoid and leupeptin.
  • enzyme stabilizers are aminoalcohols, such as mono-, di-, triethanol- and -propanolamine and mixtures thereof, aliphatic carboxylic acids up to Ci 2, such as succinic acid, other dicarboxylic acids or salts of said acids. End-capped fatty acid amide alkoxylates are also suitable for this purpose. Certain organic acids used as builders are capable, as disclosed in WO 97/18287, of additionally stabilizing a contained enzyme.
  • Lower aliphatic alcohols but especially polyols such as glycerol, ethylene glycol, propylene glycol or sorbitol are other frequently used enzyme stabilizers.
  • Di-glycerol phosphate also protects against denaturation due to physical influences.
  • calcium and / or magnesium salts are used, such as calcium acetate or calcium formate.
  • Polyamide oligomers or polymeric compounds such as lignin, water-soluble vinyl copolymers or cellulose ethers, acrylic polymers and / or polyamides stabilize the enzyme preparation, inter alia, against physical influences or pH fluctuations.
  • Polyamine N-oxide containing polymers act simultaneously as enzyme stabilizers and as dye transfer inhibitors.
  • Other polymeric stabilizers are linear C 8 -C 8 polyoxyalkylenes.
  • alkylpolyglycosides can stabilize the enzymatic components of the agent according to the invention and are able, preferably, to additionally increase their performance.
  • Crosslinked N-containing compounds preferably perform a dual function as soil release agents and as enzyme stabilizers. Hydrophobic, nonionic polymer stabilizes in particular an optionally contained cellulase.
  • Reducing agents and antioxidants increase the stability of the enzymes to oxidative degradation;
  • sulfur-containing reducing agents are familiar.
  • Other examples are sodium sulfite and reducing sugars.
  • peptide-aldehyde stabilizers for example of polyols, boric acid and / or borax, the combination of boric acid or borate, reducing salts and succinic acid or other dicarboxylic acids or the combination of boric acid or borate with polyols or polyamino compounds and with reducing salts.
  • the effect of peptide-aldehyde stabilizers is favorably enhanced by the combination with boric acid and / or boric acid derivatives and polyols, and still further by the additional action of divalent cations, such as calcium ions.
  • agents of the invention can be offered in all conceivable forms, polypeptides of the invention in all appropriate for the addition to the respective agents These include, for example, liquid formulations, solid granules or capsules.
  • the encapsulated form lends itself to protecting the enzymes or other ingredients from other ingredients, such as bleaches, or to allow for controlled release.
  • Such capsules are disclosed, for example, with the patent applications WO 97/24177 and DE 19918267.
  • a possible encapsulation method is that the proteins are encapsulated in this substance, starting from a mixture of the protein solution with a solution or suspension of starch or a starch derivative. Such an encapsulation process is described in the application WO 01/38471.
  • the proteins - polypeptides according to the invention as well as optionally contained further enzymes - can be used, for example, in dried, granulated and / or encapsulated form. They may be added separately, ie as a separate phase, or with other ingredients together in the same phase, with or without compaction. If microencapsulated enzymes are to be processed in solid form, the water can be removed by methods known from the prior art from the aqueous solutions resulting from the workup, such as spray drying, centrifuging or by solubilization. The particles obtained in this way usually have a particle size between 50 and 200 microns.
  • the proteins may be added to liquid, gelatinous or pasty agents according to the invention in a concentrated aqueous or non-aqueous solution, suspension or emulsion starting from a protein recovery and preparation carried out in the prior art, but also in gel form or encapsulated or as a dried powder.
  • Such detergents or cleaners according to the invention are generally prepared by simple mixing of the ingredients which can be added in bulk or as a solution in an automatic mixer.
  • a cleaning agent according to the invention in particular a hard surface cleaner according to the invention, may also contain one or more propellants (INCI propellants), usually in an amount of 1 to 80% by weight, preferably 1 to 5 to 30% by weight, in particular 2 to 10 wt .-%, particularly preferably 2.5 to 8 wt .-%, most preferably 3 to 6 wt .-%, contained.
  • one or more propellants ICI propellants
  • Propellants are inventively usually propellants, especially liquefied or compressed gases.
  • propellants especially liquefied or compressed gases.
  • the choice depends on the product to be sprayed and the field of application.
  • compressed gases such as nitrogen, carbon dioxide or nitrous oxide, which are generally insoluble in the liquid detergent, the Operating pressure with each valve actuation.
  • Detergent-soluble or even solvent-acting liquefied gases (liquefied gases) as propellants offer the advantage of constant operating pressure and uniform distribution because the propellant vaporizes in the air, taking up more than a hundred times that volume.
  • blowing agents are accordingly: butanes, carbon dioxides, dimethyl carbonates, dimethyl ether, ethanes, Hydrochlorofluorocarbon 22, hydrochlorofluorocarbon 142b, hydrofluorocarbon 152a, hydrofluorocarbon 134a, hydrofluorocarbon 227ea, isobutanes, isopentanes, nitrogen, nitrous oxides, pentanes, propanes.
  • Chlorofluorocarbons (chlorofluorocarbons, CFCs) as propellant are, however, preferably largely and in particular completely dispensed with because of their harmful effect on the ozone shield of the atmosphere, which protects against hard UV radiation, the so-called ozone layer.
  • Preferred blowing agents are liquefied gases.
  • Liquid gases are gases that can be performed at mostly already low pressures and 2O 0 C from the gaseous to the liquid state.
  • under liquefied gases are the hydrocarbons propane, propene, butane, butene, isobutane (2-methylpropane), isobutene (2-methylpropene), which are obtained in oil refineries as by-products from distillation and cracking of petroleum and in natural gas treatment during gasoline separation. Isobutylene) and mixtures thereof.
  • the cleaning agent particularly preferably contains propane, butane and / or isobutane, in particular propane and butane, as one or more propellants, more preferably propane, butane and isobutane.
  • an important task of the enzyme preparation and in particular of the polypeptides according to the invention is, as stated above, the primary washing performance.
  • the proteases contained in detergents can also fulfill the function of activating other enzymatic constituents by proteolytic cleavage or inactivating them after a corresponding action time.
  • An embodiment of the present invention are also those agents with protease-sensitive material capsules which are hydrolyzed, for example, by proteins of the invention at an intended time and release their contents. Polypeptides of the invention can thus also be used for inactivation, activation or release reactions, in particular in multiphase agents.
  • a further embodiment of this subject matter accordingly also represents the use of a polypeptide according to the invention for the activation, deactivation or release of ingredients of detergents or cleaners.
  • the agent with a polypeptide of the invention is designed so that it can be used regularly as a care product, for example by added to the washing process, applied after washing or applied independently of the washing.
  • the desired effect is to maintain a smooth surface texture of the fabric over a long period of time and / or to prevent and / or reduce damage to the fabric.
  • a separate subject of the invention are processes for the automated cleaning of textiles or of hard surfaces, in which at least one of the process steps uses a polypeptide according to the invention.
  • polypeptide according to the invention is used in an amount of 40 ⁇ g to 4 g, preferably from 50 ⁇ g to 3 g, particularly preferably from 100 ⁇ g to 2 g and very particularly preferably from 200 ⁇ g to 1 g per application becomes. Included are all integer and non-integer values lying between these numbers.
  • Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned in a plurality of process steps and washed off after the action time, or that the items to be cleaned are otherwise treated with a detergent or a solution of this agent.
  • a single substep of such a process for the mechanical cleaning of textiles may be that, if desired, in addition to stabilizing compounds, Salts or buffer substances is the only detergent-active component of a polypeptide of the invention is applied. This represents a particularly preferred embodiment of the present invention.
  • the relevant polypeptides according to the invention are provided in the context of one of the formulations set forth above for agents according to the invention, preferably detergents or cleaners according to the invention.
  • agents according to the invention preferably detergents or cleaners according to the invention.
  • a separate subject of the invention is the use of an inventive alkaline protease described above for cleaning textiles or hard surfaces.
  • Proteases according to the invention can be used, in particular according to the properties described above and the processes described above, to eliminate proteinaceous impurities from textiles or from hard surfaces.
  • Embodiments include, for example, hand washing, manual removal of stains from fabrics or hard surfaces, or use in conjunction with a machine process.
  • alkaline proteases according to the invention are provided in the context of one of the formulations set forth above for compositions according to the invention, preferably detergents or cleaners.
  • Another object of the present invention is also a product comprising a composition according to the invention or a detergent or cleaning agent according to the invention, in particular a hard surface cleaner according to the invention, and a spray dispenser.
  • the product may be both a single-chamber and a multi-chamber container, in particular a two-chamber container.
  • the spray dispenser is preferably a manually activated spray dispenser, in particular selected from the group consisting of aerosol spray dispensers (also known as spray can), pressure-building spray dispensers, pump spray dispensers and trigger spray dispensers, in particular pump spray dispensers and trigger spray dispensers with a transparent polyethylene or polyethylene terephthalate container.
  • Spray dispensers are described in more detail in WO 96/04940 (Procter & Gamble) and the US patents cited therein about spray dispensers, to which reference is made in this regard and the contents of which are hereby incorporated by reference.
  • Triggersprühspender and pump sprayer have over compressed gas tanks the advantage that no propellant must be used.
  • the enzyme in this embodiment may optionally also be added to the composition in a form immobilized on particles and thus metered as cleaning foam.
  • Example 1 Isolation and identification of a proteolytically active bacterial strain
  • 0.1 g of a soil sample was suspended in 1 ml of sterile NaCl and on milk powder agar plates (1, 5% agar, 0.1% K 2 HPO4, 0.5% yeast extract, 1% peptone, 1% milk powder, 0.02% MgSO 4 * 7H 2 O, 0.4% Na 2 CO 3 , pH 10) and incubated at 30 °.
  • a proteolytically active bacterium was isolated on the basis of a clarification farm, which was named Bacillus gibsonii by the German Collection of Microorganisms and Cell Cultures (DSMZ). was identified.
  • Table 1 Microbiological properties of the Bacillus gibsonii strain
  • the proteolytically active bacterium was in TBY medium (0.5% NaCl, 0.5% yeast extract, 1% tryptone, pH 7.4) cultured for 16 hours at 3O 0 C.
  • the total DNA of this bacterium was isolated, digested with the restriction enzyme Sau 3A and the resulting fragments cloned into the vector pAWA22.
  • This vector was transformed into the host strain Bacillus subtilis DB 104 (Kawamura and Doi (1984), J. Bacteriol., Vol. 160 (1), pp. 442-444).
  • the transformants were first on DM3 medium (8 g / l agar, 0.5 M succinic acid, 3.5 g / l K 2 HPO 4 , 1, 5 g / l KH 2 PO 4 , 20 mM MgCl 2 , 5 g / l Casiaminoacids, 5 g / l yeast extract, 6 g / l glucose,
  • proteolytically active clones were determined by their Lysies identified. One of the resulting proteolytically active clones was selected, the plasmid was isolated and the insert was sequenced according to standard methods.
  • the approximately 1.5 kb insert contained an open reading frame of approximately 1.2 kb. Whose sequence is in the sequence listing under the name SEQ ID NO. 1 indicated. It covers 1152 bp.
  • the deduced amino acid sequence comprises 383 amino acids followed by a stop codon. It is in the sequence listing under SEQ ID NO. 2 indicated. Of these, the first 114 amino acids are unlikely to be present in the mature protein, so the mature protein is expected to be 269 amino acids in length.
  • Table 2 Homology of the alkaline protease from Bacillus gibsonii to the nearest similar proteins. In this mean:
  • amino acid sequences of these proteases are also compared with one another in the alignment of FIG.
  • standardized contaminated textiles were used by the Eidgenössische Material-Prüfungs- und-Versuchsweg, St. Gallen, Switzerland (EMPA), or the Waschereiutzs GmbH, Krefeld.
  • the following stains and textiles were used: A (grass on cotton, EMPA 164), B (milk / oil on cotton, PC-10), C (whole / soot on cotton, 10N), D (chocolate milk / soot on cotton, C-03), E (cocoa, EMPA 112) and F (blood / milk on cotton, C-5 (044)).
  • control detergent used was a detergent base formulation of the following composition (all).
  • Ci ⁇ - cis fatty alcohol sulfate sodium salt
  • Ci 2 -C 8 fatty alcohol with 7 EO 20%
  • the detergent base recipe was for the different
  • subtilisin TI-1 (WO03 / 054184), subtilisin TII-5 (WO03 / 054185), ⁇ . / enfrvs-Alkaline Protease F 49 (WO 95/23221) or the inventive
  • protease of the invention from ß. gibsonii at 4O 0 C on some soils exceeds the homologous proteases HP302, TII-5 and TI-1 (stains B and D) and with respect to the other soils give comparable values to these proteases and that the protease according to the invention in relation to all stains with the exception of soiling C gives better values than the established protease ⁇ . / enfrvs Alkaline Protease F49.
  • Example 3 The experiment was carried out essentially as described in Example 3. The following stains and textiles were used: A (grass on cotton, EMPA 164), B (milk / oil on cotton, PC-10), C (whole / soot on cotton, 10N), D (chocolate milk / soot on cotton, C-03), E (cocoa, EMPA 112) and F (blood / milk on cotton, C-5 (044)).
  • the control detergent used was a detergent base formulation of the following composition (all figures in percent by weight): 0.3- 0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol, 0 , 3-0.5% ethanol, 4-7% FAEOS, 24-28% nonionic surfactants, 1% boric acid, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% coconut fatty acids, 0 , 5% HEDP, 0-0.4% PVP, 0-0.05% optical brightener, 0-0.001% dye, remainder demineralized water
  • the detergent base formulation was treated with the following proteases for the different test series: Subtilisin HP302 (DE102006022216), subtilisin TI-1 (WO03 / 054184), subtilisin TII-5 (WO03 / 054185), ⁇ . / enfrvs-Alkaline Protease F 49 (WO 95/23221) or the protease according to the invention
  • the whiteness of the washed fabrics was measured.
  • the measurement was carried out on a Minolta CM508d spectrometer, illuminant D65, 10.
  • the device is calibrated beforehand with a supplied white standard.
  • the results obtained are summarized as percent remission, that is to say as percentages in comparison to the white standard, together with the respective initial values in Table 4. Indicated are the mean values from 3 measurements each. They allow a direct conclusion on the contribution of the enzyme contained to the washing performance of the agent used.
  • protease of the invention from ß. gibsonii at 4O 0 C in a liquid detergent with respect to all soiling only with the exception of soiling E (cocoa), the homologous proteases Subtilisin HP302, Subtilisin TII-5 and Subtilisin TI-1 in part significantly exceeds.
  • FIG. 1 Alignment of the amino acid sequences of the invention
  • FIG. 2 The pBC16-derived expression vector pAWA22, which has a

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • General Health & Medical Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Animal Behavior & Ethology (AREA)
  • Organic Chemistry (AREA)
  • Wood Science & Technology (AREA)
  • Engineering & Computer Science (AREA)
  • Dermatology (AREA)
  • Genetics & Genomics (AREA)
  • Zoology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • Biomedical Technology (AREA)
  • Biotechnology (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Microbiology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Medicinal Chemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • Oral & Maxillofacial Surgery (AREA)
  • Birds (AREA)
  • Epidemiology (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Detergent Compositions (AREA)

Abstract

La présente invention concerne une nouvelle protéase alcaline du type subtilisine issue de Bacillus gibsonii, ainsi que des protéines suffisamment apparentées et leurs dérivés. L'invention concerne en outre des détergents et des nettoyants contenant cette nouvelle protéase alcaline du type subtilisine, des protéines suffisamment apparentées et leurs dérivés, des procédés de lavage et de nettoyage correspondants et l'utilisation de cette protéase, desdites protéines et desdits dérivés dans des détergents et des nettoyants, ainsi que d'autres possibilités d'utilisation techniques.
EP07847839A 2007-01-16 2007-12-05 Nouvelle protéase alcaline issue de bacillus gibsonii et détergents et nettoyants contenant cette nouvelle protéase alcaline Withdrawn EP2054513A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE102007003143A DE102007003143A1 (de) 2007-01-16 2007-01-16 Neue Alkalische Protease aus Bacillus gibsonii und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease
PCT/EP2007/063346 WO2008086916A1 (fr) 2007-01-16 2007-12-05 Nouvelle protéase alcaline issue de bacillus gibsonii et détergents et nettoyants contenant cette nouvelle protéase alcaline

Publications (1)

Publication Number Publication Date
EP2054513A1 true EP2054513A1 (fr) 2009-05-06

Family

ID=39400619

Family Applications (1)

Application Number Title Priority Date Filing Date
EP07847839A Withdrawn EP2054513A1 (fr) 2007-01-16 2007-12-05 Nouvelle protéase alcaline issue de bacillus gibsonii et détergents et nettoyants contenant cette nouvelle protéase alcaline

Country Status (4)

Country Link
US (1) US20090275493A1 (fr)
EP (1) EP2054513A1 (fr)
DE (1) DE102007003143A1 (fr)
WO (1) WO2008086916A1 (fr)

Families Citing this family (86)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE102007038031A1 (de) * 2007-08-10 2009-06-04 Henkel Ag & Co. Kgaa Mittel enthaltend Proteasen
DE102008038479A1 (de) 2008-08-20 2010-02-25 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft
DE102008052529A1 (de) 2008-10-21 2010-04-22 Henkel Ag & Co. Kgaa Expressionsverstärkte Nukleinsäuren
DE102008059447A1 (de) 2008-11-27 2010-06-02 Henkel Ag & Co. Kgaa Wasch- und Reinigungsmittel enthaltend Proteasen aus Bacillus pumilus
DE102008062772A1 (de) 2008-12-18 2010-06-24 Henkel Ag & Co. Kgaa Desinfektion von Viren an Textilien und harten Oberflächen
DE102009029513A1 (de) 2009-09-16 2011-03-24 Henkel Ag & Co. Kgaa Lagerstabiles flüssiges Wasch- oder Reinigungsmittel enthaltend Proteasen
DE102009045064A1 (de) 2009-09-28 2011-03-31 Henkel Ag & Co. Kgaa Stabilisierte enzymatische Zusammensetzung
DE102010002196A1 (de) 2010-02-22 2011-11-17 Henkel Ag & Co. Kgaa Kartusche für ein wasserführendes Haushaltsgerät
DE102010002762A1 (de) * 2010-03-11 2012-03-08 Henkel Ag & Co. Kgaa Leistungsverbesserte Proteasevariante
DE102010038497A1 (de) 2010-07-27 2012-02-02 Henkel Ag & Co. Kgaa Stabilisierte flüssige enzymhaltige Tensidzubereitung
DE102010038498A1 (de) 2010-07-27 2012-02-02 Henkel Ag & Co. Kgaa Stabilisierte flüssige enzymhaltige Tensidzubereitung
DE102010038501A1 (de) 2010-07-27 2012-02-02 Henkel Ag & Co. Kgaa Stabilisierte flüssige enzymhaltige Tensidzubereitung
DE102010038496A1 (de) 2010-07-27 2012-02-02 Henkel Ag & Co. Kgaa Stabilisierte flüssige enzymhaltige Tensidzubereitung
DE102010038502A1 (de) 2010-07-27 2012-02-02 Henkel Ag & Co. Kgaa Stabilisierte flüssige enzymhaltige Tensidzubereitung
DE102010038499A1 (de) 2010-07-27 2012-02-02 Henkel Ag & Co. Kgaa Stabilisierte flüssige enzymhaltige Tensidzubereitung
DE102010043934A1 (de) 2010-11-15 2012-05-16 Henkel Ag & Co. Kgaa Stabilisierte flüssige enzymhaltige Tensidzubereitung
DE102010063743A1 (de) * 2010-12-21 2012-06-21 Henkel Ag & Co. Kgaa Flüssige Tensidzubereitung enthaltend Lipase und Phosphonat
DE102011007313A1 (de) 2011-04-13 2012-10-18 Henkel Ag & Co. Kgaa Expressionsverfahren
DE102011007627A1 (de) 2011-04-18 2012-10-18 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit fester Enzymkonfektionierung
DE102011007695A1 (de) 2011-04-19 2012-10-25 Henkel Ag & Co. Kgaa Phosphatfreies Geschirrspülmittel
DE102011118032A1 (de) 2011-05-31 2012-12-06 Henkel Ag & Co. Kgaa Expressionsvektoren zur verbesserten Proteinsekretion
DE102011118037A1 (de) 2011-06-16 2012-12-20 Henkel Ag & Co. Kgaa Geschirrspülmittel mit Bleichkatalysator und Protease
DE102011118027A1 (de) 2011-09-12 2013-03-14 Henkel Ag & Co. Kgaa Verfahren zur Anpassung eines Hydrolytischen Enzyms an eine das hydrolytische Enzym stabilisierende Komponente
DE102012201297A1 (de) 2012-01-31 2013-08-01 Basf Se Expressionsverfahren
DE102012215107A1 (de) 2012-08-24 2014-02-27 Basf Se Festes Geschirrspülmittel mit verbesserter Proteaseleistung
DE102012224038A1 (de) 2012-12-20 2014-06-26 Henkel Ag & Co. Kgaa Enzymhaltige Granulatzusammensetzung
EP3080263B1 (fr) 2013-12-13 2019-07-03 Danisco US Inc. Sérines protéases du clade du bacillus gibsonii
DE102014204602A1 (de) 2014-03-12 2015-09-17 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit hydrolytisch aktivem Enzym und Steroidsäure
DE102014004533A1 (de) 2014-03-31 2015-10-01 Henkel Ag & Co. Kgaa Dosierungsform für Wasch- oder Reinigungsmittel
DE102014209241A1 (de) 2014-05-15 2015-11-19 Henkel Ag & Co. Kgaa Wasch- und Reinigungsmittel mit erhöhter Bleichleistung
DE102014218569A1 (de) 2014-09-16 2016-03-17 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit hydrolytisch aktivem Enzym und Trehaloseverbindung
JP6444104B2 (ja) * 2014-09-17 2018-12-26 シーバイエス株式会社 洗濯用液体殺菌洗浄剤組成物およびそれを用いた繊維品の非エンベロープウイルスの不活化方法
DE102014224825A1 (de) * 2014-12-04 2016-06-09 Henkel Ag & Co. Kgaa Proteasevarianten mit verbesserter Waschleistung
JP7134629B2 (ja) 2015-06-17 2022-09-12 ダニスコ・ユーエス・インク 改変プロペプチド領域を備えるプロテアーゼ
DE102017215015A1 (de) 2017-08-28 2019-02-28 Henkel Ag & Co. Kgaa Verfahren zur verbesserten Expression von Enzymen
EP3717643A1 (fr) 2017-11-29 2020-10-07 Danisco US Inc. Variants de subtilisine à stabilité améliorée
WO2019245704A1 (fr) 2018-06-19 2019-12-26 Danisco Us Inc Variantes de subtilisine
CN112204138A (zh) 2018-06-19 2021-01-08 宝洁公司 自动盘碟洗涤剂组合物
US20210363470A1 (en) 2018-06-19 2021-11-25 Danisco Us Inc Subtilisin variants
CA3102151C (fr) 2018-06-19 2023-09-26 The Procter & Gamble Company Composition de detergent pour lave-vaisselle automatique
EP3887515A1 (fr) 2018-11-28 2021-10-06 Danisco US Inc. Variants de subtilisine à stabilité améliorée
EP3666872B1 (fr) 2018-12-12 2021-08-11 Henkel AG & Co. KGaA Copolymères acryliques phosphonés pour hydrophilisation de surface
US11193095B2 (en) * 2019-01-14 2021-12-07 Wizard Labs, Llc Rinsing solution for metal blades
US11312922B2 (en) 2019-04-12 2022-04-26 Ecolab Usa Inc. Antimicrobial multi-purpose cleaner comprising a sulfonic acid-containing surfactant and methods of making and using the same
EP3976776A1 (fr) 2019-05-24 2022-04-06 Danisco US Inc. Variants de subtilisine et procédés d'utilisation
EP3770240A1 (fr) 2019-07-22 2021-01-27 Henkel AG & Co. KGaA Lave-vaisselle pourvu de catalyseur de blanchiment et protéase de bacillus gibsonii
EP3770237A1 (fr) 2019-07-22 2021-01-27 Henkel AG & Co. KGaA Agent de lavage et de nettoyage à stabilité de l'enzyme améliorée
EP3770238A1 (fr) 2019-07-22 2021-01-27 Henkel AG & Co. KGaA Agent de lavage et de nettoyage comprenant de la protéase et de l'amylase
DE102019126683A1 (de) 2019-10-02 2021-04-08 Henkel Ag & Co. Kgaa Copolymere zur Verbesserung der Lagerstabilität von Enzymen in Wasch- und Reinigungsmitteln
DE102020204505A1 (de) 2020-04-07 2021-10-07 Henkel Ag & Co. Kgaa Wasch-/Pflegeartikel umfassend Pheromone
DE102020205400A1 (de) 2020-04-29 2021-11-04 Henkel Ag & Co. Kgaa Hochalkalisches Textilwaschmittel mit Protease
DE102020205381A1 (de) 2020-04-29 2021-11-04 Henkel Ag & Co. Kgaa Hochalkalisches Textilwaschmittel mit Protease
DE102020131794A1 (de) 2020-12-01 2022-06-02 Henkel Ag & Co. Kgaa Verbesserte Reinigung durch Hydrogencarbonat im maschinellen Geschirrspülmittel
DE102021213462A1 (de) 2021-11-30 2023-06-01 Henkel Ag & Co. Kgaa Verfahren zur Reinigung einer elektromotorisch betriebenen Küchenmaschine
WO2022128620A1 (fr) 2020-12-14 2022-06-23 Henkel Ag & Co. Kgaa Procédé de nettoyage d'un robot de cuisine entraîné par un moteur électrique
EP4011256A1 (fr) 2020-12-14 2022-06-15 Henkel AG & Co. KGaA Procédé de nettoyage d'un robot de cuisine électrique
EP4012011A1 (fr) 2020-12-14 2022-06-15 Henkel AG & Co. KGaA Détergeant, en particulier pour un robot de cuisine
DE102020134229A1 (de) 2020-12-18 2022-06-23 Henkel Ag & Co. Kgaa Getränktes Reinigungstuch
DE102021116100A1 (de) 2021-06-22 2022-12-22 Henkel Ag & Co. Kgaa Blooming-Effekt durch den Einsatz von löslichen Waschtüchern
EP4134423A1 (fr) 2021-08-12 2023-02-15 Henkel AG & Co. KGaA Composition de prétraitement de blanchisserie pulvérisable
WO2023114936A2 (fr) 2021-12-16 2023-06-22 Danisco Us Inc. Variants de subtilisine et procédés d'utilisation
CN118369414A (zh) 2021-12-16 2024-07-19 宝洁公司 包含蛋白酶的自动盘碟洗涤组合物
WO2023114939A2 (fr) 2021-12-16 2023-06-22 Danisco Us Inc. Variants de subtilisine et procédés d'utilisation
CA3240638A1 (fr) 2021-12-16 2023-06-22 Michelle Jackson Composition de soin textile et menager comprenant une protease
WO2023161182A1 (fr) 2022-02-24 2023-08-31 Evonik Operations Gmbh Composition d'origine biologique
DE102022107827A1 (de) 2022-04-01 2023-10-05 Henkel Ag & Co. Kgaa Haarentfernung durch Waschmittel/-Additive enthaltend Enzyme
DE102022205593A1 (de) 2022-06-01 2023-12-07 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel mit verbesserter enzymstabilität
DE102022205591A1 (de) 2022-06-01 2023-12-07 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel mit verbesserter enzymstabilität
DE102022205594A1 (de) 2022-06-01 2023-12-07 Henkel Ag & Co. Kgaa Leistungsverbesserte und lagerstabile protease-varianten
DE102022205588A1 (de) 2022-06-01 2023-12-07 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel mit verbesserter enzymstabilität
WO2024002738A1 (fr) 2022-06-28 2024-01-04 Evonik Operations Gmbh Composition contenant un biotensioactif et de la persicomycine
DE102022206585A1 (de) 2022-06-29 2024-01-04 Henkel Ag & Co. Kgaa Reinigungsmittel mit verbesserter proteolytischer reinigungsleistung
CN115156169B (zh) * 2022-07-06 2023-07-28 杭州临港化纤有限公司 一种假捻盘的清洗工艺
WO2024037686A1 (fr) 2022-08-16 2024-02-22 Henkel Ag & Co. Kgaa Variants x de protéase à performance améliorée
DE102022208890A1 (de) 2022-08-16 2024-02-22 Henkel Ag & Co. Kgaa Leistungsverbesserte protease-varianten ix
DE102022208891A1 (de) 2022-08-16 2024-02-22 Henkel Ag & Co. Kgaa Leistungsverbesserte protease-varianten x
WO2024037685A1 (fr) 2022-08-16 2024-02-22 Henkel Ag & Co. Kgaa Variants ix de protéase à performance améliorée
EP4324900A1 (fr) 2022-08-17 2024-02-21 Henkel AG & Co. KGaA Composition détergente comprenant des enzymes
DE102022209246A1 (de) 2022-09-06 2024-03-07 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel enthaltend tannase ii
DE102022209245A1 (de) 2022-09-06 2024-03-07 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel enthaltend tannase i
WO2024102698A1 (fr) 2022-11-09 2024-05-16 Danisco Us Inc. Variants de subtilisine et procédés d'utilisation
WO2024115213A1 (fr) 2022-11-30 2024-06-06 Evonik Operations Gmbh Capsule à détergent comprenant des biotensioactifs
DE102022131732A1 (de) 2022-11-30 2024-06-06 Henkel Ag & Co. Kgaa Verbesserte Waschleistung durch den Einsatz einer Protease fusioniert mit speziellem Adhäsionsvermittlerpeptid
DE102022213537A1 (de) 2022-12-13 2024-06-13 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel enthaltend protease
DE102022213538A1 (de) 2022-12-13 2024-06-13 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel enthaltend protease
DE102023200106A1 (de) 2023-01-10 2024-07-11 Henkel Ag & Co. Kgaa Enzymhaltiges wasch- und reinigungsmittel

Family Cites Families (77)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB1154730A (en) 1965-10-08 1969-06-11 Ici Ltd Improvements in the Laundering of Synthetic Polymeric Textile Materials
GB1234445A (fr) 1967-10-03 1971-06-03
GB1377092A (en) 1971-01-13 1974-12-11 Unilever Ltd Detergent compositions
CA989557A (en) 1971-10-28 1976-05-25 The Procter And Gamble Company Compositions and process for imparting renewable soil release finish to polyester-containing fabrics
US4116885A (en) 1977-09-23 1978-09-26 The Procter & Gamble Company Anionic surfactant-containing detergent compositions having soil-release properties
CA1190695A (fr) 1981-05-14 1985-07-16 George J. Stockburger Agent anionique pour le traitement des textiles
DE3324258A1 (de) 1982-07-09 1984-01-12 Colgate-Palmolive Co., 10022 New York, N.Y. Nichtionogene waschmittelzusammensetzung mit verbesserter schmutzauswaschbarkeit
DE3413571A1 (de) * 1984-04-11 1985-10-24 Hoechst Ag, 6230 Frankfurt Verwendung von kristallinen schichtfoermigen natriumsilikaten zur wasserenthaertung und verfahren zur wasserenthaertung
ATE73150T1 (de) 1984-12-21 1992-03-15 Procter & Gamble Blockpolyester und aehnliche verbindungen, verwendbar als verschmutzungsentferner in waschmittelzusammensetzungen.
US4711730A (en) 1986-04-15 1987-12-08 The Procter & Gamble Company Capped 1,2-propylene terephthalate-polyoxyethylene terephthalate polyesters useful as soil release agents
US4713194A (en) 1986-04-15 1987-12-15 The Procter & Gamble Company Block polyester and like compounds having branched hydrophilic capping groups useful as soil release agents in detergent compositions
GB8617255D0 (en) 1986-07-15 1986-08-20 Procter & Gamble Ltd Laundry compositions
GB8629936D0 (en) 1986-12-15 1987-01-28 Procter & Gamble Laundry compositions
US4721580A (en) 1987-01-07 1988-01-26 The Procter & Gamble Company Anionic end-capped oligomeric esters as soil release agents in detergent compositions
ATE134669T1 (de) 1988-08-26 1996-03-15 Procter & Gamble Schmutzabweisende mittel mit von allylgruppen abgeleiteten sulphonierten endgruppen
ES2144990T3 (es) 1989-08-25 2000-07-01 Henkel Of America Inc Enzima proteolitica alcalina y metodo de produccion.
IT1249883B (it) 1990-08-13 1995-03-30 Ferruzzi Ricerca & Tec Agenti sequestranti del calcio a base di carboidrati ossidati e loro impiego come builder per detergenti
US5230891A (en) 1990-08-20 1993-07-27 Kanebo Limited Modified protease, method of producing the same and cosmetic products containing the modified protease
US5340735A (en) 1991-05-29 1994-08-23 Cognis, Inc. Bacillus lentus alkaline protease variants with increased stability
DE4224125A1 (de) 1991-07-27 1993-01-28 Solvay Enzymes Gmbh & Co Kg Verfahren zur verbesserung der stabilitaet von enzymen und stabilisierte enzyme
ATE155165T1 (de) 1991-07-31 1997-07-15 Ausimont Spa Verfahren zur erhöhung der bleichwirksamkeit eines inorganischen persalzes
WO1994028102A1 (fr) 1993-05-20 1994-12-08 The Procter & Gamble Company Composes de blanchiment comprenant du n-acyl caprolactame, utiles dans le lavage a la main ou dans d'autres systemes de nettoyage de textiles a faible teneur en eau
CN1066715C (zh) 1993-05-20 2001-06-06 普罗格特-甘布尔公司 包含取代的苯甲酰基己内酰胺漂白活化剂的漂白化合物
AU6949194A (en) 1993-05-20 1994-12-20 Procter & Gamble Company, The Bleaching compositions comprising n-acyl caprolactam activators
US5405413A (en) 1993-06-24 1995-04-11 The Procter & Gamble Co. Bleaching compounds comprising acyl valerolactam bleach activators
DE4338922A1 (de) 1993-11-15 1995-05-18 Degussa Aktivatoren für anorganische Persauerstoffverbindungen
AU1074295A (en) 1993-11-25 1995-06-13 Warwick International Group Limited Bleaching compositions
US5534196A (en) 1993-12-23 1996-07-09 The Procter & Gamble Co. Process for making lactam bleach activator containing particles
DE4344215A1 (de) * 1993-12-23 1995-06-29 Cognis Bio Umwelt Silberkorrosionsschutzmittelhaltige Enzymzubereitung
US5605793A (en) 1994-02-17 1997-02-25 Affymax Technologies N.V. Methods for in vitro recombination
US6335160B1 (en) 1995-02-17 2002-01-01 Maxygen, Inc. Methods and compositions for polypeptide engineering
US6117679A (en) 1994-02-17 2000-09-12 Maxygen, Inc. Methods for generating polynucleotides having desired characteristics by iterative selection and recombination
DK0701605T3 (da) 1994-02-24 2008-07-28 Henkel Ag & Co Kgaa Forbedrede enzymer og detergenter indeholdende disse
EP0759947B1 (fr) 1994-05-20 2000-07-19 Henkel Kommanditgesellschaft auf Aktien Polyesters facilitant le lavage
US5602004A (en) 1994-07-20 1997-02-11 Novo Nordisk Biotech, Inc. Thermophilic fungal expression system
DE4426216A1 (de) * 1994-07-23 1996-01-25 Merck Patent Gmbh Benzyliden-Norcampher-Derivate
DE4426215A1 (de) * 1994-07-23 1996-01-25 Merck Patent Gmbh Ketotricyclo [5.2.1.0] decan-Derivate
JP3810433B2 (ja) 1994-08-12 2006-08-16 ザ プロクター アンド ギャンブル カンパニー 非生物表面で悪臭印象を減少させるための組成物
DE4443177A1 (de) 1994-12-05 1996-06-13 Henkel Kgaa Aktivatormischungen für anorganische Perverbindungen
GB9503474D0 (en) 1995-02-22 1995-04-12 Ciba Geigy Ag Compounds and their use
DE19601063A1 (de) 1995-03-06 1996-09-12 Hoechst Ag Kristallines Natriumschichtsilikat
EP1683860B1 (fr) 1995-03-17 2013-10-23 Novozymes A/S Nouvelles endoglucanases
CA2219245A1 (fr) 1995-04-28 1996-10-31 Genencor International, Inc. Detergents comprenant des cellulases
GB9514090D0 (en) 1995-07-11 1995-09-13 Cerestar Holding Bv Non-catalysed oxidation of maltodextrin with an oxygen containing oxidant
DE19530816A1 (de) * 1995-08-23 1997-02-27 Cognis Bio Umwelt Verwendung von mutierter Subtilisin-Protease in kosmetischen Produkten
BR9611114A (pt) 1995-10-17 1999-07-13 Rohm Enzyme Finland Oy Celulases os genes codificando-as e os usos das mesmas
US5741767A (en) 1995-11-16 1998-04-21 Lever Brothers Company, Division Of Conopco, Inc. Peracid based dishwashing detergent composition
DE69615582T2 (de) 1995-12-29 2002-07-11 Novozymes A/S, Bagsvaerd Enzym enthaltende teilchen und flüssiges reinigungsmittelkonzentrat
DE19600018A1 (de) 1996-01-03 1997-07-10 Henkel Kgaa Waschmittel mit bestimmten oxidierten Oligosacchariden
FR2745014B1 (fr) * 1996-02-20 1998-04-03 Rhone Poulenc Chimie Procede de traitement antisalissure des articles a base de coton tisse
DE19616767A1 (de) 1996-04-26 1997-11-06 Henkel Kgaa Bleichaktivatoren für Wasch- und Reinigungsmittel
DE19616770A1 (de) 1996-04-26 1997-11-06 Henkel Kgaa Acyllactame als Bleichaktivatoren für Wasch- und Reinigungsmittel
DE19616769A1 (de) 1996-04-26 1997-11-06 Henkel Kgaa Acylacetale als Bleichaktivatoren für Wasch- und Reinigungsmittel
DE19616693A1 (de) * 1996-04-26 1997-11-06 Henkel Kgaa Enolester als Bleichaktivatoren für Wasch- und Reinigungsmittel
EP1293504A3 (fr) 1996-07-08 2003-11-05 Ciba SC Holding AG Dérivés de la triazine en tant que UV-filtre dans des compositions cosmétiques
CN101085985B (zh) 1996-09-17 2012-05-16 诺沃奇梅兹有限公司 纤维素酶变体
DE19709284A1 (de) 1997-03-07 1998-09-10 Henkel Kgaa Katalytisch aktive Wirkstoffkombination zur Verstärkung der Bleichwirkung
DE19712033A1 (de) 1997-03-21 1998-09-24 Basf Ag Photostabile UV-Filter enthaltende kosmetische und pharmazeutische Zubereitungen
DE19732751A1 (de) * 1997-07-30 1999-02-04 Henkel Kgaa Neue Beta-Glucanase aus Bacillus
KR20010052223A (ko) 1998-03-26 2001-06-25 데이비드 엠 모이어 아미노산 결실 및 치환을 갖는 세린 프로테아제 변이체
WO1999057258A1 (fr) 1998-05-01 1999-11-11 The Procter & Gamble Company Detergent de lavage et/ou compositions respectant les tissus comprenant une transferase modifiee
DE19918267A1 (de) 1999-04-22 2000-10-26 Henkel Kgaa Handgeschirrspülmittel mit Mikrokapseln
AU5928100A (en) 1999-07-22 2001-02-13 Procter & Gamble Company, The Subtilisin protease variants having amino acid deletions and substitutions in defined epitope regions
DE19956382A1 (de) 1999-11-24 2001-05-31 Henkel Kgaa Verfahren zur Herstellung von mikroverkapselten Enzymen
DE10019881A1 (de) * 2000-04-20 2001-11-15 Gerhard Miksch Verfahren zur Überexpression und extrazellulären Produktion bakterieller Phytasen in Escherichia coli
ATE307882T1 (de) * 2000-07-28 2005-11-15 Henkel Kgaa Neues amylolytisches enzym aus bacillus sp. a 7-7 (dsm 12368) sowie wasch- und reinigungsmittel mit diesem neuen amylolytischen enzym
ATE373716T1 (de) 2000-11-28 2007-10-15 Henkel Kgaa Cyclodextrin -glucanotransferase(cg tase) aus bacillus agaradherens(dsm 9948)sowie wasch-und reinigungsmittel mit dieser neuen cyclodextrin- glucanotransferase
DE10121463A1 (de) 2001-05-02 2003-02-27 Henkel Kgaa Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten
DE10131441A1 (de) * 2001-06-29 2003-01-30 Henkel Kgaa Eine neue Gruppe von alpha-Amylasen sowie ein Verfahren zur Identifizierung und Gewinnung neuer alpha-Amylasen
DE10138753B4 (de) 2001-08-07 2017-07-20 Henkel Ag & Co. Kgaa Wasch- und Reinigungsmittel mit Hybrid-Alpha-Amylasen
DE10153792A1 (de) 2001-10-31 2003-05-22 Henkel Kgaa Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten
DE10162727A1 (de) 2001-12-20 2003-07-10 Henkel Kgaa Neue Alkalische Protease aus Bacillus gibsonii (DSM 14391) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE10162728A1 (de) * 2001-12-20 2003-07-10 Henkel Kgaa Neue Alkalische Protease aus Bacillus gibsonii (DSM 14393) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE10163748A1 (de) * 2001-12-21 2003-07-17 Henkel Kgaa Neue Glykosylhydrolasen
DE10163883A1 (de) 2001-12-22 2003-07-10 Henkel Kgaa Neue Alkalische Protease aus Bacillus sp. (DSM 14390) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE10163884A1 (de) 2001-12-22 2003-07-10 Henkel Kgaa Neue Alkalische Protease aus Bacillus sp. (DSM 14392) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE102006022216A1 (de) 2006-05-11 2007-11-15 Henkel Kgaa Neue Alkalische Protease aus Bacillus gibsonii und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO2008086916A1 *

Also Published As

Publication number Publication date
US20090275493A1 (en) 2009-11-05
DE102007003143A1 (de) 2008-07-17
WO2008086916A1 (fr) 2008-07-24

Similar Documents

Publication Publication Date Title
EP1737952B1 (fr) Nouvelles proteases alcalines et agents de lavage et detergents renfermant celles-ci
EP2054513A1 (fr) Nouvelle protéase alcaline issue de bacillus gibsonii et détergents et nettoyants contenant cette nouvelle protéase alcaline
EP1385943B1 (fr) Nouvelles variantes de proteases alcalines et detergents contenant ces nouvelles variantes
EP1697510B1 (fr) Nouvelle protease alcaline et produits detergents et nettoyants contenant cette nouvelle protease alcaline
WO2007131657A2 (fr) Nouvelle protéase alcaline dérivée de bacillus gibsonii et produits détergents et nettoyants contenant cette nouvelle protéase alcaline
EP2016175A1 (fr) Subtilisine dérivée de bacillus pumilus et produits détergents et nettoyants contenant cette nouvelle subtilisine
EP1456368A2 (fr) Nouvelle protease alcaline obtenue a partir de bacillus sp. (dsm 14392) et agents de lavage et de nettoyage contenant cette protease alcaline
WO2003054184A9 (fr) Nouvelle protease alcaline extraite de bacillus gibsonii (dsm 14393) et agents de lavage et de nettoyage contenant cette nouvelle protease alcaline
WO2003054185A1 (fr) Nouvelle protease alcaline issue de bacillus gibsonii (dsm 14391) et agents de lavage et de nettoyage contenant cette nouvelle protease alcaline
EP1456384A2 (fr) NOUVELLE PROTEASE ALCALINE OBTENUE A PARTIR DE i BACILLUS SP /i (DSM 14390) ET AGENTS DE LAVAGE ET DE NETTOYAGE CONTENANT CETTE PROTEASE ALCALINE
DE10064983A1 (de) Neue Alkalische Protease aus Bacillus alcalophilus (DSM 11233)
EP1442120A2 (fr) Variants de protease alcaline et detergents et produits de lavage contenant ces variants
EP1789546A2 (fr) Variantes de proteases alcalines de type subtilisin a performances ameliorees et detergents et produits de nettoyage contenant lesdites variantes
DE102005037659A1 (de) Verwendung von Esterasen zur Spaltung von Kunststoffen
DE102007049830A1 (de) Neue Proteinvarianten durch zirkulare Permutation
DE10309803B4 (de) α-Amylase-Varianten mit verbesserter Alkaliaktivität
WO2007045398A2 (fr) Nouvelles cholines oxydases a specificite de substrat modifiee
WO2009053157A1 (fr) Subtilisine issue de bacillus pumilus, et agents de lavage et de nettoyage contenant cette subtilisine

Legal Events

Date Code Title Description
PUAI Public reference made under article 153(3) epc to a published international application that has entered the european phase

Free format text: ORIGINAL CODE: 0009012

17P Request for examination filed

Effective date: 20090313

AK Designated contracting states

Kind code of ref document: A1

Designated state(s): AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HU IE IS IT LI LT LU LV MC MT NL PL PT RO SE SI SK TR

AX Request for extension of the european patent

Extension state: AL BA HR MK RS

17Q First examination report despatched

Effective date: 20090707

RIN1 Information on inventor provided before grant (corrected)

Inventor name: BESSLER, CORNELIUS

Inventor name: MAURER, KARL-HEINZ

Inventor name: MERKEL, MARION

Inventor name: ENGELSKIRCHEN, JULIA

Inventor name: WIELAND, SUSANNE

Inventor name: SIEGERT, PETRA

RIN1 Information on inventor provided before grant (corrected)

Inventor name: BESSLER, CORNELIUS

Inventor name: MAURER, KARL-HEINZ

Inventor name: MERKEL, MARION

Inventor name: ENGELSKIRCHEN, JULIA

Inventor name: WIELAND, SUSANNE

Inventor name: SIEGERT, PETRA

GRAP Despatch of communication of intention to grant a patent

Free format text: ORIGINAL CODE: EPIDOSNIGR1

DAX Request for extension of the european patent (deleted)
RIN1 Information on inventor provided before grant (corrected)

Inventor name: BESSLER, CORNELIUS

Inventor name: MAURER, KARL-HEINZ

Inventor name: MERKEL, MARION

Inventor name: ENGELSKIRCHEN, JULIA

Inventor name: WIELAND, SUSANNE

Inventor name: SIEGERT, PETRA

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: THE APPLICATION IS DEEMED TO BE WITHDRAWN

18D Application deemed to be withdrawn

Effective date: 20100330