WO2005056744A1 - Enzymes hybrides a domaine de liaison cationique - Google Patents

Enzymes hybrides a domaine de liaison cationique Download PDF

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Publication number
WO2005056744A1
WO2005056744A1 PCT/EP2004/013671 EP2004013671W WO2005056744A1 WO 2005056744 A1 WO2005056744 A1 WO 2005056744A1 EP 2004013671 W EP2004013671 W EP 2004013671W WO 2005056744 A1 WO2005056744 A1 WO 2005056744A1
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Prior art keywords
enzyme
hybrid
preparation
enzymes
cleaning
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PCT/EP2004/013671
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German (de)
English (en)
Inventor
Frank Janssen
Roland Breves
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Henkel Kommanditgesellschaft Auf Aktien
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Publication of WO2005056744A1 publication Critical patent/WO2005056744A1/fr

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    • 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
    • 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
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand

Definitions

  • Hybrid enzymes with a cationic binding domain with a cationic binding domain
  • the present invention relates to hybrid enzymes, comprising a hydrolytically active unit and a cationic binding unit and preparations which contain these hybrid enzymes.
  • Biofilm is the term used to describe the growth of surfaces by microbes and, above all, the gelatinous protective layer which they collectively emit and envelop, which is also called the EPS matrix, where EPS stands for "extracellular polymeric substances".
  • This protective layer is composed, among other things from proteins and polysaccharides, in which various dirt particles such as dead cells, skin particles and lime are embedded.
  • This mucus is at the same time the reason why bacteria living under real conditions, as well as other microorganisms producing biofilms, are much more resistant to cleaning, including those containing biocides - and disinfectants are laboratory cultures that normally consist of single free-floating bacteria, so-called planktonic cells .
  • Biofilms lead to massive impairments in technical systems and can cause stubborn infections in medicine, which counteract are largely resistant to conventional antibiotics. In the household, the impairments caused by biofilms are both hygienic and aesthetic in nature.
  • European patent EP 946 207 B1 (corresponding to WO 98/26807) teaches the enzymatic treatment of biofilms with combinations of hydrolases, which serve to detach and remove the biofilms from the surface, and oxidoreductases, which kill the bacteria contained. These systems are used to clean and disinfect hard surfaces made of a wide variety of materials in various industrial areas, such as cooling towers, dairies or chemical plants, but also soft surfaces such as skin, hair or textiles.
  • EP 388 115 deals with the destruction and removal of slime on industrial, water-washed surfaces.
  • glucanases, cellulases, amylases and / or proteases are used which specifically decompose the polysaccharides of the slime matrix; then the now accessible microorganisms are to be exposed to the action of biocides.
  • WO 01/09295 claims enzymes with a ⁇ - (1,6) endoglucanase activity and corresponding DNA sequences, furthermore an enzyme preparation for the degradation of ⁇ -1,6-glucan-containing materials and their use.
  • the ß- (1, 6) - endoglucanases also serve to remove biofilms from various surfaces.
  • This Spanish document mainly deals with the degradation of the ⁇ -1,6-glucan-rich cell wall of certain fungi.
  • WO 96/36569 also describes an enzymatic method for removing biofilms.
  • a mannanase optionally in combination with at least one further enzyme, is used in order to avoid the formation of slime in industrial water-carrying systems and to remove existing slime.
  • this object can also be achieved with combinations of short-chain glycol components with at least one enzyme from the group of polysaccharidases, proteases, lipases and glycoproteases.
  • International application WO 01/53010 also teaches an enzymatic process for removing " biofilms from various with water or aqueous Solutions wash around surfaces in industrial systems as well as in the medical field, whereby the biofilms are located above the water surface, i.e. at solid / liquid / air interfaces, as well as under water, at solid / liquid interfaces.
  • the enzymes used are carbohydrases or proteases, combinations of these two enzymes are also possible.
  • the cleaning solution can contain other active substances such as corrosion inhibitors, surfactants, biocides etc. in addition to the enzymes mentioned.
  • bacterial biofilms also consist of nucleic acids and are particularly affected by nucleic acid-degrading enzymes, e.g. hydrolysable by DNAsen.
  • the object of the present invention was therefore to provide a method for the effective removal of the biofilm, in particular one which is more effective than the methods previously described in the prior art.
  • hydrolytic enzymes could be an efficient means of removing the biofilm if their residence time could be increased.
  • Another object of the present invention was, in particular, to provide cleaning agents which, without the use of biocides, are capable of Dissolve biofilms on hard surfaces in the home and remove the film-forming microorganisms.
  • the main task is solved by enzymes, which are able to remain on the surface longer and are therefore able to break down biofilm more effectively.
  • the enzymes modified in this way can adhere longer to the biofilm or to surfaces that have a biofilm and thus more effectively degrade the biofilm.
  • WO 95/31556 describes hybrid proteins from glucan-binding domains, to which antimicrobial substances are bound, for use as oral care products.
  • WO 98/18437 describes mutan binding domains to which antimicrobial substances are bound, also for use as oral care products.
  • WO 98/16190 describes hybrid proteins composed of starch-binding domains with antimicrobial substances, which are also used as oral care products.
  • WO 99/33957 describes modified enzymes which comprise a polyanionic domain, which are also used in oral care products.
  • WO 99/18999 also describes compositions which are used in oral care products, the composition comprising an enzyme and an anchor molecule which is bound to the enzyme and is capable of binding to a substrate which is close to a bacterial Colony located.
  • short-chain basic and acid molecules are mentioned as anchor molecules.
  • compositions for the treatment of biofilm structures comprising an enzyme which is able to degrade biofilm structures and comprises an anchor which is able to bind to the cellular colony or to other bioadhesive molecules.
  • the anchor molecule are the binding domain of elastase, domains that bind to carbohydrates and polysaccharides, lectins, selectins, the binding domain of heparin, the binding domain of fibronectin and the CD44 protein.
  • US 2002022005 describes a composition for degradation of biofilm structures associated with cystic fibrosis, the composition comprising an enzyme capable of degrading biofilms and an anchor capable of being surface or to bind near the biofilm structure.
  • Concanavalin, lectins, elastase, heparin and amylose binding domains are mentioned as anchor molecules.
  • WO 00/47174 and WO 00/47175 describe oral care products that contain fusion proteins that comprise an enzyme and an anchor molecule.
  • the enzymes are those that can degrade polysaccharides
  • the anchor molecule is a molecule that is capable of binding “in the vicinity of a bacterial colony”. Examples of the anchor molecule are glutathione -S- transferase, glutathione, avidin, streptavidin, biotin and antibody.
  • the oligopeptide KKEKK is also mentioned as a possible cationic anchor molecule.
  • this short-chain peptide is not capable of being coupled to a higher molecular hydrolytically active Unit to increase the pI value of the resulting protein sufficiently to enable effective binding to a biofilm.
  • Hybrid proteins according to the invention and the use according to the invention of the hybrid proteins have not previously been described in the prior art.
  • a first subject of the present invention are therefore hybrid proteins, comprising a hydrolytically active unit and a cationic binding unit.
  • the hydrolytically active unit of the hybrid enzyme according to the invention is preferably a hydrolytic enzyme, especially from the group of polysaccharidases, in particular ⁇ -glucanases, cellulases, xylanases, amylases, dextranases, glucosidases, galactosidases, pectinases, chitinases or alginate lyases or lysozyme, and / or from the group of proteases and peptidases, in particular subtilisin, thermolysin, pepsin, carboxypeptidase or acid protease, and / or from the group of nucleases, in particular DNAsen or RNAsen and / or it is a functional one Fragment of it.
  • a hydrolytic enzyme especially from the group of polysaccharidases, in particular ⁇ -glucanases, cellulases, xylanases, amylases, dextranases,
  • the cationic binding unit can be a naturally occurring or an artificially produced, naturally non-occurring binding domain.
  • the binding domain is preferably a protein or a polypeptide, so that the hybrid enzyme is a fusion protein.
  • other units which have a positive charge for example organic molecules which carry amino groups, can also be used as the cationic binding unit or cationic binding domain.
  • the cationic binding unit is preferably not more than 200, in particular not more than 150 amino acids long, particularly preferably it has a length between 10 and 200, in particular between 10 and 140, especially between 10 and 20 or between 30 and 140 amino acids.
  • the average number of charges is preferably between 0.01 and 0.8, particularly preferably between 0.1 and 0.4 positive charges per amino acid residue at neutral pH.
  • the cationic binding unit is preferably designed in terms of length or size and charge such that by adding the cationic binding unit to a hydrolytic unit with a neutral or slightly acidic p1 value (p1 ⁇ 8), a hybrid enzyme is produced which is equal to a p1 value 8.5, particularly preferably greater than or equal to 9.0. Due to the increased pI value, the binding to facilitates the negatively charged biofilm.
  • the suitable cationic binding unit can be selected in a simple manner by calculating the resulting pI value for the hybrid enzyme in silico, for example using the ExPASy Compute pl / Mw program (Bjellqvist, B., Hughes, GJ, Pasquali, Ch., Paquet, N., Ravier, F., Sanchez, J.-Ch., Frutiger, S. & Hochstrasser, DF
  • the focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences.
  • the cationic binding unit comprises a binding domain of a naturally occurring surface protein, in particular a so-called cell envelope protein, a cell membrane-associated protein and / or a so-called surface layer protein (S-layer protein) and / or a fragment and / or or a derivative thereof, the length of the cationic binding unit preferably being between 10 and 200, in particular between 10 and 140, especially between 10 and 20 or between 30 and 140 amino acids, and the values given above being preferred for the charges.
  • this can be the binding domain of an sbs protein, in particular an sbs protein from Geobacillus, especially from Geobacillus stearothermophilus, or a fragment and / or derivative thereof.
  • the binding domain can in particular comprise a polypeptide with an amino acid sequence according to SEQ ID NO: 19 or according to SEQ ID NO: 20 or derivatives of the polypeptides mentioned.
  • Derivatives are to be understood here in particular: a) naturally occurring or artificially synthesized mutants of the polypeptides mentioned, in particular those which have up to ten, preferably up to five, especially exactly one, two or three, point mutations in relation to the polypeptides mentioned, b) polypeptides which have a sequence homology or identity of at least 50%, preferably at least 60% or 70%, very particularly preferably at least 80 or 90%, in particular at least 95% or 98%, in relation to the polypeptides mentioned, c) polypeptides consisting of at least 10 or 15, particularly preferably at least 20 or 30, consecutive amino acids of said polypeptides or a polypeptide according to (a) or (b), d) polypeptides with insertions and / or deletions of up to 10, 5 or 3 amino acids in relation to the poly
  • surface proteins in addition to surface layer proteins, surface proteins are generally mentioned which are capable of binding to negatively charged polysaccharides, as are often found in cell walls, such as, for example, cell-walled proteins from plants which are able to bind to pectins ,
  • the cationic binding unit is an artificially produced, naturally non-occurring polypeptide, in particular one with a length between 10 and 100, preferably between 20 and 50, particularly preferably between 25 and 40 amino acids, which preferably carries between 0.3 and 0.4 positive charges at neutral pH, the positively charged groups preferably being lysine or arginine residues, particularly preferably lysine residues.
  • the cationic binding domain here preferably comprises a polypeptide with an amino acid sequence according to SEQ ID NO.
  • a derivative is to be understood in particular as a) naturally occurring or artificially synthesized mutants of a polypeptide with an amino acid sequence according to SEQ ID NO: 21, in particular those which contain up to ten, preferably up to five, especially precisely on, have two or three point mutations with respect to a polypeptide with an amino acid sequence according to SEQ ID NO: 21, b) polypeptides which have a sequence homology or identity of at least 50%, preferably at least 60% or 70%, very particularly preferably at least 80 or 90 %, in particular at least 95% or 98%, in relation to a polypeptide with an amino acid sequence according to SEQ ID NO: 21, c) polypeptides consisting of at least 10 or 15, particularly preferably at least 20 or 30, consecutive amino acids of a polypeptide with an amino acid sequence according to SEQ ID NO: 21 or a polypeptide according to (a) or (b), d) polypeptides with insertions and / or deletions of up to 10, 5 or 3
  • the present invention also relates to a polypeptide according to SEQ ID NO: 21 or a derivative thereof in the sense given above.
  • the present invention furthermore relates to nucleic acids which code for one of the aforementioned polypeptides.
  • the present invention furthermore relates to aqueous preparations (enzyme preparations) which contain the hybrid proteins according to the invention in dissolved form.
  • the present invention furthermore relates to the use of the hybrid enzymes according to the invention and / or of enzyme preparations comprising hybrid enzymes, in particular in sterilization, disinfection, washing and cleaning agents, especially in cleaners for removing biofilms from hard surfaces, the use of which in this use Application is preferably carried out on abiotic surfaces, especially not on living beings.
  • the use of the agents can in particular in the household or in the field of pharmaceutical, food, brewery, medical technology, paint, wood, textile, cosmetic, leather, Tobacco, fur, rope, paper, pulp, plastic, fuel, oil, rubber or machine industries or in dairies.
  • the hybrid enzymes according to the invention can be used in particular for the removal of biofilms from household and / or sanitary objects, as well as in pulp and paper mills, in circulation cooling towers and in other systems which carry flowing and / or circulating water.
  • the hybrid enzymes according to the invention are, for example, also suitable for use in detergents for cleaning textiles, in particular for removing stains.
  • the positively charged binding unit makes it easier to adhere to negatively charged textile surfaces.
  • the present invention furthermore relates to sterilization, disinfection, washing and cleaning agents which contain hybrid enzymes according to the invention and / or enzyme preparations containing hybrid enzymes.
  • the agent can in principle be an agent for any type of surface.
  • the surface can therefore be a biotic or abiotic, artificially synthesized or natural, soft or hard surface. However, in this use, application is preferably carried out on an abiotic surface, in particular not on living beings.
  • the surface can be, for example, a textile, ceramic, metal and / or plastic surface.
  • the item can be, for example, laundry, sanitary facilities, floor coverings, shoes, leather, utility articles made of rubber, ship's hulls, prostheses, teeth, dentures or catheters.
  • the cleaning agent can be, in particular, a household cleaner or a cleaner for industrial plants, in particular those mentioned above.
  • the cleaner is one for cleaning hard surfaces, such as floors, tiles, tiles, plastics and other hard surfaces in the household, in industrial plants, in public sanitary facilities, in swimming pools, saunas, Sports facilities or in medical or massage practices.
  • biofilms that can be removed with hybrid enzymes according to the invention are, for example, biofilms caused by chronic lung infections eg in cystic fibrosis patients. Furthermore, it can be dental plaque or biofilms that have to be removed from contact lenses, implants or from medical devices, instruments or apparatus such as catheters or endoscopes.
  • the present invention therefore also relates to the use of the enzyme preparations according to the invention and / or enzyme preparations containing hybrid enzymes in cosmetic and / or pharmaceutical products, and to cosmetic and / or pharmaceutical products which contain the hybrid enzymes and / or enzyme preparations according to the invention and also the use of the hybrid enzymes according to the invention and / or enzyme preparations for the production of cosmetic and / or pharmaceutical products.
  • the product may, for example, be a product for removing plaque from tooth surfaces or a product for removing biofilms caused by or associated with chronic lung infections, such as e.g. in the case of cystic fibrosis.
  • the present invention therefore primarily relates to oral, dental or denture care products which contain the hybrid enzymes according to the invention.
  • the sterilization, disinfection, washing and cleaning agents can contain further components as are known to the person skilled in the art, in particular one or more components selected from the group consisting of surfactants, builders, acids, alkaline substances, hydrotropes, solvents, thickeners, dyes , Perfumes, corrosion inhibitors and skin protection agents.
  • the cleaning agent is to be sprayed, it may also contain a blowing agent.
  • the cleaning agent is preferably a liquid aqueous agent, but it can also be, for example, a gel, a paste or a powder.
  • Another object of the invention is a product containing an enzyme preparation according to the invention or a cleaning agent according to the invention and a spray dispenser.
  • the spray dispenser is preferably a manually activated spray dispenser, in particular selected from the group comprising aerosol spray dispensers (pressurized gas containers; also referred to as a spray can), self-building spray dispensers, Pump spray dispenser and trigger spray dispenser, in particular pump spray dispenser and trigger spray dispenser with a container made of transparent polyethylene or polyethylene terephthalate.
  • Spray dispensers are described in greater detail in WO 96/04940 (Procter & Gamble) and the US patents cited therein for spray dispensers, all of which are referred to in this regard and the contents of which are hereby incorporated into this application.
  • Trigger spray dispensers and pump atomizers have the advantage over pressurized gas containers that no propellant has to be used.
  • the agent containing the enzyme preparation is not atomized as an aerosol, since in this case small amounts of the enzyme preparation can get into the respiratory tract and under certain circumstances could trigger allergic reactions there.
  • the enzyme can be added to the agent in a form immobilized on particles by suitable, particle-compatible attachments, nozzles etc. (so-called "nozzle valves") on the spray dispenser and metered as cleaning foam. When producing these compact foams, no respirable particles are formed, so that the danger of inhaling allergens is essentially eliminated.
  • Yet another object of the invention is a process for the hydrolysis of biofilms on hard surfaces, in which the vitality of the microbial cells is not damaged.
  • the enzyme preparation according to the invention or the cleaning agent according to the invention if appropriate using a product according to the invention, is applied to the surface covered with biofilm and, if necessary, rinsed with clear water after an exposure time of 1 to 30 minutes, in the case of more severe infection also for a few hours or overnight.
  • the preparation or agent can also be blurred or rubbed on the surface infested with biofilm before rinsing with a cloth, sponge, brush or other utensil suitable for cleaning, e.g. improved cleaning performance in the presence of abrasive substances in the cleaning agent.
  • the surface is dried with a dry cloth. If the surface is very heavily infested with biofilm, the cleaning process can then be repeated.
  • the enzyme preparation according to the invention is a system containing one or more of the hybrid enzymes according to the invention. If appropriate, further, unmodified enzymes, in particular selected from polysaccharidases, proteases and nucleases, can also be contained in the enzyme preparation. Unless explicitly differentiated, the following explanations refer both to the free enzymes and to the hydrolytic unit which is part of the hybrid enzymes.
  • Polysaccharidases are enzymes that catalyze the hydrolytic cleavage of polysaccharides.
  • cellulose is broken down by cellulase, while the glucosidase from the oligosaccharide or polysaccharide molecule cleaves individual glucose units from the end.
  • the extracellular polysaccharide matrix of the biofilm consists of homo- and heteropolysaccharides, which are mainly made up of glucose, fucose, mannose, galactose, fructose, pyruvate, mannuronic acid and glucuronic acid. Accordingly, the polysaccharides for example levane, polymannane, dextrans, cellulose, amylopectin, glycogen or alginate.
  • the enzyme preparation preferably contains at least one enzyme either as a free enzyme or as a hydrolytic unit of the hybrid enzyme from the group ⁇ -glucanase, cellulase, xylanase, amylase, dextranase, glucosidase, galactosidase, pectinase, chitinase, lysozyme, hemicellulase and alginate lyase , These enzymes can include several family members.
  • both an ⁇ -1,4-glucosidase which was also referred to as maltase
  • a ⁇ -1,4-glucosidase are known.
  • all these subgroups are included.
  • Commercially available mixtures of polysaccharidases can also be used.
  • Viscozyme a liquid enzyme preparation from Aspergillus sp., which is composed of various polysaccharidases, is suitable, among others. from arabanase, cellulase, ⁇ -glucanase, hemicellulase and xylanase, for use in the context of this invention.
  • Proteases are enzymes that catalyze the hydrolytic cleavage of the peptide bond of proteins and peptides. They can therefore also be used to break down biofilms, since these can contain polysaccharides as well as proteins secreted by the film-forming organisms. Proteases can be systematically divided into acidic, neutral and alkaline proteases based on the pH optimum of their activity, but also classified according to the catalytically active group in the active center. A distinction is made between serine, cysteine, aspartate and metal proteases.
  • proteases can be used to break down biofilms, but at least one protease selected from the group consisting of subtilisin, thermolysin, pepsin, carboxypeptidase and acid protease is preferably used.
  • the nucleases are enzymes that break down nucleic acids. Depending on the hydrolysis site, a distinction is made between endonucleases that cleave within the nucleic acid strand (eg DNAse I from pancreas) and exonucleases that Release nucleotides from the end (eg exonuclease III from E. col i). DNA single strands (S1 nuclease from Aspergillus oryzae) or double strands (exonuclease III) can serve as a substrate and can be broken down into unspecific strands or shorter nucleotides. Mixed specificities are also possible and occur depending on, for example, the enzyme concentration and the presence of certain ions.
  • RNA molecules Analogously, the cleavage of RNA molecules is also possible.
  • Highly specific endonucleases require certain nucleotide sequences (typically 4-8 base pairs) and are sometimes also referred to as restriction enzymes or restriction endonucleases.
  • biofilms can also consist of nucleic acids, all nucleases are also suitable for use in biofilm-degrading agents according to the invention.
  • non-specific DNAsen or RNAsen are preferably used.
  • the free enzymes which can be used in the context of this invention can be obtained from the corresponding organisms by customary biochemical methods. However, they are also commercially available, for example from Novozymes, Genencor International, Sigma, AB Enzymes or ASA Enzyme.
  • the enzyme preparations can also be of technical quality and consist of several different enzyme activities. The presence of side activities, which are sometimes not characterized in more detail, can also have a favorable influence on the hydrolysis of the complex biofilm polymers.
  • proteases are to be combined with other enzymes, for example polysaccharidases, it should be noted, regardless of whether it is hybrid enzymes according to the invention or free enzymes, that these are contained in liquid agents by components such as surfactants or organic acids or also in the cleaner could be attacked by the rather nonspecific proteases, which would reduce the effectiveness of the agents against non-protein biofilm components.
  • enzymes for example polysaccharidases
  • the different enzymes can be separated in different ways.
  • the enzymes can also be immobilized in each case on a solid carrier which is suspended in the cleaning agent and can additionally serve as an abrasive when the agent is used. The immobilization takes place in a manner known to the person skilled in the art; In addition to inorganic substances, for example silicates or porous glass, polymers can also be used as carrier materials.
  • Another conceivable possibility could also be incorporation into a multi-phase agent, so that the protease would predominantly be located in one phase and the other enzymes would predominantly be in a further phase.
  • Such an agent would be shaken up shortly before use and the resulting emulsion applied to the surface to be cleaned; the agent remaining in the storage bottle would then experience a rapid phase separation, so that the enzymes would only come into contact for a short time and possibly at the phase interface.
  • the situation would be similar if an enzyme were incorporated into a phase which was stably dispersed in the form of droplets in the second phase containing the other enzyme; the agent would not be shaken, but dosed directly from the storage bottle, if necessary also sprayed.
  • such a multiphase means would be a technically complex and difficult to implement solution. In addition, consumer acceptance would probably be low.
  • a two- or multi-chamber bottle offers further advantages. It is possible, for example, to store an enzyme in a solution with an optimal pH in terms of storage stability in one chamber and to store a solution in another chamber, the pH of which leads to the result that a cleaning solution is formed when it is mixed with the enzyme storage solution. whose pH value ensures optimum enzyme activity. For example, many polysaccharidases are particularly stable at neutral pH, but display their highest activity at pH 4 to 5.
  • the hybrid enzyme and / or the enzyme preparation can also be used in a cleaning agent for hard surfaces.
  • the cleaning agent can contain the enzyme preparation in particular in amounts of 0.1 to 10.0% by weight, preferably 0.5 to 3% by weight.
  • the cleaning agent is preferably biocide-free, but can optionally also contain biocide, preferably in small amounts.
  • a liquid, gel-like or pasty aqueous cleaning agent for hard surfaces can also contain customary cleaning agent components according to the invention.
  • These ingredients include, for example, surfactants, but also builders, acids, alkalis, hydrotropes, solvents, thickeners, abrasives and other auxiliaries and additives such as dyes, perfumes, corrosion inhibitors or even skin care products.
  • the surfactants optionally used are preferably selected from the group consisting of anionic surfactants, nonionic surfactants and / or amphoteric surfactants.
  • Anionic and / or nonionic surfactants are preferably used. If they are used, anionic surfactants preferably come in amounts of 0.1 to 15% by weight, nonionic surfactants preferably in amounts of 0.1 to 10% by weight and amphoteric surfactants preferably in amounts of 0.1 to 4% by weight .-% for use, each based on the total composition.
  • anionic surfactants preferably come in amounts of 0.1 to 15% by weight
  • nonionic surfactants preferably in amounts of 0.1 to 10% by weight
  • amphoteric surfactants preferably in amounts of 0.1 to 4% by weight .-% for use, each based on the total composition.
  • cationic surfactants can also be used in amounts of up to 2% by weight, based on the Total composition.
  • Cationic surfactants can also be used. In
  • the anionic surfactants which can be used according to the invention include aliphatic sulfates such as fatty alcohol sulfates, fatty alcohol ether sulfates, dialkyl ether sulfates, monoglyceride sulfates and aliphatic sulfonates such as alkane sulfonates, ⁇ -olefin sulfonates, ether sulfonates, n-alkyl ether sulfonates, sulfonated fatty acids and lignin sulfonates.
  • aliphatic sulfates such as fatty alcohol sulfates, fatty alcohol ether sulfates, dialkyl ether sulfates, monoglyceride sulfates and aliphatic sulfonates such as alkane sulfonates, ⁇ -olefin sulfonates, ether sulfonates, n-alky
  • alkylbenzene sulfonates (ride Fettklaretau, N-acyl taurides), fatty acid salts (soaps), fatty acid cyanamides, sulfosuccinates (sulfosuccinic acid mono- and dialkyl esters), sulfosuccinamates, sulfosuccinamides, Carbonchureamidethersulfate, Alkylpolyglykolethercarboxylate, fatty acylaminoalkanesulfonates, fatty acid sarcosinates, ether carboxylic acids and Alkyl (ether) phosphates and ⁇ -sulfofatty acid salts, acylglutamates, monoglyceride disulfates and alkyl ethers of glycerol disulfate, and finally their mixtures.
  • fatty acids or fatty alcohols or their derivatives are representative of branched or unbranched carboxylic acids or alcohols or their derivatives having preferably 6 to 22 carbon atoms, in particular 8 to 20 carbon atoms, particularly preferably 10 to 18 carbon atoms, most preferably 12 to 16 carbon atoms, for example 12 to 14 carbon atoms.
  • the fatty acids / alcohols or their derivatives with an even number of carbon atoms are preferred for ecological reasons, in particular because of their vegetable basis as based on renewable raw materials, but without restricting the teaching according to the invention to them.
  • the oxo alcohols or their derivatives obtainable, for example, according to RoELEN's oxo synthesis, or their derivatives, having preferably 7 to 19 carbon atoms, in particular 9 to 19 carbon atoms, particularly preferably 9 to 17 carbon atoms, most preferably 11 to 15 carbon atoms, for example 9 to 11 , 12 to 15 or 13 to 15 carbon atoms, can be used accordingly.
  • alkali metal and alkaline earth metal salts in particular sodium, potassium and magnesium salts, as well as ammonium and mono-, di-, tri- or Tetraalkylammonium salts and, in the case of the sulfonates, also in the form of their corresponding acid, for example dodecylbenzenesulfonic acid.
  • the alkyl ether sulfates always contain residual contents of non-alkoxylated fatty alcohol sulfates, especially at low degrees of ethoxylation.
  • the agents according to the invention can also contain soaps, ie alkali or ammonium salts of saturated or unsaturated C 6 -C 22 fatty acids.
  • the anionic surfactants are preferably selected from the group comprising fatty alcohol sulfates in amounts of up to 5% by weight, alkylbenzenesulfonates in amounts of up to 7.5% by weight and soaps in amounts of up to 2% by weight, in each case based on the overall composition, as well as mixtures thereof.
  • Suitable nonionic surfactants are, for example, C ⁇ -C-i ⁇ -
  • C ⁇ -Ci ⁇ -alkyl alcohol polypropylene glycol / polyethylene glycol ether can by the formula R 1 0- (CH 2 CH (CH 3 ) 0) p (CH 2 CH 2 0) eH
  • R 1 is a linear or branched, aliphatic alkyl and / or alkenyl radical having 8 to 18 carbon atoms
  • p is 0 or numbers from 1 to 3
  • e is numbers from 1 to 20.
  • They are obtained by the addition of propylene oxide and / or ethylene oxide to alkyl alcohols, preferably to fatty alcohols.
  • end-capped C 8 -C 8 -alkyl alcohol polyglycol ethers can also be used, ie alkyl alcohol polyalkylene glycol ethers according to the above formula in which the free OH group is etherified.
  • Cleaners according to the invention can contain alkyl alcohol polyglycol ethers in amounts of 0.1 to 4% by weight, based on the total composition.
  • Preferred nonionic surfactants are furthermore alkyl polyglycosides (APG) of the formula
  • R 2 0 [G] x in which R 2 is a linear or branched, saturated or unsaturated alkyl radical having 8 to 22 carbon atoms, [G] is a glycosidically linked sugar radical and x is a number from 1 to 10.
  • alkyl glycosides are preferred whose degree of oligomerization is less than 1.7, and in particular between
  • the alkyl or alkenyl radical R 2 can be derived from primary alcohols having 8 to 18, preferably 8 to 14, carbon atoms. Typical examples are capronic alcohol, caprylic alcohol, capric alcohol and undecyl alcohol and their technical mixtures, such as those obtained in the course of the hydrogenation of technical fatty acid methyl esters or in the course of the hydrogenation of aldehydes from RoELEN's oxo synthesis.
  • the alkyl or alkenyl radical R 2 is preferably derived from lauryl alcohol, myristyl alcohol, cetyl alcohol, palmoleyl alcohol, stearyl alcohol, isostearyl alcohol or oleyl alcohol.
  • Elaidyl alcohol, petroselinyl alcohol, arachidyl alcohol, gadoleyl alcohol, behenyl alcohol, erucyl alcohol and their technical mixtures are also to be mentioned.
  • Alkyl polyglycosides can be present in cleaners according to the invention in amounts of 0.1 to 6% by weight, based on the total composition.
  • Nitrogen-containing surfactants may be included as further nonionic surfactants, e.g. Fatty acid polyhydroxyamides, for example glucamides, and ethoxylates of alkylamines, vicinal diols and / or carboxamides which have alkyl groups with 10 to 22 C atoms, preferably 12 to 18 C atoms.
  • the degree of ethoxylation of these compounds is generally between 1 and 20, preferably between 3 and 10.
  • Ethanolamide derivatives of alkanoic acids having 8 to 22 carbon atoms, preferably 12 to 16 carbon atoms, are preferred.
  • the particularly suitable compounds include lauric acid, myristic acid and palmitic acid monoethanolamides.
  • amphoteric surfactants (amphoteric surfactants, zwitterionic surfactants) which can be used according to the invention include betaines, amine oxides, alkylamido alkylamines, alkyl substituted amino acids and acylated amino acids.
  • amphoteric surfactants are, for example, betaines of the formula
  • R 3 is an alkyl radical with 8 to 25, preferably 10 to 21 carbon atoms, which is optionally interrupted by heteroatoms or heteroatom groups
  • R 4 and R 5 are identical or different alkyl radicals with 1 to 3 carbon atoms, in particular Cio-Cis-alkyl-dimethylcarboxymethylbetaine and Cn- C ⁇ 7 - Alkyamidopropyl-dimethylcarboxymethylbetaine.
  • cationic surfactants are present in the composition, these are preferably the quaternary ammonium compounds of the formula
  • R 6 to R 9 stand for four identical or different types, in particular two long and two short chains, alkyl radicals and X " for an anion, in particular a halide ion, for example didecyl-dimethyl-ammonium chloride, alkyl-benzyl-didecyl-ammonium chloride and mixtures thereof, but the detergent composition is preferably free of cationic surfactants.
  • the enzyme activity is preferably reduced by no more than 50%, in particular by no more than 30%, during a typical average exposure time of 15 minutes.
  • SDS sodium dodecyl sulfate
  • the agents according to the invention can also contain builders.
  • Suitable builders are, for example, alkali metal gluconates, citrates, nitrilotriacetates, carbonates and bicarbonates, in particular sodium gluconate, citrate and nitrilotriacetate, and also sodium and potassium carbonate and bicarbonate, and also alkali metal and alkaline earth metal hydroxides, in particular sodium and potassium and ammonium hydroxides, in particular sodium and potassium and ammonium amides, and ammonium and potassium amides , in particular mono- and triethanolamine, or mixtures thereof.
  • This also includes the salts of glutaric acid, succinic acid, adipic acid, tartaric acid and benzene hexacarboxylic acid as well as phosphonates and phosphates.
  • the agents can contain builders in amounts, based on the composition, of 0.1 to 5% by weight.
  • the agents according to the invention can furthermore contain acids and / or alkalis.
  • these serve as pH regulators, on the other hand, the acids can also help to remove limescale from the surfaces to be cleaned.
  • acids may be inorganic mineral acids, for example hydrochloric acid, and / or to C1.- 6 - mono-, di-, tri- or polycarboxylic acids or hydroxy carboxylic acids such as formic acid, acetic acid, lactic acid, citric acid, gluconic acid, glutaric acid , Succinic acid, adipic acid, tartaric acid or malic acid as well as other organic acids such as salicylic acid or amidosulfonic acid.
  • citric acid is particularly preferably used; Mixtures of several acids can also be used. Acids can be present in the cleaning agent according to the invention in amounts of up to 6% by weight, based on the total composition.
  • the bases which can optionally be used include alkanolamines, for example mono- or diethanolamine, and also ammonium or alkali metal hydroxides, especially sodium hydroxide.
  • the cleaning agent according to the invention can contain bases in amounts of up to 2.5% by weight, based on the total composition.
  • the agent according to the invention can furthermore contain one or more thickeners for viscosity regulation. Natural and synthetic polymers and inorganic thickeners are suitable as thickeners.
  • the polymers that can be used include polysaccharides or heteropolysaccharides and other organic natural thickeners, including the polysaccharide gums such as acacia, agar, alginates, carrageenan and their salts, guar, guarane, tragacanth, gellan, ramsan, dextran or xanthan and their derivatives, for example propoxylated Guar, as well as their mixtures, also pectins, polyoses, locust bean gum, starch, dextrins, gelatin, casein.
  • polysaccharide gums such as acacia, agar, alginates, carrageenan and their salts, guar, guarane, tragacanth, gellan, ramsan, dextran or xanthan and their derivatives, for example propoxylated Guar, as well as their mixtures, also pectins, polyoses, locust bean gum, starch, de
  • Organic modified natural substances such as carboxymethyl cellulose and cellulose ether, hydroxyethyl and propyl cellulose and the like, or cellulose acetate and gum flour ether can also be used.
  • Homo- and copolymeric polycarboxylates, especially polyacrylic and polymethacrylic compounds, as well as vinyl polymers, polycarboxylic acids, polyethers, polyimines or polyamides can be used as fully synthetic synthetic thickeners.
  • the inorganic thickeners that can be used include polysilicic acids, clay minerals such as montmorillonites, zeolites, silica, and various nanoparticulate inorganic compounds such as nanoparticulate metal oxides, oxide hydrates, hydroxides, carbonates and phosphates, and silicates with an average particle size of 1 to 200 nm, based on the Particle diameter in the longitudinal direction, ie in the direction of the greatest expansion of the particles.
  • these nanoparticulate substances can optionally be treated with one or more surface modification agents. The surface modification is carried out in a manner known to the person skilled in the art using mono- and polybasic C 2 .
  • the cleaning agent according to the invention can contain electrolyte salts. These can also contribute to an increase in viscosity.
  • electrolyte salts are salts which break down into their ionic constituents in the aqueous composition according to the invention.
  • the salts in particular alkali metal and / or alkaline earth metal salts, are preferred, an inorganic acid, preferably an inorganic acid from the group comprising the hydrohalic acids, nitric acid and sulfuric acid, in particular the chlorides and sulfates.
  • an electrolyte salt can also be used in the form of its corresponding acid / base pair, for example hydrochloric acid and sodium hydroxide instead of sodium chloride.
  • Organic and / or inorganic thickeners in amounts of up to 2% by weight, based on the total composition, can be used in the agent according to the invention.
  • the agent according to the invention can advantageously additionally contain one or more water-soluble organic solvents, usually in an amount of up to 6% by weight, based on the total composition.
  • the solvent is used, in particular, as a hydrotrope, viscosity regulator and / or cold stabilizer. It has a solubilizing effect, particularly for surfactants and electrolytes, as well as perfume and dye, and thus contributes to their incorporation, prevents the formation of liquid-crystalline phases and is involved in the formation of clear products.
  • the viscosity of the agent according to the invention decreases with increasing amount of solvent. However, too much solvent can cause an excessive drop in viscosity. Finally, the cold cloud and clear point of the agent according to the invention decrease with increasing amount of solvent.
  • Suitable solvents are, for example, saturated or unsaturated, preferably saturated, branched or unbranched C 1-2 o-hydrocarbons, preferably C 2 -i 5 hydrocarbons, with at least one hydroxyl group and optionally one or more ether functions COC, ie oxygen atoms interrupting the carbon atom chain.
  • Preferred solvents are, however, - if appropriate on one side with a C ⁇ etherified -6 alkanol - C. 2 6 - alkylene glycols and poly-C 2 .
  • 3- alkylene glycol ethers with an average of 1 to 9 identical or different, preferably identical, alkylene glycol groups per molecule, for example ethylene glycol, propylene glycol, butylene glycol, diethylene glycol, dimethoxy diglycol, dipropylene glycol, propylene glycol butyl ether, propylene glycol propyl ether, Dipropylene glycol monomethyl ether and PEG.
  • Other preferred solvents are the C ⁇ -6 alcohols such as methanol, ethanol, n-propanol, isopropanol, n-butanol, t-butanol etc., ethanol and / or isopropanol is particularly preferably used.
  • alkanolamines and alkylbenzenesulfonates having 1 to 3 carbon atoms in the alkyl radical e.g. Xylene or cumene sulfonate
  • Other usable hydrotropes are e.g. Octyl sulfate or butyl glucoside.
  • the agent according to the invention can contain these hydrotropes in amounts of up to 4% by weight, based on the total composition.
  • the agents according to the invention can contain abrasives.
  • Solid water-soluble and water-insoluble, preferably inorganic compounds and mixtures thereof can serve as the abrasive component. These include, for example, alkali carbonates, alkali bicarbonates and alkali sulfates, alkali borates, alkali phosphates, silicon dioxide, crystalline or amorphous alkali silicates and layered silicates, finely crystalline sodium aluminum silicates and calcium carbonate.
  • the advantage of water-soluble abrasive components is that the agent can be rinsed off practically without residue.
  • abrasives obtained from living nature for example crushed nut shells or woods
  • abrasion-resistant plastics for example polyethylene beads, or ceramic or glass beads
  • the cleaning agent according to the invention can contain abrasives in amounts of up to 2% by weight, based on the total composition.
  • the agents according to the invention can contain one or more further auxiliaries and additives, as are customary above all in cleaning agents for hard surfaces.
  • auxiliaries and additives include in particular UV stabilizers, corrosion inhibitors, cleaning enhancers, antistatic agents, preservatives (for example 2-bromo-2-nitropropane-1, 3-diol or an isothiazolinone-bromonitropropanediol preparation), perfume, dyes, pearlescent agents (for example glycol distearate) and opacifiers or also skin protection agents, as described for example in EP 522 506.
  • the amount of such additives is usually not more than 12% by weight in the cleaning agent.
  • the lower limit of the Use depends on the type of additive and can, for example, be up to 0.001% by weight and below for dyes.
  • the amount of auxiliaries is preferably between 0.01 and 7% by weight, in particular 0.1 and 4% by weight.
  • All dyes usually used in household cleaning agents can be used as dyes. All common perfumes can also be used for the fragrances. Fruity fragrances, for example citrus, pine (spruce) and mint, and floral fragrances are preferred. Preservatives have a biocidal effect, so that it is desirable to use only low concentrations, but preferably no preservatives at all, in cleaning agents according to the invention.
  • the agent contains no complexing agents; the addition of a bleaching agent to the cleaning agent according to the invention is not necessary.
  • the pH of the agents according to the invention is preferably between 1 and 7.5, particularly preferably between 2 and 5, in particular between 2.5 and 4.5.
  • the pH of the agent is to be understood as the pH of the temporary emulsion formed after shaking, in the case of agents that are offered in multi-chamber bottles, the pH of the agent is the pH of the common Intended dosing of the solution obtained in the various chambers. It means the pH value of the ready-to-use cleaning solution.
  • viscosity preferably up to 1000 mPas.
  • gel-like or pasty cleaning agents can have viscosities of up to 150,000 mPas.
  • the viscosity measurements are carried out at 20 ° C in a Brookfield LVDV II viscometer with a rotor frequency of 20 rpm (spindle no. 31, conc. 100%).
  • the cleaning agent can contain one or more propellants (INCI propellants), usually in an amount of 1 to 80% by weight, preferably 1.5 to 30% by weight, in particular 2 to 10% by weight, particularly preferably 2.5 up to 8% by weight, most preferably 3 to 6% by weight.
  • blowing agents are usually blowing gases, in particular liquefied or compressed gases. The choice depends on the product to be sprayed and the area of application. When using compressed gases such as nitrogen, carbon dioxide or nitrous oxide, which are generally insoluble in the liquid cleaning agent, the operating pressure decreases with each valve actuation. Liquefied gases (liquefied gases) as propellants, which are soluble in the detergent or even act as a solvent, offer the advantage of constant operating pressure and even distribution, because the propellant evaporates in air and takes up several hundred times its volume.
  • blowing agents designated according to INCI are suitable: butanes, carbon dioxides, dimethyl carbonates, dimethyl ethers, ethanes, hydrochlorofluorocarbon 22, hydrochlorofluorocarbon 142b, hydrofluorocarbon 152a, hydrofluorocarbon 134a, hydrofluorocarbon 227ea, isobutanes, isopentanes, nitrogenous, nitrous oxides.
  • chlorofluorocarbons chlorofluorocarbons, CFCs
  • blowing agents are 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.
  • liquid gases are gases that can be converted from gaseous to liquid at mostly low pressures and 20 ° C.
  • liquid gases include the hydrocarbons that are produced in oil refineries as by-products in the distillation and cracking of petroleum and in gas processing for gasoline separation - propane, propene, butane, butene, isobutane (2-methyl propane), isobutene (2-methyl propene, Isobutylene) and their mixtures understood.
  • the cleaning agent particularly preferably contains propane, butane and / or isobutane, in particular propane and butane, most preferably propane, butane and isobutane, as one or more blowing agents.
  • propane, butane and / or isobutane in particular propane and butane, most preferably propane, butane and isobutane, as one or more blowing agents.
  • the mouth, tooth and / or denture care products according to the invention can be present, for example, as mouthwash, gel, liquid toothbrush lotion, stiff toothpaste, chewing gum, denture cleaner or denture adhesive cream.
  • Powdery preparations or aqueous-alcoholic solutions which, as mouthwashes, contain 0 to 15% by weight of ethanol, 1 to 1.5% by weight of aromatic oils and 0.01 to 0.5% by weight of sweeteners or as mouthwash concentrates 15 to 60% by weight of ethanol, 0.05 to 5% by weight of aromatic oils, 0.1 to 3% by weight of sweeteners and, if appropriate, further auxiliaries, and may be diluted with water before use.
  • concentration of the components must be chosen so high that the dilution does not fall below the specified concentration limits after use.
  • gels and more or less flowable pastes can also serve as carriers, which are expressed from flexible plastic containers or tubes and applied to the teeth with the aid of a toothbrush.
  • Such products contain higher amounts of humectants and binders or consistency regulators and polishing components.
  • these preparations also contain aromatic oils, sweeteners and water.
  • humectants e.g. Glycerin, sorbitol, xylitol, propylene glycols, polyethylene glycols or mixtures of these polyols, in particular those polyethylene glycols with molecular weights from 200 to 800 (from 400 to 2000) can be used.
  • Sorbitol is preferably present as a humectant in an amount of 25-40% by weight.
  • Condensed phosphates in the form of their alkali metal salts preferably in the form of their sodium or potassium salts, can be present as anti-tartar active ingredients and as demineralization inhibitors.
  • the aqueous solutions of these phosphates are alkaline due to hydrolytic effects.
  • the pH of the Oral, dental and / or denture care agents according to the invention are set to the preferred values of 7.5-9.
  • a sodium or potassium tripolyphosphate is preferably present in a quantity of 5-10% by weight of the composition as the condensed phosphate.
  • a preferably contained active ingredient is a caries-inhibiting fluorine compound, preferably from the group of fluorides or monofluorophosphates in an amount of 0.1-0.5% by weight of fluorine.
  • Suitable fluorine compounds are, for example, sodium monofluorophosphate (Na 2 P0 3 F), potassium monofluorophosphate, sodium or potassium fluoride, tin fluoride or the fluoride of an organic amino compound.
  • Natural and synthetic water-soluble polymers such as carrageenan, tragacanth, guar, starch and their non-ionic derivatives such as hydroxypropyl guar, hydroxyethyl starch, cellulose ethers such as hydroxyethyl cellulose or methyl hydroxypropyl cellulose are used as binders and consistency regulators.
  • Other substances that are suitable for viscosity control are layered silicates such as, for example, montmorillonite clays, colloidal thickening silicas, for example airgel silica or pyrogenic silicas.
  • polishing components may all heretofore known polishing agent, but preferably precipitated and gel silicas, aluminum hydroxide, aluminum silicate, alumina, alumina trihydrate, insoluble sodium metaphosphate, calcium pyrophosphate, calcium hydrogen phosphate, dicalcium phosphate, chalk, hydroxyapatite, hydrotalcites, talc, magnesium aluminum silicate (Veegum ®), Calciumsuifat, magnesium carbonate, Magnesium oxide, sodium aluminum silicates, for example zeolite A or organic polymers, for example polymethacrylate, can be used.
  • the polishing agents are preferably used in smaller amounts, for example 1-10% by weight.
  • the dental and / or oral care products according to the invention can be improved in their organoleptic properties by adding aromatic oils and sweeteners. All natural and synthetic aromas customary for mouth, tooth and / or denture care products are suitable as aroma oils. Natural flavors can be used both in the form of the essential oils isolated from the drugs and in the individual components isolated from them. At least one aromatic oil from the group peppermint oil, spearmint oil, anise oil, caraway oil, eucalyptus oil, fennel oil, cinnamon oil, geranium oil, sage oil, thyme oil, marjoram oil, basil oil, citrus oil, Gaultheria oil or one or more synthetically produced components of these oils isolated therefrom should be contained.
  • oils mentioned are, for example, menthol, carvone, anethole, cineol, eugenol, cinnamaldehyde, geraniol, citronellol, linalool, salves, thymol, terpinene, terpinol, methylchavicol and methyl salicylate.
  • suitable flavors are, for example, menthyl acetate, vanillin, jonone, linalyl acetate, rhodinol and piperiton.
  • Suitable sweeteners are either natural sugars such as sucrose, maltose, lactose and fructose or synthetic sweeteners such as saccharin sodium salt, sodium cyclamate or aspartame.
  • alkyl and / or alkenyl (oligo) glycosides can be used as surfactants.
  • Their preparation and use as surface-active substances are, for example, from US-A-3 839 318, US-A-3 707 535, US-A-3 547 828 DE-A-19 43 689, DE-A-20 36 472 and DE -A-30 01 064 and EP-A-77 167 known.
  • the degree of oligomerization is a statistical mean value which is based on a homolog distribution customary for such technical products.
  • An alkyl and / or alkenyl (oligo) glycoside is preferably an alkyl and / or alkenyl (oligo) glucoside of the formula RO (C 6 H ⁇ oO) x -H, in which R is an alkyl and / or Alkenyl group with 8 to 14 carbon atoms and x has an average of 1 to 4.
  • Alkyl oligoglucosides based on hardened C 2 / i 4 coconut alcohol with a DP of 1 to 3 are particularly preferred.
  • the alkyl and / or alkenyl glycoside surfactant can be very good be used sparingly, with quantities of 0.005 to 1% by weight already being sufficient.
  • non-ionic, ampholytic and cationic surfactants may also be present, such as: fatty alcohol polyglycol ether sulfates, monoglyceride sulfates, monoglyceride ether sulfates, mono- and / or dialkyl sulfosuccinates, fatty acid isethionates, fatty acid seguric acid amides, fatty acid seguric acid amides, fatty acid segaric acid amides, fatty acid seguric acid amides, fatty acid segaric acid amides, fatty acid seguric acid amides, fatty acid segaric acid amides, fatty acid seguric acid amides, fatty acid segaric acid amides, fatty acid segaric acid amides, fatty acid segasucurate fatty acids, fatty acid sarcosinate fatty acids, kylamido-betaine and / or protein fatty acid condensates, the latter preferably based on
  • a nonionic solubilizer from the group of surface-active compounds may be required.
  • Particularly suitable for this purpose are e.g. ethoxylated fatty acid glycerides, ethoxylated
  • Fatty acid sorbitan partial esters or fatty acid partial esters of glycerol or sorbitan oxethylates Solubilizers from the group of the ethoxylated fatty acid glycerides primarily comprise addition products of 20 to 60 mol ethylene oxide with mono- and diglycerides of linear fatty acids with 12 to 18 carbon atoms or with triglycerides of hydroxy fatty acids such as oxystearic acid or ricinoleic acid.
  • solubilizers are ethoxylated fatty acid sorbitan partial esters; these are preferably addition products of 20 to 60 mol of ethylene oxide with sorbitan monoesters and sorbitan diesters of fatty acids with 12 to 18 carbon atoms.
  • fatty acid partial esters of glycerol or sorbitan oxyethylates these are preferably mono- and diesters of -C 2 -C 8 fatty acids and addition products of 20 to 60 moles of ethylene oxide with 1 mole of glycerol or with 1 mole of sorbitol.
  • the oral, dental and / or denture care agents according to the invention preferably contain adducts of 20 to 60 mol ethylene oxide with hardened or unhardened castor oil (ie with oxystearic acid or ricinoleic acid triglyceride), with glycerol mono- and / or as a solubilizer for aromatic oils which may be present -distearate or sorbitan mono- and / or -distearate.
  • hardened or unhardened castor oil ie with oxystearic acid or ricinoleic acid triglyceride
  • glycerol mono- and / or as a solubilizer for aromatic oils which may be present -distearate or sorbitan mono- and / or -distearate.
  • ⁇ -adjusting agents and buffer substances such as sodium bicarbonate, sodium citrate, sodium benzoate, citric acid, phosphoric acid or acid salts, e.g. NaH 2 P0 4 wound healing and anti-inflammatory substances such as allantoin, urea, panthenol, azulene or chamomile extract other substances effective against calculus such as organophosphonates, for example hydroxyethane diphosphonates or azacycloheptane diphosphonate, preservatives such as sorbic acid salts, p-hydroxybenzoic acid esters.
  • Plaque inhibitors such as hexachlorophene, chlorhexidine, hexetidine, triclosan, bromochlorophene, phenylsalicylic acid ester.
  • the composition is a mouthwash, a mouthwash, a denture cleaner or a denture adhesive.
  • Denture cleaning tablets and powders in addition to the ingredients already mentioned for oral, dental and / or dental prosthesis care, are also suitable for per-compounds such as peroxoborate, peroxomonosulfate or percarbonate. They have the advantage that they have a deodorising and / or disinfecting effect in addition to the bleaching effect.
  • the use of such per compounds in prosthesis cleaners is between 0.01 and 10% by weight, in particular between 0.5 and 5% by weight.
  • Enzymes such as e.g. Proteases and carbohydrase, suitable for breaking down proteins and carbohydrates.
  • the pH can be between pH 4 and pH 12, in particular between pH 5 and pH 11.
  • auxiliaries necessary for the denture cleaning tablets such as agents that produce a bubbling effect, such as C0 2 releasing substances such as sodium bicarbonate, fillers such as sodium sulfate or dextrose, lubricants, for example magnesium stearate, glidants such as colloidal silicon dioxide and granulating, like the already mentioned high molecular weight polyethylene glycols or polyvinyl pyrrolidone.
  • Denture adhesives can be offered as powders, creams, foils or liquids and support the adhesion of the dentures.
  • Natural and synthetic swelling agents are suitable as active ingredients.
  • plant gums such as e.g. Gum arabic, tragacanth and karaya gum as well as natural rubber.
  • alginates and synthetic swelling agents e.g. Sodium carboxymethyl cellulose, high molecular weight ethylene oxide copolymers, salts of poly (vinyl ether-co-maleic acid) and polyacrylamides.
  • auxiliaries for pasty and liquid products are hydrophobic bases, in particular hydrocarbons, such as white petroleum jelly (DAB) or paraffin oil.
  • hydrocarbons such as white petroleum jelly (DAB) or paraffin oil.
  • Fig. 1 shows schematically the DNA fragment of glucanase (Glu)
  • Fig. 5 shows the associated DNA and protein sequences (SEQ ID NO: 3 and 4) (see Example 1).
  • Fig. 2 shows schematically the DNA fragment of the hybrid enzyme from glucanase and small binding domain (KBD)
  • Fig. 6 shows the associated DNA and protein sequences (SEQ ID NO: 7 and 8) (see Example 2).
  • Fig. 3 shows schematically the DNA fragment of the hybrid enzyme from glucanase and large binding domain (GBD)
  • Fig. 7 shows the associated DNA and protein sequences (SEQ ID NO: 12 and 13) (see Example 3).
  • Fig. 4 shows schematically the DNA fragment of the hybrid enzyme from glucanase and medium binding domain (MBD)
  • Fig. 8 shows the associated DNA and protein sequences (SEQ ID NO: 17 and 18) (see Example 4).
  • the amplificate was cloned into the TA cloning vector (pGEM-Teasy, Promega) and transformed into XLIBIue MRF 'E. coli cells (Stratagene) (according to the manufacturer's instructions).
  • the isolated gene had to be transferred to a Bacillus expression system.
  • the plasmid was isolated from an overnight culture of the transformed E. coli cells using the QIAprep Spin Miniprep Kit (Qiagen).
  • the gene was then cut from the pGEM-Teasy vector with the restriction enzymes Bell and Sacl and integrated into the corresponding cleavage sites of the Henkel Bacillus expression vector pAWA31.
  • the transformed Bacillus subtilis cells were deficient before the transformation with glucanase (strain MW10, Bacillus Genetic Stock Center, Columbus, USA).
  • the small binding domain corresponds to the DNA range 238-276 base pairs from the sbsA gene (X71092) from Geobacillus stearothermophilus.
  • the gene codes for a Surface protein.
  • the sequence was added by extending the glucanase primer (without stop codon).
  • the stop codon was placed behind the region of the sbsA gene.
  • DNA was isolated from B. subtilis using the DNeasy Kit (Qiagen) using standard methods.
  • the gene was in a PCR reaction (1x PCR buffer, Gibco; 0.2 mM each dNTP, Gibco; 1, 5 mM MgCl 2 , Gibco; 2.5 U Taq polymerase, Gibco) with the primers GluBcl (5TGATCATGCCTTATCTGAAACGAG3 ') (SEQ ID NO: 5) and GluKyrSac (5'GAGCTCCTAACGGTATCGTTTTTTCGCTTTGTTGTATTCAGCATATACTTTTTTTG TAT AGCGC3 ") (SEQ ID NO: 6) (both 0.6 ⁇ M) in a thermal cycler (Eppendorf) under the following conditions
  • the amplificate was cloned into the TA cloning vector (pGEM-Teasy, Promega) and transformed into XLI BIue MRF 'E. coli cells (Stratagene) (according to the manufacturer's instructions).
  • the isolated gene had to be transferred to a Bacillus expression system.
  • the plasmid was isolated from an overnight culture of the transformed E. coli cells using the QIAprep Spin Miniprep Kit (Qiagen).
  • the gene was then cut from the pGEM-Teasy vector with the restriction enzymes Bell and Sacl and integrated into the corresponding cleavage sites of the Henkel Bacillus expression vector pAWA31.
  • the transformed Bacillus subtilis cells were deficient before the transformation with glucanase (strain MW10, Bacillus Genetic Stock Center, Columbus, USA).
  • Example 3 Isolation of the ⁇ -glucanase (EC 3.2.1.6, X00754) from B. subtilis with incorporation of the large positive binding domain (GBD):
  • the large positive binding domain corresponds to the DNA region 276-686 base pairs from the sbsC gene (AF055578) from Geobacilus stearothermophilus (DSM22).
  • the gene codes for a surface protein.
  • the sequence was isolated by PCR and ligated molecularly to the C-terminus of the glucanase. The ligation was carried out through a Kas interface, which functions as a linker between the two domains.
  • DNA was isolated from B. subtilis and G. stearothermophilus using the DNeasy Kit (Qiagen) using standard methods.
  • the glucanse gene without a stop codon was obtained in a PCR reaction from B. subtilis DNA (1x PCR buffer, Gibco; 0.2 mM each dNTP, Gibco; 1, 5 mM MgCl 2) Gibco; 2.5 U Taq polymerase, Gibco) with the primers GluBcl (5TGATCATGCCTTATCTGAAACGAG3 ') and GluKas (5'GGCGCCTTTTTTTGTATAG CGCACCC3') (SEQ ID NO: 9) (both 0.6 ⁇ M) in a Thermocyeler (Eppendorf) under the following Conditions amplified:
  • the gene segment from the sbsC gene from G. stearothermophilus DNA was analyzed in a PCR reaction (1x PCR buffer, Gibco; 0.2 mM each dNTP, Gibco; 1.5 mM MgCl 2 , Gibco; 2.5 U Taq polymerase , Gibco) with the primers KassbsC (5'GGCGCCGACAAAAAGAAAGCAGTCAAA3 ') (SEQ ID NO: 10) and SacsbsC (5OAGCTCTTAGCGCATTTTGTCTMTTTTG3 1 ) (SEQ ID NO: 11) (both 0.1 ⁇ M each) in a thermocyeler under the following conditions (Eppendorf amplified: 94 ° C 10 minutes 30 cycles:
  • a stop codon was inserted at the end of the sbsC section by the primer SacsbsC.
  • the fragments were cloned into the pGEM-Teasy vector (Promega) and transformed into JM110 cells (Stratagene).
  • Plasmids were isolated using the QiaPrep Spin Kit (Qiagen).
  • Glucanase The glucanase was isolated from the vector in two steps. plasmid
  • DNA was mixed with buffer A (final conc. 1x) and 50 units of Narl (both tubes) for 6 h at 37
  • the DNA was concentrated using the PCR purification kit (Qiagen) and then cleaved with 1x buffer M and 50 units Bell (Röche) at 37 ° C. for 3 h.
  • SbsC gene fragment: The sbsC gene fragment was isolated from the vector in two steps. Plasmid DNA was mixed with buffer A (final conc. 1x) and 50 units of Narl (both
  • Both fragments were separated from the vector on a preparative, 2% agarose gel, cut out under UV light and purified from the gel using the QIAquick Gel Extraction Kit (Qiagen).
  • Glucanase Approximately 20 ng of the glucanase were ligated with approx. 60 ng GBD in the presence of 1x ligation buffer and 0.5 U T4 ligase (Röche) at 4 ° C. overnight.
  • the ligation product was combined with the primers GluBcl and SacsbsC (both 0.6 ⁇ M each) in the presence of (1x PCR buffer, Qiagen; 0.3 mM each dNTP, Gibco; 2.5 U ProofStart DNA polymerase, Qiagen) in one Thermocyeler (Eppendorf) amplified under the following conditions:
  • the amplificate was integrated into the Henkel Bacillus expression vector pAWA31 via the built-in interfaces Bell and Sacl.
  • the transformed Bacillus subtilis Cells were deficient before transformation to glucanase (strain MW10, Bacillus Genetic Stock Center, Columbus, USA).
  • the middle positive binding domain is an artificially synthesized DNA segment, which is characterized in that it contains regions with positive charges.
  • the MBD was synthesized using two successive PCR reactions. The sequence is determined by the choice of the primers used. The primers themselves served as template DNA.
  • DNA was isolated from B. subtilis using the DNeasy Kit (Qiagen) using standard methods.
  • the glucanse gene without a stop codon was isolated in a PCR reaction from B. subtilis DNA (1x PCR buffer, Gibco; 0.2 mM each dNTP, Gibco; 1.5 mM MgCl 2 , Gibco; 2.5 U Taq - Polymerase, Gibco) with the primers GluBcl (5TGATCATGCCTTATCTGAAACGAG3 ') and GluKas (5'GGCGCCTTTTTTTGTATAG CGCACCC3') (both 0.6 ⁇ M each) amplified in a Thermocyeler (Eppendorf) under the following conditions:
  • the MBD was synthesized in two successive PCR reactions.
  • an 81 bp fragment was amplified in a Thermocyeler (Eppendorf) under the following conditions: 1x PCR buffer, Gibco; 0.2 mM per dNTP, Gibco; 1.5 mM MgCl 2) Gibco; 2.5 U Taq polymerase, Gibco Primer: PBD front
  • the 81 bp fragment was placed in a new PCR reaction (1x PCR buffer, Gibco; 0.2 mM each dNTP, Gibco; 1.5 mM MgCl 2 , Gibco; 2.5 U Taq polymerase, Gibco) with the primers PBDvorne
  • the fragments were cloned according to the manufacturer's instructions into the pGEM-Teasy vector (Promega) and transformed into XL1-Blue MRF 'cells (Stratagene).
  • Plasmids were isolated using the QiaPrep Spin Kit (Qiagen).
  • the glucanase was isolated from the vector in two steps. Plasmid DNA was cleaved with buffer A (final conc. 1x) and 50 units of Narl (both tubes) for 6 h at 37 ° C. The DNA was concentrated using the PCR purification kit (Qiagen) and then cleaved with 1x buffer M and 50 units Bell (Röche) at 37 ° C. for 3 h.
  • MBD The MBD fragment was isolated from the vector in two steps. Plasmid DNA was digested with buffer A (final conc. 1x) and 50 units of Narl (both tubes) for 3 hours at 37 ° C. and then split with an additional 25 units of Sacl (tubes) at 37 ° C. for 3 hours.
  • Both fragments were separated from the vector on a preparative, 2% agarose gel, cut out under UV light and purified from the gel using the QIAquick Gel Extraction Kit (Qiagen).
  • Glucanase Approximately 20 ng of the glucanase were ligated with approx. 60 ng MBD in the presence of 1x ligation buffer and 0.5 U T4 ligase (Röche) at 4 ° C. overnight.
  • the ligation product was combined with the primers GluBcl and PBDhinten (both 0.6 ⁇ M each) in the presence of (1x PCR buffer, Qiagen; 0.3 mM each dNTP, Gibco; 2.5 U ProofStart DNA polymerase, Qiagen) in one Thermocyeler (Eppendorf) amplified under the following conditions:
  • the amplificate was integrated into the Henkel Bacillus expression vector pAWA31 via the built-in interfaces Bell and Sacl.
  • the transformed Bacillus subtilis cells were deficient before the transformation with glucanase (strain MW10, Bacillus Genetic Stock Center, Columbus, USA).
  • a B. subtilis glucanase was cloned. This enzyme has been genetically engineered with three different, positively charged binding domains:
  • GluMBD glucanase + linker + artificial binding domain
  • GluKBD glucanase + small positively charged area from surface protein from G. stearothermophilus
  • GluGBB glucanase + linker + large positively charged area from surface protein from G. stearothermophilus. Fig. 1).
  • Example 7 p1 values of ⁇ -glucanase with different cationic binding units
  • the pl values were calculated in silico using the ExPASy Compute pl / Mw program (Bjellqvist, B., Hughes, GJ, Pasquali, Ch., Paquet, N., Ravier, F., Sanchez, J.-Ch., Frutiger, S. & Hochstrasser, DF
  • the focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 1993, 14, 1023-1031, Bjellqvist, B., Basse, B., Olsen, E. and Celis, JE Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions. Electrophoresis 1994, 15, 529-539).
  • Table 1 ⁇ -glucanase with small (KBD, VYAEYNKAKKRYR), medium (MBD, GAQL-KKKLQALKKKNAQLKWKLQALKKKLAQGGC) and large binding domain (GBD, GA-sbsC2-i3 ⁇ ) compared to the enzyme with KKEKK-binding

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Abstract

L'invention concerne des enzymes hybrides comprenant une unité à activité hydrolytique et une unité de liaison cationique, ainsi que des préparations contenant lesdites enzymes hybrides.
PCT/EP2004/013671 2003-12-13 2004-12-02 Enzymes hybrides a domaine de liaison cationique WO2005056744A1 (fr)

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WO2007025665A2 (fr) * 2005-09-02 2007-03-08 Henkel Kommanditgesellschaft Auf Aktien Agents de lavage
WO2007147814A1 (fr) * 2006-06-20 2007-12-27 Henkel Ag & Co. Kgaa Procédé de nettoyage
DE102006001148B4 (de) * 2006-01-06 2008-03-27 Henkel Kgaa Mund- und Zahnpflege und -reinigungsmittel mit Enzym(en)
US7424891B2 (en) 2005-09-02 2008-09-16 Henkel Ag & Co. Kgaa Detergents
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US9404069B1 (en) 2015-06-12 2016-08-02 Crossford International, Llc Systems and methods for cooling tower fill cleaning with a chemical gel
US10030216B2 (en) 2015-06-12 2018-07-24 Crossford International, Llc Systems and methods for cooling tower fill cleaning with a chemical gel

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CN109385382B (zh) * 2018-11-27 2021-10-26 合肥市东方美捷分子材料技术有限公司 一种污泥堆肥用复合菌剂的制备方法及其应用

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US8920576B2 (en) 2005-09-02 2014-12-30 Henkel Ag & Co. Kgaa Methods of removing stains and machine dishwashing methods
WO2007025665A3 (fr) * 2005-09-02 2007-05-03 Henkel Kgaa Agents de lavage
US7424891B2 (en) 2005-09-02 2008-09-16 Henkel Ag & Co. Kgaa Detergents
WO2007025665A2 (fr) * 2005-09-02 2007-03-08 Henkel Kommanditgesellschaft Auf Aktien Agents de lavage
DE102006001148B4 (de) * 2006-01-06 2008-03-27 Henkel Kgaa Mund- und Zahnpflege und -reinigungsmittel mit Enzym(en)
WO2007147814A1 (fr) * 2006-06-20 2007-12-27 Henkel Ag & Co. Kgaa Procédé de nettoyage
US8012267B2 (en) 2006-06-20 2011-09-06 Henkel Ag & Co. Kgaa Machine dishwashing method with separately metered liquid cleaning agents
WO2013037933A3 (fr) * 2011-09-14 2013-05-30 Dupont Nutrition Biosciences Aps Enzymes
CN103814129A (zh) * 2011-09-14 2014-05-21 杜邦营养生物科学有限公司 包含具有内切–1,4–β–木聚糖酶活性的酶和具有内切–1,3(4)–β葡聚糖酶活性的酶的组合物
CN106434246A (zh) * 2011-09-14 2017-02-22 杜邦营养生物科学有限公司 木聚糖酶的用途
US9683224B2 (en) 2011-09-14 2017-06-20 Dupont Nutrition Biosciences Aps Enzymes
EA027084B1 (ru) * 2011-09-14 2017-06-30 ДюПон НЬЮТРИШН БАЙОСАЙЕНСИЗ АпС Ферменты
US9404069B1 (en) 2015-06-12 2016-08-02 Crossford International, Llc Systems and methods for cooling tower fill cleaning with a chemical gel
US10030216B2 (en) 2015-06-12 2018-07-24 Crossford International, Llc Systems and methods for cooling tower fill cleaning with a chemical gel

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