CA2331137A1 - Laundry detergent and/or fabric care compositions comprising a modified cellulase - Google Patents

Abstract

The present invention relates to a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain (CBD) having a relative binding constant (Kr-a) for binding to amorphous cellulose higher than 2.4l/gcellulose, preferably higher than 3.5l/gcellulose, more preferably higher than 4l/gcellulose, for selective binding and hydrolysis of amorphous cellulose of cotton containing fabrics in a laundry and/or fabric care application. The present invention further relates to laundry detergent and/or fabric care compositions comprising this modified enzyme.

Description

LAUNDRY DETERGENT ANDIOR FABRIC CARE COMPOSITIONS
COMPRISING A MODIFIED CEI_LULASE
Field of the Invention The present invention relates to laundry detergent and/or fabric care compositions comprising a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain (CBD) having a relative binding constant (Kr-aj for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51lgcellulose, more preferably higher than 4 Ilgcellulose.
Background of the invention Detergent compositions include nowadays a complex combination of active ingredients and in particular, detergent enzymes such as cellulases.
The activity of cellulase is one in which cellulo:~ic fibres or substrates are attacked by the cellulase and is depending on the particular function of the cellulase, which can be endo- or exo- cellulase and on the respective hemicellulases. The cellulose structures are dep~olymerized or cleaved into smaller and thereby more soluble or dispersible fractions. This activity in particular on fabrics provides cleaning, rejuvenation, softening and generally improved handfeel characteristics to the fabric structure. This has been previously speculated to be the result of the cleavage of fibrils from the surface of fibres such that the main strand of the fibre beconnes smoother, less available for incrustation, less likely to entangle with other fibers and optically less diffuse in its light reflecting and emission.
Improvements in the activity of particular cellulase compositions have been made over time in order to allow lower usage or shorter exposure times for similar benefits. In the detergent feld, cellulase~s performing in a typical detergent wash environment are available with an <~ctivity at which the desired z cellulase performance is reached prior to the end of a wash-cycle. However, since the cellulase continues to react, even after having provided the desired performance, cleavage of the cellulose will continue. Therefore, there is a potential risk of tensile strength loss. .
It should be noted however, that tensile strength loss of fabric is also an unavoidable result of mechanical action due to u:>e/wearing and may further result from damage by a bleaching component in they laundry process, especially if the fabric is contaminated with metal compounds.
The object of the present invention is to provide laundry detergent andlor fabric care compositions which achieve excellent fabric care, including anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide static control, fabric softness, colour appearance and fabric anti-wear properties and benefits, and which achieve excellent fabric cleaning while preventing tensile strength loss.
The above objective has been met by formulating laundry detergent and/or fabric care compositions comprising a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain (CBD) haring a relative binding constant (Kr-a) for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51lgcelluloae, more preferably higher than 4l/gcellulose.
W091110732 discloses an enzyme which exhibits c:ellulase activity, producible by a strain of Bacillus spp., NICMB 40250, especially an 75, 56 or 45 kD
Molecular weight endoglucanase or characterised bay a high specific activity for e.g. detergency application, providing softening, soil removal and colour clarification. Novel derivatives of celiulase enzyme:; combining a core region derived from said endoglucanase with a CBD derived from another cellulase enzyme or a combining a core region derived from another cellulase enzyme with a CBD derived from said endoglucanase, are therein contemplated to construct cellulase enzymes with improved binding properties.
W094/07998 describes cellulase variants of a cellullase classified in family 45, comprising a CBD, a Catalytically Active Domain (CAD) and a region finking the CBD to the CAD, wherein one or more amino acid residues have been added, deleted or substituted andlor another CBD is added at the opposite end of the CAD. These enzymes have improved propertie:> such as alkaline activity, harshness reduction, compatibility with detergent ingredients, particulate soil removal, colour clarification, defuzzing, depilling, harshness reduction and sensitivity to anionic surfactants and peroxidase bleaching systems and are useful in detergent compositions.
W095I16782 relates to the cloning and high level expression of novel truncated cellulose proteins or derivatives thereof in Tn~choderma longibrachiatum.
Combinations of different core regions with severail CBDs are described in the fibrelfabric context.
A cellulolytic enzyme preparation comprising a cellulose with reduced mobility, e.g. by increasing the molecular weight ar apparent size of the cellulose protein molecule or by insolubilising or immobilising the cellulose, has been disclosed in W097/01629. The mobility of the cellulose component may be reduced by adsorption to an insoluble or soluble carrier e.g" via the existing or newly introduced CBD.
However, none of these documents disclose a modifiied enzyme which comprises a catalytically active amino acid sequence of a celluloiytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain having a Kr-a of a definite va#ue, thereby defining a cellulose especially adapted to selectively bind and hydrolyse amorphous cellulose of cotton containing fabrics for a laundry and/or fabric care application.
Summaryr of the invention The present invention relates a modified cellulolytic enzyme demonstrating selective binding and hydrolysis of amorphous cellulose in cotton containing fabrics. The present invention further relates to a laundry detergent andlor fabric care composition comprising said modified enzyme. Said compositions achieve excellent fabric care and fabric cleaning while preventing tensile strength loss.
This modified enzyme comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain {CBD) having a relative binding constant (Kr-a) for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 4l/gcellulose.
In a further embodiment of the present invention, the' present invention relates to a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain further characterised by having a relative binding constant for bacterial microcrystalline cellulose (Kr-c) lower than 1l/gcellulose, preferably lower than 0.5i/gcellulose.
More preferably, the modified enzyme of the present invention, comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain further characterised by having a relative binding cone~tant (Kr-a) for binding to amorphous cellulose to a relative binding constant lfor bacterial microcrystalline cellulose (Kr-c) ratio above 3.
The present invention further relates to laundry detergent and/or fabric care compositions comprising said modified enzyme and which preferably further comprise a detergent ingredient selected from cationic surfactants, dye transfer inhibiting polymer, builders, - in particular zeolite A and sodium tripolyphosphate andlor clays .
Detailed description of the invention The present invention relates to a modified enzyme which comprises a catalytically active amino acid sequence of a ceiluilolytic enzyme linked to an amino acid sequence comprising a cellulose binding domain having a relative binding constant for binding to amorphous cellulose higher than 2.411gcellulose, preferably higher than 3.511gcellulose, more preferably higher than 4 Ilgcellulose.
Cellulolytic enzyme A modified enzyme for use in accordance with the present invention comprises a catalytically active (enzymatically active) amino acid sequence {in general a polypeptide amino acid sequence) of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain having a high affinity for binding to amorphous cellulose.
The catalytically active amino acid sequence in question may comprise or consist of the whole of - or substantially the whole of - the full amino acid sequence of the mature enzyme in question, or it may consist of a portion of the full sequence which retains substantially the same catalytic (enzymatic) properties as the full sequence.
Modified enzymes (enzyme hybrids) of the type in question, as well as detailed descriptions of the preparation and purification thereof, are known in the art [see, e.g., WO 90/00609, WO 94/24158 and 1N0 95116782, as well as Greenwood et al., Biotechnology and Bioeng~inee~ri_ ngi 44, (1994) pp. 1295 -1305j. The praduction of enzymes hybrid is described in WO 91/10732 wherein novel derivatives of cellulase enzymes combining a core region derived from a Bacillus NICB 40250 endoglucanase with a CBD derived from another cellulase enzyme or a combining a core region derived from another ceilulase enzyme with a CBD derived from a Bacillus NICB 40250 endoglucanase, are constructed. WO 95/16782 describes the combinatiions of different core regions with several CBD and the cloning and high level expression of these novel truncated cellulase proteins or derivatives thereof, in Trichoderma longibrachiatum.
They may, e.g., be prepared by transforming into .a host cell a DNA construct comprising at least a fragment of DNA encoding the cellulose-binding domain ligated, with or without a Pinker, to a DNA sequence encoding the enzyme of interest, and growing the transformed host cell to express the fused gene. One relevant, but non-limiting, type of recombinant product (enzyme hybrid) obtainable in this matter - often referred to in the art as a "fusion protein'" - may be described by one of the following general formulae:
A-CBD-MFL-X-B

A-X-MR-CBD-B
In the latter formulae, CBD is an amino acid sequence comprising at least the cellulose-binding domain (CBD) per se.
MR (the middle region; a linking region) may be a bond, or a linking group comprising from 1 to about 100 amino acid residue~~, in particular of from 2 to 40 amino acid residues, e.g. from 2 to 15 amino aicid residues. MR may, in principle, alternatively be a non-amino-acid linker (See below).
X is an amino acid sequence cor~iprising the above-mentioned, catalytically (enzymatically) active sequence of amino acid residues of a polypeptide encoded by a DNA sequence encoding the cellulol~tic enzyme of interest.
The moieties A and B are independently optional. lNhen present, a moiety A or B constitutes a terminal extension of a CBD or X moiety, and normally comprises one or more amino acid residues.
It will thus, inter alia, be apparent from the above: that a CBD in an enzyme hybrid of the type in question may be positioned C-terminally, N-terminally or internally in the enzyme hybrid. Correspondingly, an X moiety in an enzyme hybrid of the type in question may be positioned N-terminally, C-terminally, or internally in the enzyme hybrid.
Enzyme hybrids of interest in the context of thE; invention include enzyme hybrids which comprise more than one CBD, e.g. :such that two or more CBDs are linked directly to each other, or are separated from one another by means of spacer or linker sequences (consisting typically of a sequence of amino acid residues of appropriate length. Two CBDs in an enzyme hybrid of the type in question may, for example, also be separated from one another by means of an -MR-X- moiety as defined above. One or more cellulose binding domain can be linked to the N-terminal andlor C-terminal parts of the cellulase core region.
Any part of a CBD can be selected, modified, truncated E~tc.
Preferably, attention will be given in the construction of enzyme hybrids of the type in question to the stability towards proteolytic degradation. Two- and multi-domain proteins are particularly susceptible towards proteolytic cleavage of linker regions connecting the domains. Proteases causing such cleavage may, for example, be subtilisins, which are known to often exhibit broad substrate specificities [see, e.g. : Grr~n et al., Biochemistry 31 (1992), pp. 6011-6018;
Teplyakov et al., Protein Enaineerinc 5 (1992), pp. 413-420]. Glycosylation of linker residues in eukaryotes is one Nature's ways of preventing proteolytic degradation. Another is to employ amino acids which are less favoured by the surrounding proteases. The length of the linker also plays a role in relation to accessibility by proteases. Which "solution" is optimal depends on the environment in which the enzyme hybrid is to function. When constructing new enzyme hybrid molecules, preferably attention will be paid to the linker stability.
Plasmids Preparation of plasmids capable of expressing fusion proteins having the amino acid sequences derived from fragments of more than one poiypeptide is well known in the art (see, for example, WO 90J0060~9 and WO 95/16782). The expression cassette may be included within a replication system for episomal maintenance in an appropriate cellular host or may be provided without a replication system, where it rnay become integratecl into the host genome. The DNA may be introduced into the host in accordance with known techniques such as transformation, microinjection or the like.
Once the fused gene has been introduced into the appropriate host, the host may be grown to express the fused gene. Normally it is desirable additionally to add a signal sequence which provides for secretion of the fused gene. Typical examples of useful genes are 1) Signal sequence -- (pro-peptide) -- carbohydratE;-binding domain -- linker --enzyme sequence of interest, or 2) Signal sequence -- (pr~-peptide} -- enzyme sequence of interest -- linker --carbohydrate-binding domain, in which the pro-peptide sequence normally contains 5-100, e.g. 5-25, amino acid residues. The recombinant product may be glycosylated or non-glycosylated.
Celiulolytic enzymes Any enzyme which exhibits a cellulase activity is suitable for the purpose of the present invention and includes cellulases without naturally occurring CBD, cellulase to which a CBD of Kr-a for binding to amorphous cellulose higher than 2.411gcellulose, preferably higher than 3.511gcellulose, more preferably higher than 4 IIgceHulose, is added and/or cellulases having a CBD presenting a lower Kr value, to which a CBD of Kr-a higher than 2.411gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 4 Ilgcellulose, is then substituted or added.
The catalytically active amino acid sequence of a cellulolytic enzyme can be derived from any cellulase. The cellulases usablEe in the present invention include both bacterial or fungal cellulases. Preferably, they will have a pH
optimum of between 5 and 12 and a specific activity above 50 CE9/Ulmg (Cellulose ~Aiscosity Unit). Suitable cellulases arE: disclosed in U.S. Patent 4,435,307, Barbesgoard et al, J61078384 and W096102653 which discloses fungal cellulase produced respectively from Huminola insolens, Trichoderma, Thielavia and Sporotrichum. EP 739 982 describes cellulases isolated from novel Bacillus species. Suitable cellulases are also disclosed in GB-A-2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and W095I26398.
Examples of such cellulases are cellulases produced by a strain of Humicola insolens (Humicola grisea var. thermoidea), particulairly the Numicola strain DSM
1800. Other suitable cellulases are cellulases originated from Humicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing 415 amino acids; and a -43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. WO 91/17243. Also suitable cellulases are the EG111 cellulases from Trichoderma longibrachiatum described in W094/21801, Genencor, published September 29, 1994. Especially suitable cellulases are the cellulases having colour care benefits. Examples of such cellulases are cellulases described in European patent application No. 91202879.2, filed November 6, 1991 (Novo).
Carezyme and Celluzyme (Novo Nordisk A/S) are especially useful. See also W091117244 and W091/21801. Other suitable cellulases for fabric care andlor cleaning properties are described in W096/34092, W096I17994 and W095/24471.

WO 99/57259 PCT/US99/094(19 Preferred catalytically active amino acid sequences of a celluiolytic enzyme for the laundry detergent andlor fabric care compositions of the present invention are producible by a fungal strain, preferably produced by a strain of Humicola insolens and more preferably is a "43kD endoglucanase derived from Hr~micola insolens, DSM 1800, exhibiting cellulose activity.
Said modified cellulolytic enzymes are normally incorporated in the laundry detergent and/or fabric care composition at levels from 0.0001 % to 2%, preferably 0.0001 % to 0.5%, more preferably 0.000.5% to 0.1 % of pure modified enzyme by vveight of the detergent composition.
Preferred catalytically active amino acid sequence of a cellulolytic enzyme for specific applications are derived from alkaline celluiases, i.e. enzymes having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of their maximum activity at a pH ranging from 7 to 12, preferably 10.5. More preferred core cellulases are enzymes having their maximum activity at a pH ranging from 7 to 12, preferably 10.5.
The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, ps,ychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Nowadays, it is common practice to modify wild-type enzymes via protein / genetic engineering techniques in order to optimise their performance efficiency in the laundry dei;ergent andlor fabric care compositions of the invention. For example, the variants may be designed such that the compatibility of the enzyme to commonly encountered ingredients of such compositions is increased. Alternatively, the variant may be designed such that the optimal pH, bleach or chelant stability, catalytic activity and the like, of the enzyme variant is tailored to suit the particular clE~aning application.
In particular, attention should be focused on amino acids sensitive to oxidation in the case of bleach stability and on surface charges for the surfactant compatibility. The isoelectric point of such enzyme's may be modified by the substitution of some charged amino acids, e.g. an increase in isoelectric point IO
may help to improve compatibility with anionic surfactants. The stability of the enzymes may be further enhanced by the creation of e.g. additional salt bridges and enforcing metal binding sites to increase cheian~t stability.
Cellulose Binding Domain (CBD}
Cellulose Binding Domains fn the present context, the terms "amino acid sequence comprising a CBD, Cellulose Binding Domain or CBD" are intended to indicate an amino acid sequence capable of effecting binding of the cellul;ase to a cellulosic substrate (e.g., as described in P. Kraulis et al., Determination of the three-dimensional structure of the C terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamically simulated annealing. Biochemistry 28:7241-7257, 1989).
The classification and properties of cellulose binding domains are presented in P. Tomme et al., in the symposium "Enzymatic degradation of insoluble polysaccharides" (ACS Symposium Series 618, edited by ,i.N. Saddler and M.H.
Penner, ACS, 1995).
Cellulose-binding (and other carbohydrate-binding} domains are polypeptide amino acid sequences which occur as integral parts of large polypeptides or proteins consisting of two or more polypeptide amino acid sequence regions, especially in hydrolytic enzymes (hydrolases) which ilypically comprise a catalytic domain containing the active site for substrate hydrolysis and a carbohydrate-binding domain for binding to the carbohydrate substrate in question. Such enzymes can comprise more than one catalytic domain and one, two or three carbohydrate-binding domains, and they may further comprise one or more polypeptide amino acid sequence regions linkinc; the carbohydrate-binding domains) with the catalytic domain(s), a region of i;he latter type usually being denoted a "linker".
Examples of hydrolytic enzymes comprising a cellulose-binding domain are cellulase, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. "Cellulose-binding domains" have also been found in algae, e.g. in the red alga porphyra purpurea in the form of a non-hydrolytic polysaccharide-binding protein jsee P. Tomme et al., Cellulose-binding domains -Classification and Properties in En~matic Degradation of Insoluble CarbohKdrates , John N.
Saddler and Michael H. Penner (Eds.}, ACS Symposium Series, No: 618 (1996)]. However, most of the known CBDs (which are classified and referred to by P. Tomme et al. (op. cit.) as "cellulose-binding domains" derive from cellulases and xylanases.
In the present context, the term "cellulose-binding domain" is intended to be understood in the same manner as in the latter reference (P. Tomme et al., op.
cit. } The P. Tomme et al. reference classifies more than 120 "cellulose-binding domains" into 10 families (I-X) which may have dlifferent functions or roles in connection with the mechanism of substrate binding. However, it is to be anticipated that new family representatives and additional families will appear in the future.
in proteinslpolypeptides in which CBDs occur (e.g. enzymes, typically hydrolytic enzymes such as cellulases), a CBD may be located at the N or C terminus or at an internal position.
The part of a polypeptide or protein (e.g. hydrolytic enzyme) which constitutes a CBD per se typically consists of more than about 30 and less than about 250 amino acid residues. For example, those CBDs listed and classified in Family I
in accordance with P. Tomme et al. (op. cit.) consist of 33-37 amino acid residues, those listed and classified in Family Ila consist of 95-108 amino acid residues, those listed and classified in Family VI consist of 85-92 amino acid residues, whilst one CBD (derived from a cellulase from Clostridium thermocellum) fisted and classified in Family VII consists of 240 amino acid residues. Accordingly, the molecular weight of an amino acid sequence constituting a CBD per se will typically be in the range of from about 4kD to about 40kD, and usually below about 35kD.
Cellulose binding domains can be produced by recombinant techniques as described in H. Stalbrand et al., Applied and Environmental Microbiology, Mar.
1995, pp. 1090-1097; E. Brun et al., (1995) Eur. J. Biochem. 237, pp. 142-148;
J.B. Coutinho et al., (1992) Molecular Microbiology 6(9,, pp. 1243-1252 In order to isolate a cellulose binding domain of, e.g. a cellulose, several genetic engineering approaches may be used. One method uses restriction enzyme to remove a portion of the gene and then to fuse the remaining gene-vector fragment in frame to obtain a mutated gene that encodes a protein truncated for a particular gene fragment. Another method involves the use of exonucleases such as Ba131 to systematically delete nucleotides either externally from the 5' and the 3' ends of the DNA or internally from a restricted gap within the gene.
These gene-deletion methods result in a mutated gene encoding a shortened gene molecule whose expression product may then be evaluated for substrate-binding (e.g. cellulose-binding) ability. Appropriate substrates for evaluating the binding ability include cellulosic materials such as Avicel T"" and cotton fibres.
Other methods include the use of a selective or :specific protease capable of cleaving a CBD, e.g. a terminal CBD, from the remainder of the polypeptide chain of the protein in question.
As already indicated {vide supra), once a nucleotide sequence encoding the substrate-binding (carbohydrate-binding) region has been identified, either as cDNA or chromosomal DNA, it may then be manipulated in a variety of ways to fuse it to a DNA sequence encoding the enzyme o~r enzymatically active amino acid sequence of interest. The DNA fragment encoding the carbohydrate-binding amino acid sequence, and the DNA encoding the enzyme or enzymatically active amino acid sequence of interest are then ligated with or without a linker. The resulting ligated DNA may then be manipulated in a variety of ways to achieve expression. Preferred microbial expression hosts include certain Aspergillus species (e.g. A. niger or A. oryzae), Bacillus species, and organisms such as Escherichia coli or Saccharomyc:es cerevisiae.
The Cellulose Binding Domains of the present invention The relative binding constant Kr for binding to regenerated cellulosic (amorphous - PASC phosphoric acid swollen cellulose) or crystalline cellulose (bacterial microcrystalline cellulose - BMCC) celiuloses at 4°C and pH
7.0 is defined as Kr = [NO]Ka and determined from the slope of a plot of 1/[Xb] vs 11[Xf], using a double-weighted, least-squares analysis; wherein [Nd] is the concentration of binding sites in the absence of ligand (mol(g of cellulose)-1 ), Ka is the equi9ibrium association constant {L mol-1}, [Xb] is the concentration of bound ligand (mol (g of cellulose)-1 ) and [Xf] is the concentration of free ligand (molar) (N.R. Gilkes et al., (1992) J. Biol. Chem. ;267, pp. 6743-6749) such as described in P.E. Johnson et ai., (1996) Biochem. ~i5, 13895-13906.
Microcrystalline cellulose (Avicel PH101) can be obtained from FMC
International (Little Island, County. Cork, Ireland). Bacterial rnicrocrystailine cellulose (BMCC) can be prepared from cultures of Acetobacter xylinum (ATCC
23769) as described in Gilkes at al. 1992. Regenerated cellulose (PASO) can be obtained by phosphoric-acid treatment of Avicel PH101 as reported in J. B.
Coutinho at al., (1992) Mol. Microbioi. 6, 1243-1252;.
Suitable CBDs for the purpose of the present invention are the CBDs derived from a fungal or bacterial strain, preferably a bacterial strain, more preferably from Family Il or IV according the current classificai:ion [See P. Tomme et al. (op cit.)]; having a relative binding consfant (Kr-a} for binding to amorphous cellulose higher than 2.41lgcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 411gcellulose ceilulase.
More preferred CBDs are CBDs from family IV as. currently classified, derived from organisms selected from Cellulomonas fi,mi, Clostridium stecorarium (NCIMB11754), Clostridium cellulolyticum, Myxocccus xanthus, Streptomyces reticuli andlor Thermomonospora fusca. Most preferred CBDs are the CBDs selected from CBDs of the tandem N-terminal cellulose binding domains from Cellulomonas ~mi [3-1,4-glucanase CenC which binds amorphous but not crystalline cellulose (P.E. Johnson et al., (1996) Biochem. 35, 13895-13906 and 14381-14394; J.B. Coutinho et al., (1992) Molecular Microbiology 6(9), pp.
1243-1252}, CBD-dimer from Clostridium stecomrium (NCIMB11754) XynA
andlor the CBD E3 from Thermonospora fusca.
Preferably, the cellulose binding domains for tl7e purpose of the present invention will be further characterised by having a relative binding constant for crystalline cellulose (Kr-c) lower than 1l/gceliul~ose, preferably lower than 0.51lgceliulose.

More preferably, the modified enzyme of the present invention comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain {CBD) .further characterised by having a relative binding constant {Kr-a) for binding to amorphous cellulose to a relative binding constant for crystalline cellulose (Kr-c) ratio above 3.
Even more preferably for the purpose of the present invention, the modified enzyme comprising a catalytically active (enzymatically active) amino acid sequence of a cellulolytic enzyme linked to CBD as defined in the present invention, will provide an enzymatic hydrolysis activity on phosphoric acid-swollen cellulose higher than 60 moles glucose equivalents released per minute and per mole enzyme. Activities were determined air 37°C and pH7 (N.
Din et al., (1995) Prog. Biotech. 90, pp. 261-270).
Linking region The term "linker" or "linking region" or "Middle region- MR" is intended to indicate a region that might adjoin the CBD and connect it to the catalytically active amino acid sequence of the cellulolytic enzyme. When present, this linking can be achieved chemically or by recombinant technique's.
An example of the recombinant technique describing the expression of an enzyme with the CBD of different origin is described in S. Karita et al., (1996) Journal of Fermentation and Bioengineering, Vol. 81, No. 6, pp. 553-556.
Preferred linking regions are amino acid (peptides), some examples thereof are described in N.R. Gilkes et al., Microbiol. Rev. 55, 1991, pp. 303-315. The linking regian can comprise from 1 to about 1 ()0 amino acid residues, in particular of from 2 to 40 amino acid residues, e.g. from 2 to 15 amino acid residues. As stated above, it is preferred to use amino acids which are less favored by the surrounding proteases. Suitable amino acid linking regions are the HumicoBa insolens family 45 cellulase linker, the NifA gene of Klebsie!!a pneumoniae-CiP linker, the E. coli OmpA gene-CiP linker, the E3 cellulase Thermomon~spora fusca linker and the CenA cellulase linker.; preferably the Humicola insoJens family 45 cellulase linker and the E3 cellulase Thermomonospora fusca linker.
Non amino acid/proteinic compounds, referred to as "non-amino acid" can also be used for the linking of the catalytically active .amino acid sequence to the CBD:
1 ) Suitable non-amino acid linking regions acre the polyethylene glycol derivatives described in the Shearwater polymers, Inc. catalog of January 1996, such as the nucleophilic PEGs, the carboxyl PEGs, the electrophilicaily activated PEGs, the sulfhydryl-selective PEGs, the heterofunctional PEGs, the biotin PEGS, the vinyl derivatives, the PEG silanes and the PEG phospholipids. In particular, suitable non-amino acid linking regions are the heterofunctional PEG, (X-PEG-Y) polymers from Shearwater such as P~EG(NPC)2, PEG-(NH2)2, t-BOC-NH-PEG-NH2, t-BOC-NH-PEG-C02NHS, OH-PEG-NH-tBOC, FMOC-NH-PEG-C02NHS or PEG(NPG)2 MW 3400 from Sigma, glutaric dialdehyde 50 wt% solution in water from Aldrich, disuccinimidyl suberate (DSS) form Sigma, y-maleimidobutyric acid N-hydroxysuccinimide ester (GMBS) from Sigma, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC) from Sigma and dimethyl suberimidate hydrochloride (DMS) from Sigma.
2) Other suitable non-amino acid linking regions are 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide, N-ethyl-5-phenylisoaxolium-3-sulphonate, 1-cyclohexyl-3(2morpholinoethyl) carbodide metho-p-toluene sulphonate, N-ethoxycarbonyl-2-ethoxy 1,2, dihydroquinoline or glutaraldehyde.
3) Also suitable are the crosslinkers described in the 199912000 Pierce Products Catalogue from the Pierce Company, under the heading "Cross linking reagents the SMPH, SMCC, LC-SMCC compounds, and preferably the Sulfo-KMUS
compound.
Preferred chemical linking regions are PEG(NPC)2, (NH2)2-PEG, t-BOC-NH-PEG-NH2, MAL-PEG-NHS, VS-PEG-NHS polymers from Shearwater andlor the Sulfo-KMUS compound from Pierce.
Detergent comJ~onents The laundry detergent andlor fabric care compositions of the invention will comprise at least one additional detergent andlor fabric care components. The 1&
precise nature of these additional components, and levels of incorporation thereof will depend on the physical form of the composition, and the nature of the cleaning operation for which it is to be used.
The laundry detergent andlor fabric care compositions of the present invention preferably further comprise a detergent ingredient selected from cationic surfactants, dye transfer inhibiting polymers, builders - in particular zeolite A and sodium tripolyphosphate - and/or clays. These laundry detergent and/or fabric care compositions achieve improved~fabric care, in<;luding improved anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide enhanced static control, fabric softness, colour appearance and fabric anti-wear properties and benefits and improved fabric cleaning while preventing tensile strength Toss.
The laundry detergent and/or fabric care compositions according to the invention can be liquid, paste, gets, bars, tablets, spray, foam, powder or granular forms.
Granular compositions can also be in "compact" norm, the liquid compositions can also be in a "concentrated" form.
The compositions of the invention may for example, be formulated as hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the soaking and/or pretreatment of stained fabrics, rinse added fabric softener compositions. Pre-or post treatment of fabric include gel, spray and liquid fabric care compositions. A rinse cycle with or without the presence of softening agents is also contemplated.
iNhen formulated as compositions suitable for use in a laundry machine washing method, the compositions of the invention preferably contain both a surfactant and a builder compound and additionally one or more detergent components preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersant:>, lime-soap dispersants, soil suspension and anti-redeposition agents and corrosion inhibitors. Laundry compositions can also contain softening agenia, as additional detergent components.

The compositions of the invention can also be used as detergent additive products in solid or liquid form. Such additivE~ products are intended to supplement or boost the performance of conventional detergent compositions and can be added at any stage of the cleaning process.
If needed the density of the laundry detergent compositions herein ranges from 400 to 1200 gllitre, preferably 600 to 950 g/litre of composition measured at 20°C.
The "compact" form of the compositions herein is best reflected by density and, in terms of composition, by the amount of inorganic filler salt; inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are present in substantial amounts, typically 17-35% by weight of the total composition. In the compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, most preferably not exceeding 5%
by weight of the composition. The inorganic filler salts, such as meant in the present compositions are selected from the alkali and alkaline-earth-metal salts of sulphates and chlorides. A preferred filler salt is sodium sulphate.
Liquid detergent compositions according to the preaent invention can also be in a "concentrated form", in such case, the liquid detergent compositions according the present invention will contain a lower amount of water, compared to conventional liquid detergents. Typically the water content of the concentrated liquid detergent is preferably less than 40%, mores preferably less than 30%, most preferably less than 20% by weight of the detergent composition.

Surfactant system The laundry detergent and/or fabric care compositions according to the present invention comprise a surfactant system wherein the surfactant can be selected from nonionic and/or anionic and/or cationic and/or ampholytic and/or zwitterionic and/or semi-polar surfactants. Preferred surfactants are cationic surfactants. It has been surprisingly found that the laundry detergent and/or fabric care compositions further comprising a .cationic surfactant, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide enhanced static control, fabric softness, colour appearance and fabric anti-wear properties and benefits and improved fabric cleaning while preventing tensile strength loss.
The surfactant is typically present at a level of from 0.1 % to 60% by weight.
More preferred levels of incorporation are 1 % to 35'% by weight, most preferably from 1 % to 30% by weight of laundry detergent and/or fabric care compositions in accord with the invention.
The surfactant is preferably formulated to be~ compatible with enzyme components present in the composition. In liquid or gel compositions the surfactant is most preferably formulated such that lit promotes, or at least does not degrade, the stability of any enzyme in these compositions.
Cationic detersive surfactants suitable for use in the laundry detergent and/or fabric care compositions of the present invention are those having one long-chain hydrocarbyl group. Examples of such cationic surfactants include the ammonium surfactants such as alkyltrimethylammonium halogenides, and those surfactants having the formula [RZ(OR3)yl~R4(OR3)yl2Rbf~+~-wherein R2 is an alkyl or alkyl benzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R3 is selected from the group consisting of -CHZCH2-, -CH2CH(CHg)-, -CH2CH(CH20H)-, -CH2CH2CH2-, and mixtures thereof; each R4 is selected from the group consisting of C1-C4 alkyl, C1-C4 hydroxyaikyl, benzyl ring structures formed by joining the two R4 groups, -CH2CHOH-CHOHCOR6CHOHCH20H wherein Rf~ is any hexose or hexose polymer having a molecular weight less than about 1000, and hydrogen when y is not 0; R5 is the same as R4 or is an alkyl chain wherein the total number of carbon atoms of R~ plus R5 is not more than about 18; each y is from 0 to about and the sum of the y values is from 0 to about 15; and X is any compatible anion:
Quaternary ammonium surfactant suitable for they present invention has the formula (I):
RZ ~ s' ' ''R4 R
~~O ~Rs ,K-Formula I
whereby R1 is a short chainlength alkyl (C6-C10) or alkylamidoalkyl of the formula (II) C6-C.~ N
~CH~
O
Formula II
y is 2-4, preferably 3.
whereby R2 is H or a C1-C3 alkyl;
whereby x is 0-4, preferably 0-2, most preferably 0, whereby R3, R4 and R5 are either the same or diifferent and can be either a short chain alkyl (C1-C3) or alkoxylated alkyl of the formula III, whereby X- is a counterion, preferably a halide, e.g. chloride or methyfsulfate.
Rs ~H
O z Formula III

R6 is C1-C4 and z is 1 or 2.
Preferred quat ammonium surfactants are those as defined in formula t whereby R1 is Cg, C1p or mixtures thereof, x=o, R3, R4 = CH3 and R5 = CH2CH20H.
Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition having the formula R1 R2R3R4N+X- (i) wherein R1 is Cg-C1g alkyl, each of R2, R3 and R4 is independently C1-C4 alkyl, C1-C4 hydroxy alkyl, benzyl, and -(C2H40)xEi where x has a value from 2 to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl.
The preferred alkyl chain length for R1 is G12-C1;5 particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or OXO alcohols synthesis. Preferred groups for R2R3 and R4 are methyl and hydroxyeahyl groups and the anion X
may be selected from halide, methosulphate, acetaite and phosphate ions.
Examples of suitable quaternary ammonium compounds of formutae (i) for use herein are coconut trimethyl ammonium chloride or bromide;
coconut methyl dihydroxyethyl ammonium chloride or bromide;
decyl triethyl ammonium chloride;
decyl dimethyt hydroxyethyl ammonium chloride or bromide;
C12-15 dimethyl hydroxyethyl ammonium chloride or bromide;
coconut dimethyl hydroxyethyl ammonium chloricle or bromide;
myristyl trimethyl ammonium methyl sulphate;
lauryl dimethyl benzyl ammonium chloride or bromide;
lauryl dimethyl {ethenoxy)4 ammonium chloride c~r bromide;
choline esters (compounds of formula (i) wherein R1 is CH2-CHI-O-C-C12-14 alkyl and R2R3R4 are methyl).
O
di-alkyl imidazolines [compounds of formula (i)].

WO 99/57259 PCT/tJS99/09409 Other cationic surfactants useful herein are also described in U.S. Patent 4,228,044, Cambre, issued October 14, 1980 and in European Patent Application EP 000,224.
Typical cationic fabric softening components include the water-insoluble quaternary-ammonium fabric softening actives or the corresponding amine precursor, the most commonly used having been cli-long alkyl chain ammonium chloride or methyl sulfate.
Preferred cationic softeners among these include the following:
1} ditallow dimethylammonium chloride (DTDMAC);
2) dihydrogenated tallow dimethylammonium chloride;
3) dihydrogenated tallow dimethylammonium methylsulfate;
4) distearyl dimethylammonium chloride;
5) dioleyl dimethylammonium chloride; , 6) dipalmityl hydroxyethyl methylammonium chloride;

7) stearyl benzyl dimethylarnmonium chloride;

8) tallow trimethylammonium chloride;

9) hydrogenated tallow trimethylammonium chloride;

10) C12-14 alkyl hydroxyethyl dimethylammonium chloride;

11 ) C12_~ g alkyl dihydroxyethyl methylammonium chloride;

12) di(stearoyioxyethyl) dimethylammonium chloride (DSOEDMAC);

13) di(tallow-oxy-ethyl) dimethylammoniunn chloride;

14) ditailow imidazolinium methylsulfate;

15} 1-(2-tallowylamidoethyl)-2-talfowyl imiciazolinium methylsulfate.
Biodegradable quaternary ammonium compounds have been presented as alternatives to the traditionally used di-long alkyl chain ammonium chlorides and methyi sulfates. Such quaternary ammonium compounds contain long chain alk(en}yl groups interrupted by functional groups such as carboxy groups. Said materials and fabric softening compositions containing them are disclosed in numerous publications such as EP-A-0,040,562, and EP-A-0,239,910.
The quaternary ammonium compounds and amine precursors herein have the formula (I} or (I1), below R3~ /RZ _ +\i/ (CH2)rnCH -CHI X
N (C~)ri Qw'1' 1 X R3 Q
Rt T: T2 or wherein Q is selected from -O-C(O)-, -C(O)-O-, -O-C(O)-O-, -NR4-C(O)-, -C(O)-N R4-;
R1 is (CH2)n-Q-T2 or T3;
R2 is (CH2)m-Q-T4 or T5 or R3;
R3 is C1-C~ alkyl or C1-C~ hydroxyalkyi or H;
R4 is H or C1-C4 alkyl or C1-Cq. hydroxyalkyl;
T1, T2, T3, T4, T5 are independently C11-C22 alkyl or alkenyl;
n and m are integers from 1 to 4; and X- is a softener-compatible anion.
Non-limiting examples of softener-compatible anions include chloride or methyl sulfate.
The alkyl, or alkenyl, chain T1, T2, T3, T4, T~ muat contain at least 11 carbon atoms, preferably at least 16 carbon atoms. The chain may be straight or branched.
Tallow is a convenient and inexpensive source of long chain alkyl and alkenyl material. The compounds wherein T1, T2, T~, T4, Tb represents the mixture of long chain materials typical for tallow are particularly preferred.
Specific examples of quaternary ammonium compounds suitable for use in the aqueous fabric softening compositions herein include 1) N,N-di{tallowyl-oxy-ethyl)-N,N-dimethyl ammonium chloride;
2) N,N-di{tallowyl-oxy-ethyl)-N-methyl, N-{2-hydroxyethyl) ammonium methyl sulfate;
3) N,N-di(2-tallowyl-oxy-2-oxo-ethyl)-N,N-dimethyl ammonium chloride;

WO 99/57259 PCT/~JS99/09409 4) N,N-di(2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl)-N,N-dimethyl amrrionium chloride; .
5) N-(2-tallowyl-oxy-2-ethyl)-N-(2-tallowyl-oxy-2-ox;o-ethyl)-N,N-dimethyl ammonium chloride;
6) N,N,N-tri(tallowyl-oxy-ethyl)-N-methyl ammonium chloride;
7) N-(2-tallowyi-oxy-2-oxo-ethyl)-N-(tallowyl-N,N-diimethyl-ammonium chloride;
and 8) 1,2-ditallowyl-oxy-3-trimethylamrrioniopropane chloride;
and mixtures of any of the above materials.
When included therein, the laundry detergent and/or fabric care compositions of the present invention typically comprise from 0.2"/° to about 25%, preferably from about 1 % to about 8°/~ by weight of such cationic surtactants.
Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl phenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with the polyethylene oxide condensates being preferred. These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms" in either a straight-chain or branched-chain configuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount equal to from about 2 to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene oxide per mole of alkyl phenol. Commercially available nonionic surfactants of this type include IgepaIT~ CO-630, marketed by the GAF Corporation; and TritonTM X-45, X-114, X-100 and X-102, all marH;eted by the Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkyl phenol ethoxylates).
The condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention.
The alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products ~of alcohols having an alkyl group containing from about 8 to about 20 carbon atoms, more preferably from about 10 to about 18 carbon atoms, with from ak>out 2 to about 10 moles of ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide and most preferably from 2 to 5 moles of ethylene oxide per mole of alcohol 'are present in said condensation products. Examples of commercially available nonionic surfactants of this type include TergitoIT~M 15-S-9 (the condensation product of C11-C15 linear alcohol with 9 moles ethylene oxide), TergitoITM 24-L-6 NMW (the condensation product of C12-C14 primary alcohol with 6 moles ethylene oxide with a narrow molecular weight distribution), both marketed by Union Carbide Corporation; NeodoITM 45-9 (the condensation product of C14-C15 linear alcohol with 9 moles of ethylene oxide), NeodoITM 23-3 (the condensation product of C12-C13 linear alcohol with 3.0 moles of ethylene oxide), NeodoITM 45-7 {the condensation product of C14-C15 linear alcohol with 7 moles of ethylene oxide), NeodoITM 45-5 (the condensation product of C14-C15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company, KyroTM EOB {the condensation product of C13-C15 alcohol with 9 moles ethylene oxide), marketed by The Procter' & Gamble Company, and Genapol LA 030 or 050 (the condensation product of C12-C14 alcohol with 3 or 5 moles of ethylene oxide) marketed by Hoechst;. Preferred range of HLB in these products is from 8-11 and most preferred from 8-10.
Also useful as the nonionic surfactant of the surfactant systems of the present invention are the alkylpolysaccharides disclosed in U.S. Patent 4,555,647, Llenado, issued January 21, 1985, having a hydro~>hobic group containing from about 5 to about 30 carbon atoms, preferably from abaut 10 to about 1fi carbon atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units., Any reducing saccharide containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and galactosyl moieties can be substituted for the glucosyl moieties (optionally the hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glucoside or galactoside). The intersaccharide bonds can be, e.g., between the one position of the additional saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding saccharide units.

The preferred alkylpolyglycasides have the formula R2o(CnH2no)t(9lYcosyl;~x wherein R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about '10, preferably 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7. The glycosyl is preferalbly derived from glucose.
To prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attachment at the 1-position). The additional glycosyl units can then be attached between their 1-position and the precediing glycosyl units 2-, 3-, 4-andlor 6-position, preferably predominately the 2-poaition.
The condensation products of etihylene oxide with a hydrophobic base formed by the condensation of propylene oxide with propylene glycol are also suitable for use as the additional nonionic surfactant systems of the present invention.
The hydrophobic portion of these compounds will preferably have a molecular weight of from about 1500 to about 1800 and will exhibit water insolubility.
The addition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50% of the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide. Examples of compounds of this type include certain of the comrn~;rcially-available PlurafacTM
LF404 and PluronicTM surfactants, marketed by BA;iF.
Also suitable for use as the nonionic surfactant of the' nonionic surfactant system of the present invention, are the condensation proclucts of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine.
The hydrophobic moiety of these products consist:> of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of from about 2500 to about 3000. Tlhis hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11,~D00. Examples of this type of nonionic surfactant include certain of the commercially available TetronicTM
compounds, marketed by BASF.
Preferred for use as the nonionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylerie oxide, alkylp~olysaccharides, and mixtures thereof. Most preferred are Cg-C14 alkyl phenol etlhoxylates having from 3 to ethoxy groups and Cg-C1g alcohol ethoxylates (preferably C10 avg.) having from 2 to 10 ethoxy groups, and mixtures thereof.
Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula.
R2-C-N-Z, wherein R1 is H, or R1 is C1_4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R2 is C5_31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyi having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof. Preferably, R1 is methyl, R2 is a straight C11_15 alkyl or C1g_1g alkyl or aikenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive amination reaction.
Suitable anionic surfactants to be used are linear alkyl benzene sulfonate, alkyl ester sulfonate surfactants including linear esters of Cg-C20 carboxylic acids (i.e., fatty acids) which are sulfonated with gaseous S03 according to "The Journal of the American Oil Chemists Society°°, 52 (19?5), pp.
323-329. Suitable starting materials would include natural fatty substances as derived from tallow, palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especially for laundry applications, comprise alkyl ester sulfonate surfactants of the struictural formula:

O
I I

I

wherein R3 is a Cg-C2p hydrocarbyl, preferably an alkyl, or combination thereof, R4 is a C1-C6 hydrocarbyl, preferably an alkyl, or combination thereof, and M
is a ration which forms a water soluble salt with the alkyl ester sulfonate.
Suitable salt-forming rations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium rations, such as mono-ethanolamine, diethanolarnine, and triethanolamine. Preferably, R3 is C10-C1g alkyl, and R4 is methyl, ethyl or isopropyl. Especially preferred are the methyl ester sulfonates wherein R3 is C10-C1g alkyl.
Other suitable anionic surfactants include the alkyl sulfate surfactants which are water soluble salts or acids of the formula ROSO~sM wherein R preferably is a C10-C24 hYdrocarbyl, preferably an alkyl or hydroxyalkyl having a C10-C20 alkyl component, more preferably a C12-C18 alkyl or hydroxyalkyl, and M is H or a ration, e.g., an alkali metal ration (e.g. sodium, potassium, lithium), or ammonium or substituted ammonium (e.g. methyl-, dimethyl-, and trimethyl ammonium rations and quaternary ammonium rations such as tetramethyl-ammonium and dimethyl piperdinium rations and quaternary ammonium rations derived from alkylamines such as ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like). Typically, alkyl chaiins of C12-C16 are preferred for lower wash temperatures (e.g. below about 50°C) and C16-18 alkyl chains are preferred for higher wash temperatures (e.g. above about 50°C).
Other anionic surfactants useful for detersive purposes can also be included in the laundry detergent andlor fabric care compositions of the present invention.
These can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono-, di-~ and triethanolamine salts) of soap, Cg-C22 primary of secondary alkanesulfonates, Cg-C24 olefinsulfonates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No. 1,082,179, Cg-C24 alkylpolyglycolethersulfates (containing up to 10 moles of ethylene oxide); alkyl glycerol sulfonates, fatty ;aryl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isethionates such as the aryl isethionates, N-aryl taurates, alkyl succinarnates and sulfosuccinates, rnonoesters of sulfosuccinates (especially saturated and unsaturated C~2-C1g imonoesters) and diesters of sulfosuccinates (especially saturated and unsatuirated Cg-C12 diesters), aryl sarcosinates, sulfates of alkyipolysaccharides such as the sulfates of alkylpolyglucoside (the nonionic nonsulfated compounds being described below), branched primary alkyl sulfates, and alkyl polyethoxy carboxylates such as those of the formula RO(CH2CH20)k-CH2C0C)-M+ wherein R is a Cg-C22 alkyl, k is an integer from 1 to 10, and M is a soluble salt-forming ration.
Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil.
Further examples are described in °'Surface Active Agents and Detergents" {Vol.
I and II by Schwartz, Perry and Berch). A variety of such surfactants are also generally disclosed in U.S. Patent 3,929,678, is:>ued December 30, 1975 to Laughiin, et al. at Column 23, line 58 through Column 29, line 23 (herein incorporated by reference).
When included therein, the laundry detergent compositions of the present invention typically comprise from about 1 % to about 40%, preferably from about 3% to about 20% by weight of such anionic surfactants.
Highly preferred anionic surfactants include alkyl alkoxylated sulfate surfactants hereof are water soluble salts or acids of the formula RO(A)mS03M wherein R
is an unsubstituted C10-C24 alkyl or hydroxyalkyl group having a C10-C24 alkyl component, preferably a C12-C20 alkyl or hydroxyalkyl, more preferably C12-C1g alkyl or hydroxyalkyl, A is an ethoxy or propox~~ unit, m is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, and M is H or a ration which can be, for example, a metal ration (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substituted-ammonium ration. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium rations include methyl-, dimethyl, trimc~thyl-ammonium rations and quaternary ammonium rations such as tetramethyl-ammonium and dimethyl piperdinium rations and those derived from alkyl:amines such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. Exemplary surfactants are C12-C18 alkyl polyethoxylate (1.0) sulfate (C12-CIgE{1.0)M), C12-C1g alkyl polyethoxylate (2.25) sulfate (C12-C18E(2.25)M), (~12-C1g alkyl polyethoxylate (3.0) sulfate (C12-C18E(3.0)M), and C12-C18 alkyl polyethoxylate (4.0) sulfate (C12-C18E(4.0)M), wherein M is conveniently selected from sodium and potassium.
The laundry detergent and/or fabric care compositiions of the present invention may also contain ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic andlor anionic surfactants other than those already described herein.
Ampholytic surfactants are also suitable for use in the laundry detergent and/or fabric care compositions of the present invention.. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight- or branched-chain. One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic water-solubilizing group, e.g. carboxy, sulfonate, sulfate. See U.S. Patent No. 3;929,fi78 to Laughlin et al., issued December 30, 1975 at ~;,olumn 19, lines 18-35, for examples of ampholytic surfactants.
When included therein, the laundry detergent and/or fabric care compositions of the present invention typically comprise from 0.2'% to about 15%, preferably from about 1 % to about 10% by weight of such amp~holytic surfactants.
Zwitterionic surfactants are also suitable for use in laundry detergent andlor fabric care compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. See U.S. Patent No.
3,929,678 to Laughlin et al., issued December 30" 1975 at column 19, line 38 through column 22, line 48, for examples of zwitterioniG surfactants.

When included therein, the laundry detergent andlor fabric care compositions of the present invention typically comprise from 0.2;% to about 15%, preferably from about 1% to about 10% by weight of such zwiiterionic surfactants.
Semi-polar nonionic surfactants are a special category of nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; water-soluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety of from about 10 to about 18 carbon .atoms and a moiety selected from the group consisting of alkyl and hydroxyaikyl moieties of from about 1 to about 3 carbon atoms.
Semi-polar nonionic detergent surfactants include the amine oxide surfactants having the formula T
R3(OR4)xN(R5)2 wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures therof containing from about 8 to about 22 carbon ai:oms; R4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon at~ms or mixtures thereof; x is from 0 to about 3; and each 1~5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups. The R5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure.
These amine oxide surfactants in particular include C10-C1 g alkyl dimethyl amine oxides and Cg-C12 alkoxy ethyl dihydroxy etl'~yl amine oxides.
When included therein, the cleaning compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1 % to about 10% by weight of such semi-polar nonionic surfactaints.

WO 99157259 PCTlUS99109409 The laundry detergent andlor fabric care composition of the present invention may further comprise a cosurfactant selected from the group of primary or tertiary amines.
Suitable primary amines for use herein include amiines according to the formula R1NH2 wherein R1 is a Cg-Cl2t preferably Cg-C1~~ alkyl chain or R4X(CH2~n, X
is -O-,-C(O)NH- or -NH-, Rq, is a Cg-C12 alkyl chain n is between 1 to 5, preferably 3. R1 alkyl chains may be straight or branched and may be interrupted with up to 12, preferably less than 5 ethylene oxide moieties.
Preferred amines according to the formula herein above are n-alkyl amines.
Suitable amines for use herein may be selected from 1-hexylamine, 1-octylamine, 1-decylamine and laurylamine. Other preferred primary amines include C8-C10 oxypropylamine, octyioxypropylamine, 2-ethylhexyloxypropyl-amine, lauryl amido propylamine and amido propylaimine.
Suitable tertiary amines for use herein include tertiary amines having the formula R1 R2RgN wherein R1 and R2 are C1-Cg alkylchains or Rs -~ CHZ-CH-O~H
R~ is either a Cg-C12, preferably Cg-C1 p alkyl chain, or R3 is R4X(CH2)n, whereby X is -O-, -C(O)NH- or -NH-,R4 is a C4-C129 n is between 1 to 5, preferably 2-3. R~ is H or C1-C2 alkyl and x is between 1 to 6 .
R8 and R4 may be linear or branched ; Rg alkyl chains may be interrupted with up to 12, preferably less than 5, ethylene oxide moieties.
Preferred tertiary amines are R1 R2R3N where R1 is a C6-C12 alkyl chain, R2 and R3 are C1-C3 alkyl or Rs -( CHZ-CH-O~H
where R5 is H or CH3 and x = 1-2.
Also preferred are the amidoamines of the formula:

WO 99/57259 PCT/US99/09~109 O
R1-C-NH-( CHZ n N-( R2 2 wherein R1 is Cg-C1~ alkyl; n is 2-4, preferably n is 3; Rz and R3 is C1-C4 Most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine,CB-10oxypropylamine, N coco 1-3diaminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl bis(hydroxyethyl)amine, coco bis(hydroxyehtyl}amine, lauryl amine 2 moles propoxylated, octyl amine 2 moles propoxylated, lauryl arnidopropyl-dimethylamine, C8-10 amidopropyldimethylamine and C10 amidopropyl-dimethylamine.
The most preferred amines for use in the compositions herein are 1-hexyiamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Especially desirable are n-dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7 times ethoxylated, lauryi amido propylamine and cocoamido propylamine.
Conventional detergent enzymes The laundry detergent and/or fabric care compositions can in addition to the modified cellulase, further comprise one or mare enzymes which provide cleaning performance andlor fabric care benefits.
Said other enzymes include enzymes selected fronn cellulases without naturally occuring CSDs or with a having a relative binding constant (Kr-a) for binding to amorphous cellulose lower than 2.41/gcellulose, hemicellulases, peroxidases, proteases, gluco-amylases, amylases, xylanase:>, lipases, phospholipases, esterases, cutinases, pectinases, keratanase~s, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, f3-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase or mixtures thereof.

A preferred combination is a laundry detergent andlor fabric care composition having cocktail of conventional applicable enzymes like protease, amylase, lipase, cutinase and/or cellulase in conjunction with one or more plant cell wall degrading enzymes.
Suitable proteases are the subtilisins which are obtained from particular strains of B. subtilis and B. licheniformis (subtilisin BPIN and BPN'). One suitable protease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, developed and sold as ESPERASE~ by Novo Industries AIS of Denmark, hereinafter "Novo". The preparation of this enzyme and analogous enzymes is described in GB 1,243"784 to Novo. Other suitable proteases include ALCALASE~, DURAZYM~ and SAVINASE~ from Novo and MAXATASE~~ MAXACAL~, PROPERASE~ and MAXAPEM~ (protein engineered Maxacal) from Gist-Brocades. Proteolytic enzymes also encompass modified bacterial serine proteases, such as those described in European Patent Application Serial Number 87 303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98), and which is called herein "Protease B", and in European Patent Application 199,404, Venegas, published October 29, 1986, which refers to a modified bacterial serine protealytic enzyme which is called "Protease A"
herein. Suitable is what is called herein "Protease; C", which is a variant of an alkaline serine protease from Bacillus in which lysine replaced arginine at position 27, tyrosine replaced valine at position 104, serine replaced asparagine at position 123, and alanine replaced threonine ai: position 274. Protease C
is described in EP 90915958:4, corresponding to WO 91106637, Published May 16, 1991. Genetically modified variants, particul<arly of Protease C, are also included herein.
A preferred protease referred to as "Protease D" is a carbonyl hydrolase variant having an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for a plurality of amino acid residues at a position in said carbonyl hydrolase equivalent to position +7fi, preferably also in combination with one or more amino acid residue positions equivalent to those selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +'i28, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274 according to the numbering of Bacillus amyloliquefK~ciens subtilisin, as described in W095110591 and in the patent application of C. Ghosh, et al, "Bleaching WO 99!57259 PCT/US99/09409 Compositians Comprising Protease Enzymes'° having US Serial No.
08/322,677, filed October 13, 1994. Also suitable is a carbonyl hydrolase variant of the protease described in W095i10591, having an amiino acid sequence derived by replacement of a plurality of amino acid residues replaced in the precursor enzyme corresponding to position +210 in combination with one or more of the following residues : +33, +629 +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +16.6, +167, +170, +209, +215, +217, +218, and +222, where the numbered position corresponds to naturally-occurring subtilisin from Bacillus arriyloliquefaciens or to equivalent amino acid residues in other carbonyl hydrolases or subtiiisins, such as Bacillus lentos subtilisin (ca-pending patent application US Serial No. 60/048,550, filed June 04, 1997).
Also preferred proteases are multiply-substituted! protease variants. These protease variants comprise a substitution of an amino acid residue with another naturally occurring amino acid residue at an amino acid residue position corresponding to position 103 of Bacillus arrryloliquefaciens subtilisin in combination with a substitution of an amino acid re;>idue positions corresponding to positions 1, 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 1 !~, 20, 21, 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, T7, 78, 79, 86, 87, 89, 97, 98, 99, 101, 102, 104, 106, 107, 109, 111, 114, 116, 117, 119, 121, 123, 126, 128, 130, 131, 133, 134, 137, 140, 141, 142, 146, 147, '158, 159, 160, 166, 167, 170, 173, 174, 177, 181, 182, 183, 184, 185, 188, 192, '194, 198, 203, 204, 205, 206, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, :?22, 224, 227, 228, 230, 232, 236, 237, 238, 240, 242, 243, 244, 245, 246, 247, :?48, 249, 251, 252, 253, 254, , 255, 256, 257, 258, 259, 260, 261, 262, 263, 265, .268, 269, 270, 271, 272, and 275 of Bacillus amyloliquefaciens subtilisin; wherein when said protease variant includes a substitution of amino acid residues at positions corresponding to positions 103 and 76, there is also a substitution of an amino acid residue at one or more amino acid residue positions othE:r than amino acid residue positions corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128, 166, 204, 206, 210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus amyloliquefaciens subtiiisin and/or multiply-substituted protease variants comprising a substitution of an amino acid re:;idue with another naturally occurring amino acid residue at one or more amino acid residue positions corresponding to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaciens subtilisin as described in PCT application Nos.

PCTIUS98122588, PCT/US98/22482 and PCTIUS!38/22486 all filed on October 23, 1998 from The Procter & Gamble Company.
Also suitable for the present invention are proteases described in patent applications EP 251 446 and WO 91 /06637, protease BLAP~ described in W091/02792 and their variants described in WO 9;i/23221.
See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO
93118140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhiibitor are described in WO
92103529 A to Novo. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 95/07791 to Procter ~
Gamble. A recombinant trypsin-like protease for detergents suitable herein is described in WO 94/25583 to Novo. Other suitable proteases are described in EP 516 200 by Unilever.
The proteolytic enzymes are incorporated in the eletergent compositions of the present invention a level of from 0.0001 % to 2°/«, preferably from 0:001 % to 0.2%, more preferably from 0.005% to 0.1 % pure enzyme by weight of the composition.
The cellulases without naturally occurring CBDs or with a having a relative binding constant (Kr-a) for binding to amorphous cellulose lower than 2.411gcellulose, include both bacterial or fungal ce~llulases. Preferably, they will have a pH optimum of between 5 and 72 and an activity above 50 CEVU
(Cellulose Viscosity Unit). Suitable cellulases acre disclosed in U.S. Patent 4,435,307, Barbesgoard et al, J61078384 and VV096/02653 which discloses fungal cellulase produced respectively from Hurrricofa insolens, Trichoderma, Thielavia and Sporotrichum. EP 739 982 describes cellulases isolated from novel Bacillus species. Suitable cellulases arE: also disclosed in GB-A-2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and W095I26398.
Examples of such cellulases are cellulases produced by a strain of Humicola insolens (Humicofa grisea var. thermoidea), particularly the Humicola strain DSM
1800. Other suitable celluiases are cellulases originated from Humicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing 415 amino acids; and a -43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. WO 91!17243. Also suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum described in W094l21801, Genencor, published September 29, 1994. Especially suitable cellulases are the cellulases having color care benefits. Examples of such cellulases; are cellulases described in European patent application No. 91202879.2, filed November fi, 1991 (Novo).
Carezyme and Celluzyme (Novo Nordisk A/S) arcs especially useful. See also W091117244 and W091/21801. Other suitable cellulases for fabric care and/or cleaning properties are described in W096~I34092, W096l17994 and W095/24471.
Said cellulases are normally incorporated in the df;tergent composition at levels from 0.0001 % to 2% of pure enzyme by weight of the detergent composition.
Peroxidase enzymes are used in combination with oxygen sources, e.g.
percarbonate, perborate, persulfate, hydrogen peroxide, etc and with a phenolic substrate as bleach enhancing molecule. They are used for "solution bleaching", i.e. to prevent transfer of dyes or pigments removed from substrates during wash operations to other substrates in the wash solution. Peroxidase enzymes are known in the art, and include, for example, horseradish peroxidase, ligninase and haioperoxidase such as chloro- and bromo-peroxidase. Peroxidase-containing detergent compositions are disclosed, for example, in PCT
International Application WO 89/099813, W089!09813 and in European Patent application EP No. 91202882.f>, filed on November 6, 1991 and EP No.
96870013.8, filed February 20, 1996. Also suitable is the laccase enzyme.
Enhancers are generally comprised at a level of from 0.1 % to 5% by weight of total composition. Preferred enhancers are substituted phenthiazine and phenoxasine 10-Phenothiazinepropionicacid {PPT), 10-ethylphenothiazine-4-carboxyfic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-methylphenoxazine (described in WO 94112621) and substituted syringates (C3-C5 substituted alkyl syringates) and phenols. Sodium percarbonate or perborate are preferred sources of hydrogen peroxide.
Said peroxidases are normally incorporated in the detergent composition at levels from 0.0001 % to 2°/~ of pure enzyme by weight of the detergent composition.
Other enzymes that can be included in the detergent compositions of the present invention include lipases. Suitable lipase enzymes for detergent usage WO 99/57259 ° PCT/(JS99109409 include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034.
Suitable lipases include those which show a positive immunological cross-reaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P
"Amano," hereinafter referred to as "Amano-P". Other suitable commercial lipases include Amano-CES, lipases ex Ch!romobacter viscosum, e.g.
Chromobacfer viscosum var. lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases i'rom U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. Especially suitable lipases are lipases such as M1 LipaseR and LipomaxR (Gist-Brocades) and LipolaseR and lLipolase UItraR(Novo) which have found to be very effective when used in combination with the compositions of the present invention. Also suitables are the lipollytic enzymes described in EP
258 068, WO 92105249 and WO 95122615 by Novo Nordisk and in WO
94/03578, WO 95135381 and WO 96/00292 by Unilever.
Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special kind of lipase, namely lipases which do not require interfacial activation.
Addition of cutinases to detergent compositions have been described in e.g. WO-A-88109367 (Genencor}; WO 90109446 {Plant Genetic System) 'and WO 94/14963 and WO 94/14964 (Unilever).
The lipases and/or cutinases are normally incorporated in the detergent composition at levels from 0.0001 % to 2% of pure enzyme by weight of the detergent composition.
Amylases (oc and/or (3) can be included for removal of carbohydrate-based stains. W094/02597, Novo Nordisk A/S published February 03, 1994, describes cleaning compositions which incorporate mutant amylases. See also W095/10603, Novo Nordisk AIS, published April 20, 1995. Other amylases known for use in cleaning compositions include both a- and [i-amylases. a,-Amylases are known in the art and include tho;>e disclosed in US Pat. no.
5,003,257; EP 252,666; W0/91/00353; FR 2,676,456; EP 285,123; EP 525,610;
EP 368,341; and British Patent specification n~o. 1,296,839 (Novo}. Other suitable amylases are stability-enhanced amylasea described in W094I18314, published August 18, 1994 and W096/05295, Genencor, published February WO 99!57259 PCT/US99/09409 . 22, 1996 and amylase variants having additional modification in the immediate parent available from Novo Nordisk A/S, disclosed in WO 95/10f03, published April 95. Also suitable are amylases described in EP 277 216, W095/26397 and W096/23873 (all by Novo Nordisk).
Examples of commercial a-amylases products are Purafect Ox Am~ from Genencor and Termamyl~, Ban~ ,Fungamyl~ and Durarnyl~, all available from Novo. Nordisk AIS Denmark. W095/26397 describfa other suitable amylases : a -amylases characterised by having a specific activity at least 25% higher than the specific activity of Termamyl~ at a temperature range of 25°C to 55°C and at a pH value in the range of 8 to 10, measured b~y the Phadebas~ a-amylase activity assay. Suitable are variants of the above enzymes, described in W096/23873 (Novo Nordisk). Other amylolytic enzymes with improved properties with respect to the activity level and the combination of thermostability and a higher activity level are described in W095/35382.
The amylolytic enzymes are incorporated in the detergent compositions of the present invention a level of from 0.0001 % to 2%, preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the composition.
The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, p;sychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic; halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Also included by definition, are mutants of native enzymes. Mutants can be obtained e.g. by protein and/or genetic engineering, chemical and/or physical modifications of native enzymes.
Common practice as well is the expression of the enzyme via host organisms in which the genetic material responsible for the production of the enzyme has been cloned.
Said enzymes are normally incorporated in the detergent composition at levels from 0.0001 % to 2% of pure enzyme by weight oiF the detergent composition.
The enzymes can be added as separate single ingredients (prills, granulates, stabilized liquids, etc. containing one enzyme ) or as mixtures of two or more enzymes ( e.g. cogranulates ).

Other suitable detergent ingredients that can be added are enzyme oxidation scavengers which are described in Copending European Patent application 92870018.6 filed on January 31, 1992. Examples of such enzyme oxidation scavengers are ethoxylated tetraethylene polyamines.
A range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A
to Genencor International, WO 8908694 A to Novo, and U.S. 3,553,139, January 5, 1971 to McCarty et al. Enzymes are further disclosed in U.S.
4,101,457, Place et al; July 18, 1978, and in U.S. 4,507,219, Hughes, March 26, 1985. Enzyme materials useful for liquid detergent formulations, and their incorporation into such formulations, are disclosed in U.S. 4,261,868, Hora et al, April 14, 1981. Enzymes for use in detergents can be stabilised by various techniques. Enzyme stabilisation techniques are disclosed and exemplified in U.S. 3,600,319, August 17, 1971, Gedge et al, E:P 199,405 and EP 200,586, October 29, 1986, Venegas. Enzyme stabilisation systems are also described, for example, in U.S. 3,519,570. A useful Bacillus>, sp. AC13 giving proteases, xylanases and cellulases, is described in WO 9401:532 A to Novo.
Colour care and fabric care benefits Technologies which provide a type of colour care benefit can also be included.
Examples of these technologies are metallo catalysts for colour maintenance.
Such metallo catalysts are described in copending European Patent Application No. 92870181.2. Dye fixing agents, polyolefin dispersion for anti-wrinkles and improved water absorbancy, perfume and amino-functional polymer for color care treatment and perfume substantivity are further examples of colour care I
fabric care technologies and are described in the co-pending Patent Application No. 96870140.9, filed November 07, 1996.
Fabric softening agents can also be incorporated unto laundry detergent and/or fabric care compositions in accordance with the present invention. These agents may be inorganic or organic in type. Inorganic softening agents are exemplified by the smectite clays disclosed in GB-A-1 400 898 and in USP 5,019,292.
Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP-BO 011 340 and their combination with mono C12-C14 quaternary ammonium salts are disclosed in EP-B-0 026 527 and EP-B-0 026 528 and di-long-chain amides as disclosed in EP-B-0 242 919.
Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0 313 146.
Preferred fabric softening agent for the purpose of the present invention is a smectite clay. It has been surprisingly found that the laundry detergent and/or fabric care compositions of the present invention further comprising a smectite clay, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide enhanced static control, fabric softness, colour appearance and fabric anti-wear properties and benefits while preventing tensile strength loss.
Levels of smectite clay are normally in the range from 2% to 20%, more preferably from 5% to 15% by weight, with the material being added as a dry , mixed component to the remainder of the formulation. Organic fabric softening agents such as the water-insoluble tertiary amiines or dilong chain amide materials are incorporated at levels of from 0.5% to 5% by weight, normally from 1 % to 3% by weight whilst the high molecular weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1 % to 2%, normally from 0.15% to 1.5% by weight. These materials are normally added to the spray dried portion of the composition, although in some instances it may be more convenient to add them as a dry mixed particulate, or spray them as molten liquid on to other solid components of the composition.
Bleaching agent Other detergent ingredients that can be included in the laundry detergent and/or fabric care compositions of the present invention include bleaching agents.
Bleaching agents include hydrogen peroxide, PB1, I'B4 and percarbonate with a particle size of 400-800 microns. These bleaching agent components can include one or more oxygen bleaching agents and, depending upon the bleaching agent chosen, one or more bleach activsitors. When present oxygen bleaching compounds will typically be present at levels of from about 1 % to about 25%.

WO 99l57Z59 PCT/US99/09409 The bleaching agent component for use herein c:an be any of the bleaching agents useful for cleaning compositions including oxygen bleaches as well as others known in the art. The bleaching agent suitable for the present invention can be an activated or non-activated bleaching agent.
One category of oxygen bleaching agent that can be used encompasses percarboxylic acid bleaching agents and salts therE:of. Suitable examples of this class of agents include magnesiuim monoperox~yphthalate hexahydrate, the magnesium salt of meta-chioro perbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaching agents are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740,446, European Patent Application 0,133,354 and U.;i. Patent 4,412,934. Highly preferred bleaching agents also include 6-nonylamino-6-oxoperoxycaproic acid as described in U.S. Patent 4,634,551.
Another category of bleaching agents that can be used encompasses the halogen bleaching agents. Examples of hypohalite bleaching agents, for example; include trichloro isocyanuric acid and the sodium and potassium dichloroisocyanurates and N-chloro and N-bromo <~Ikane sulphonamides. Such materials are normally added at 0.5-10% by weight of the finished product, preferably 1-5% by weight.
The hydrogen peroxide releasing agents can be usE:d in combination with bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene-sulfonate (HOBS, described in I.IS 4,412,934), 3,5,-trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591) or pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6-aminocaproic acid (NAOA-OBS, described in WO94/28106), which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect. Also suitable activators are acylated citrate esters such as disclosed in Copending European Patent Application No. 91870207.7.
Useful bleaching agents, including peroxyacids and bleaching systems comprising bleach activators and peroxygen bfeac;hing compounds for use in detergent compositions according to the inventioin are described in our co-pending, applications USSN 08/136,626, PCl-IUS95/07823, W095/27772, WO95/27773, W095127774 and W095I27775.
The hydrogen peroxide may also be present by adding an enzymatic system (i.e., an enzyme and a substrate therefore) which is capable of generating hydrogen peroxide at the beginning or during the washing andlor rinsing process. Such enzymatic systems are disclosed in EP Patent Application 91202655.6 fled October 9, 1991.
Metal-containing catalysts for use in bleach compositions, include cobalt-containing catalysts such as Pentaamine acetate cobalt(III) salts and manganese-containing catalysts such as those described in EPA 549 271; EPA
549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US
5,114,611. Bleaching composition comprising a pecoxy compound, a manganese-containing bleach catalyst and a chelating agent is described in the patent application No 94870206.3.
Bleaching agents other than oxygen bleaching agents are also known in the art and can be utilized herein. One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as the sulfonated zinc and/or aluminum phthalocyanines. These materials can be deposited upon the substrate during the washing process. Upon ilrradiation with light, in the presence of oxygen, such as by hanging clothes out to dry in the daylight, the sulfonated zinc phthalocyanine is activated and, consequently, the substrate is bleached. Preferred zinc phthalocyanine and .a photoactivated bleaching process are described in U.S. Patent 4,033,7'18. Typically, detergent compositions wile contain about 0.025% to about 1.25%, by weight, of suifonated zinc phthalocyanine.
Builder system The compositions according to the present invention may further comprise a builder system. It has been surprisingly found that said laundry detergent andlor fabric care compositions further comprising a builcler, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide enhanced static control, fabric softness, colour appearance arid fabric anti-wear properties and benefits and improved fabric cleaning while preventing tensile strength loss. Preferred builders are zeolite A
and sodium tripolyphosphate.
Any conventional builder system is suitable for use herein including aluminosiiicate materials, silicates, polycarboxylaires, alkyl- or alkenyl-succinic acid and fatty acids, materials such as ethylenediamine tetraacetate, diethylene triamine pentamethyleneacetate, metal ion sequ~estrants such as aminopoly-phosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid. Phosphate builders can also be used herein.
Suitable builders can be an inorganic ion exchange material, commonly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
Another suitable inorganic builder material is layered silicate, e.g. SKS-6 (Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na2Si205).
Suitable poiycarboxylates containing one carboxy group include lactic acid, glycolic acid and ether derivatives thereof as discllosed in Belgian Patent Nos.
831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy groups include the water-soluble salts of succinic acid, rnalonic acid, (ethylenedioxy) diacetic acid, malefic acid, diglycollic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates described in German Offenlegenschrift 2,446,686, and 2,446,687 and U.S. Patent No. 3,935,257 and the suifinyl carboxylates described in Belgian Patent No. 840,623. Polycarboxylates containing three carboxy groups include, in particulbr, water-soluble citrates, aconitrates and citraconates as well as succinaite derivatives such as the carboxymethyloxysuccinates described in British Patent No. 1,379,241, lactoxysuccinates described in Netherlands Application 7205873, and the oxypolycarboxylate materials such as 2-oxa-1,1,3-propane tricarboxylates described in British Patent No. 1,387,447.
Polycarboxylates containing four carboxy groups include oxydisuccinates disclosed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates, 1,1,3,3-propane tetracarboxylates and 1,1,2,3-propane tetracarboxylates.

WO 99!57259 PCT/US99/09409 Polycarboxylates containing sulfo substituents include the sulfosuccinate derivatives disclosed in British Patent Nos. 1,398,~121 and 1,398,422 and in U.S.
Patent No. 3,936,448, and the sulfonated pyrolysed citrates described in British Patent No. 1,082,179, while polycarboxylates containing phosphone substituents are disclosed in British Patent No. 1,439,000.
Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis,cis,cis-tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydro-furan - cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-~furan -cis -dicarboxylates, 2,2,5,5-tetrahydrofuran - tetracarboxyiates, 1,2,3,4,5,6-hexane -hexa-carboxylates and and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic poly-carboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent No.
1,425,343.
Of the above, the preferred polycarboxylates are hydroxycarboxylates containing up to three carboxy groups per molecule, more particularly citrates.
Preferred builder systems for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS-6), and a water-soluble carboxylate chelating agent such as citric acid.
Preferred builder systems include a mixture of a wrater-insoluble aluminosilicate builder such as zeolite A, and a watersolubte carboxylate chelating agent such as citric acid. Preferred builder systems for use in liquid detergent compositions of the present invention are soaps and polycarboxylates.
Other builder materials that can form part of the builder system for use in granular compositions include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as the organic phosphonates, amino polyalkylene phosphonates and amino polycarboxylates.
Other suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.

Polymers of this type are disclosed in GB-A-1,59Ei,756. Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with malefic anhydride, such copolymers having a molecular weight of from 20,000 to 70,000, especially about 40,000.
Detergency builder salts are normally included in amounts of from 5% to 80% by weight of the composition preferably from 10% to 70% and most usually from 30% to fi0% by weight.
Chelating Agents The laundry detergent andlor fabric care compositions herein may also optionally contain one or more iron and/or manganese chelating agents. Such chelating agents can be selected from the group consisting of amino carboxylates, amino phosphonates, polyfunctionally-substituted aromatic chelating agents and mixtures therein, all as hereinafter defined. Without intending to be bound by theory, it is believed that the benefit of these materials is due in part to their exceptional ability to remove iron and manganese ions from washing solutions by formation of soluble chelates.
Amino carboxylates useful as optional chelating agents include ethylenediaminetetracetates, N-hydroxyethyfethylf:nediaminetriacetates, nitrilo-triacetates, ethylenediamine tetraproprionaites, triethylenetetraamine-hexacetates, diethylenetriaminepentaacetates, and ethanoldiglycines, alkali metal, ammonium, and substituted ammonium salts therein and mixtures therein.
Amino phosphonates are also suitable for use as chelating agents in the compositions of the invention when at Lease low levels of total phosphorus are permitted in detergent compositions, and include ethylenediaminetetrakis (methylenephosphonates) as DEQUEST. Preferrec#, these amino phosphonates do not contain alkyl or alkenyl groups with more than about 6 carbon atoms:
PoPyfunctionally-substituted aromatic chelating agents are also useful in the compositions herein. See U.S. Patent 3,812,044'., issued May 21, 1974, to Connor et a!. Preferred compounds of this type in acid form are dihydroxydisulfobenzenes such as 1,2-dihydroxy-3,;5-disulfobenzene.

A preferred biodegradable chelator for use herein is ethylenediamine disuccinate ("EDDS"), especially the [S,S] isomer as described in U.S. Patent 4,704,233, November 3, 1987, to Hartman and Perkins.
The compositions herein may also contain water-soluble methyl glycine diacetic acid (MGDA) salts (or acid form) as a chelant or co-builder useful with, for example, insoluble builders such as zeolites, IayerE~d silicates and the like.
If utilized, these chelating agents will generally comprise from about 0.1 %
to about 15% by weight of the detergent compositions herein. More preferably, if utilized, the chelating agents will comprise from about 0.1 % to about 3.0% by weight of such compositions.
Suds suppressor Another optional ingredient is a suds suppressor, exemplified by silicones, and silica-silicone mixtures. Silicones can be generally represented by alkylated polysiloxane materials while silica is normally wised in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. These materials can be incorporated as p<srticulates in which the suds suppressor is advantageously releasably incorporated in a water-soluble or water-dispersible, substantially non-surface-active detergent impermeable carrier. Alternatively the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to ~one or more of the other components.
A preferred silicone suds controlling agent is disclosed in Bartoilota et al.
U.S.
Patent 3 933 672. Other particularly useful such suppressors are the self emulsifying silicone suds suppressors, described in German Patent Application DTOS 2 646 12fi published April 28, 1977. An example of such a compound is DC-544, commercially available from Dow Corning, which is a siloxane-glycol copolymer. Especially preferred suds controlling agent are the suds suppressor system comprising a mixture of silicone oils and 2-alkyl-alcanols. Suitable 2-alkyl-alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R.

WO 99/57259 PCTI~JS99/09409 Such suds suppressor system are described in Copending European Patens application N 92870174.7 filed 10 November, 199:?.
Especially preferred silicone suds controlling agents are described in Copending European Patent application N°92201649.8. Said compositions can comprise a silicone/silica mixture in combination with fumed nonporous silica such as AerosilR.
The suds suppressors described above are normally employed at levels of from 0.001 % to 2% by weight of the composition, preferably from 0.01 % to 1 % by weight.
Others Other components such as soil-suspending ageni;s, soil-release agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, and/or.
encapsulated or non-encapsulated perfumes may be employed.
Especially suitable encapsulating materials are vuater soluble capsules which consist of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1,464,fi16.
Other suitable water soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid-esters of substituted dicarboxylic acids such as described in US 3,455,838. These acid-ester dextrins are,preferably, prepared Pram such starches as waxy maize, waxy sorghum, sago, tapioca and potato.
Suitable examples of said encapsulating materials include N-Lok manufactured by National Starch. The N-Lok encapsulating maiterial consists of a modified maize starch and glucose. The starch is modified by adding monafunctional substituted groups such as octenyl succinic acid anhydride.
Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their salts. Polymers of this type include the polyacryiates and malefic anhydride-acrylic acid copolymers previously mentioned as builders, as well as copolymers of malefic anhydride with ethylene, methylvinyl ether or methacrylic acid, the WO 99/57259 PCT/t1S99/09409 malefic anhydride constituting at least 20 mole percent of the copolymer.
These materials are normally used at levels of from 0.5% to 10% by weight, more preferably from 0.75% to 8%, most preferably from 1 % to 6% by weight of the composition.
Preferred optical brighteners are anionic in character, examples of which are disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-ylamino)stilbene-2:2' disulphonate, disodium 4, - 4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino-stilbene-2:2° - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-triazin-6-ylamino)stilbene-2:2' - disulphonate, monosodium 4',4" -bis-(2,4-dianilino-s-tri-azin-6 ylamino)stilbene-2-sulphonate, disodium 4,~4' -bis-(2-anilino-4-(N-methyl-N-2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2,2' - disulphonate, di-sodium 4,4' -bis-(4-phenyl-2,1,3-triazol-2-yl)-stilberne-2,2' disulphonate, di-so-dium 4,4'bis(2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazin-6- ylami-no)stilbene-2,2'disulphonate, sodium 2(stilbyl-4"-(naphtho-1',2':4,5)-1,2,3 -triazole-2"-sulphonate and 4,4'-bis(2-sulphostyryll)biphenyl. Highly preferred brighteners are the specific brighteners of copending European Patent application No. 95201943.8.
Other useful polymeric materials are the polyethylene glycols, particularly those of molecular weight 1000-10000, more particularly 2000 to 8000 and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5% by weight. These polymers and the previously mentioned homo- or co-polymeric polycarboxyl;ate salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proteinaceous and oxidizat~le soils in the presence of transition metal impurities.
Soil release agents useful in compositions of the present invention are conventionally copolymers or terpolymers of tere~phthalic acid with ethylene glycol andlor propylene glycol units in various arrangements. Examples of such polymers are disclosed in the commonly assigned l1S Patent Nos. 4116885 and 4711730 and European Published Patent Application No. 0 272 033. A
particular preferred polymer in accordance with EP-I~-0 272 033 has the formula WO 99/57259 PCT/fJS99109409 (CH3(PEG)43)0.75(POH)0,25~T-PO)2.g(T-PEG)0.4)T(PO
H)0.25((PEG)43CH3)0.75 where PEG is -(OC2H4)O-,PO is (OC3Hg0) and T is (pcOCgH4CO).
Also very useful are modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthaiate, ethylene glycol and 1-2 propane diol, the end groups consisting primarily of sulphobenzo~ate and secondarily of mono esters of ethylene glycol and/or propane-diol. The target is to obtain a polymer capped at both end by sulphobenzoate groups, "primarily", in the present context most of said copolymers herein will be end-capped by sulphobenzoate groups. However, some copolymers will be less than fully capped, and therefore their end groups may consist of monoester of ethylene glycol andlor propane 1-2 diol, thereof consist "secondarily" of such species.
The selected polyesters herein contain about 4.fi% by weight of dimethyl terephthalic acid, about 16% by weight of propane -1.2 diol, about 10% by weight ethylene glycol about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3.000. The polyesters and their method of preparation are described in detail in EPA 311 342.
It is well known in the art that free chlorine in tap vvater rapidly deactivates the enzymes comprised in detergent compositions. Therefore, using chlorine scavenger such as perborate, ammonium sulfate, sodium sulphite or polyethyleneimine at a level above 0.1 % by weighs; of total composition, in the formulas will provide improved through the wash stability of the detergent enzymes. Compositions comprising chlorine scavE:nger are described in the European patent application 92870018.6 filed January 31, 1992.
Alkoxylated polycarboxylates such as those prepared from polyacrylates are useful herein to provide additional grease removal p~erFormance. Such materials are described in WO 91/08281 and PCT 90/01815 .at p. 4 et sep., incorporated herein by reference. Chemically, these materials comprise polyacrylates having one ethoxy side-chain per every 7-8 acrylate units. The side-chains are of the formula -(CH2CH20)m(CH2)nCH3 wherein m is 2-3 and n is 6-12. The side-WO 99/57259 PCT/~IS99/09409 chains are ester-linked to the poiyacrylate "backbone" to provide a "comb"
polymer type structure. The molecular weight can vary, but is typically in the range of about 2000 to about 50,000. Such alkoxylated polycarboxylates can comprise from about 0.05% to about 10%, by weight, of the compositions herein.
Dispersanfs The laundry detergent and/or fabric care composition of the present invention can also contain dispersants : Suitable water-soluble organic salts are the homo-or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each .other by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with malefic anhydride, such copolymers having a molecular weight of from.1,000 to 100,000.
Especially, copolymer of acrylate and methyiacrylatE: such as the 480N having a molecular weight of 4000, at a level from 0.5-20% by weight of composition can be added in the laundry detergent and/or fabric care compositions of the present invention.
The compositions of the invention may contain a lime soap peptiser compound, which has preferably a lime soap dispersing power (LSDP), as defined hereinafter of no more than 8, preferably no more than 7, most preferably no more than 6. The lime soap peptiser compound is preferably present at a level from 0% to 20% by weight.
A numerical measure of the effectiveness of a lime soap peptiser is given by the lime soap dispersant power (LSDP) which is determined using the lime soap dispersant test as described in an article by H.C. Borghetty and C.A. Bergman, J. Am. Oil. Chem. Soc., volume 27, pages 88-90, (1950). This lime soap dispersion test method is widely used by practitioners in this art field being referred to, for example, in the following review articles; W.N. Linfield, Surtactant science Series, Volume 7, page 3; W.N. Linfield, Tenside surf. det., volume 27, pages 159-163, (1990); and M.K. Nagarajan, VU.F. Master, Cosmetics and Toiletries, volume 104, pages 71-73, (1989). The L.SDP is the % weight ratio of dispersing agent to sodium oleate required to disperse the lime soap deposits formed by 0.025g of, sodium oleate in 30m1 of water of 333ppm CaCo3 (Ca:Mg=3:2) equivalent hardness.
Surtactants having good lime soap peptiser capability will include certain amine oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated alcohols.
Exemplary surfactants having a LSDP of no more lrhan 8 for use in accord with the present invention include C1g-C18 dimethyl <~mine oxide, C12-C1g alkyl ethoxysulfates with an average degree of ethoxyla~tion of from 1-5, particularly C12-C15 alkyl ethoxysulfate surfactant with a degree of ethoxyfation of amount 3 (LSDP=4), and the C14-C15 ethoxylated alcohol:, with an average degree of ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol A012 and Lutensol A030 respectively, by BASF GmIbH.
Polymeric lime soap peptisers suitable for use hereon are described in the article by M.K. Nagat-ajan, W.F. Master, to be found in Cosmetics and Toiletries, volume 104, pages 71-73, (1989).
Hydrophobic bleaches such as 4-[N-octanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-nonanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-decanoyl-6-aminohexanoyl]benzene sulfonate and mixtures i;hereof; and nonanoyloxy benzene sulfonate together with hydrophilic / hydrophobic bleach formulations can also be used as lime soap peptisers compounds.
Dye transfer inhibition The laundry detergent and/or fabric care compositions of the present invention can preferably include compounds for inhibiting dye transfer from one fabric to another of solubilized and suspended dyes encountered during fabric laundering operations involving colored fabrics. It has been surprisingly found that the laundry detergent andlor fabric care compositions of the present invention further comprising a dye transfer inhibition polymer, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage properties WO 99!57259 PCT/US99/09409 to fabrics, as well as provide enhanced static c:ontrol, fabric softness, colour appearance and fabric anti-wear properties and benefits and improved fabric cleaning while preventing tensile strength loss.
Polymeric dye transfer inhibiting agents The laundry detergent andlor fabric care compositions according to the present invention may also comprise from 0.001 % to 10 %., preferably from 0.01 % to 2%, more preferably from 0.05% to 1 % by weight of polymeric dye transfer inhibiting agents. Said polymeric dye transfer inhibiting agents are normally incorporated into cleaning compositions in order to inhibit the transfer of dyes from colored fabrics onto fabrics washed therewith. These polymers have the ability to complex or adsorb the fugitive dyes washed out o1F dyed fabrics before the dyes have the opportunity to become attached to other airticles in the wash.
Especially suitable polymeric dye transfer inhibiting agents are polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and poiyvinylimidazoles or mixtures thereof.
Addition of such polymers also enhances the pferformance of the enzymes according the invention.
a) Polyamine N-oxide polymers The polyamine N-oxide polymers suitable for use contain units having the following structure formula P
(I) Ax I
R
wherein P is a polymerisable unit, whereto the R-N-O group can be attached to or wherein the R-N-O group forms part of the polymerisable unit or a combination of both.

II II II
A is NC, CO, C, -o-,-s-, -N- ; x is o or 1;
R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclic or alicyclic groups or any combination thereof whereto the nitrogen of the N-O group can be attached or whE~rein the nitrogen of the N-O
group is part of these groups.
The N-O group can be represented by the following general structures O O
I I
(R1)x -N- (R2)y =N- (R1)x I
(R3)z wherein R1, R2, and R3 are aliphatic groups, aromatic, heterocyclic or alicyclic groups or combinations thereof, x or/and y orland z is 0 or 1 and wherein the nitrogen of the N-O group cain be attached or wherein the nitrogen of the N-O group forms part of these groups.
The N-O group can be part of the polymerisable unit (P) or can be attached to the polymeric backbone or a combination of both.
Suitable poiyamine N-oxides wherein the N-O group forms part of the polymerisable unit comprise polyamine N-oxides wherein R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups.
One class of said polyamine N-oxides comprises the group of polyamine N-oxides wherein the nitrogen of the N-O group forms part of the R-group.
Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, puinoline, acridine and derivatives thereof.
Another class of said polyamine N-oxides comprises the group of polyamine N-oxides wherein the nitrogen of the N-O group is attached to the R-group.
Other suitable polyamine N-oxides are the polyamiine oxides whereto the N-O
group is attached to the polymerisable unit.

WO 99!57259 PCT/US99/09409 Preferred class of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R is an aromatic, h~eterocyclic or alicyclic groups wherein the nitrogen of the N-0 functional group is part of said R group.
Examples of these classes are polyamine oxides wherein R is a heterocyclic compound such as pyrridine, pyrrole, imidazole and derivatives thereof.
Another preferred class of polyamine N-oxides are the polyamine oxides having the general formula (I) wherein R are aromatic, hcsterocyclic or alicyciic groups wherein the nitrogen of the N-0 functional group is attached to said R groups.
Examples of these classes are polyamine oxidea wherein R groups can be aromatic such as phenyl.
Any polymer backbone can be used as long as the amine oxide polymer formed is water-soluble and has dye transfer inhibiting properties. Examples of suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamide, polyimides, polyacrylates and mixtures thereof.
The amine N-oxide polymers of the present invention typically have a ratio of amine to the amine N-oxide of 10:1 to 1:1000000. I-lowever the amount of amine oxide groups present in the polyamine oxide polymer can be varied by appropriate copolymerization or by appropriate degree of N-oxidation.
Preferably, the ratio of amine to amine N-oxide is firom 2:3 to 1:1000000.
More preferably from 1:4 to 1:1000000, most preferably from 1:7 to 1:1000000. The polymers of the present invention actually encompass random or block copolymers where one monomer type is an amine N-oxide and the other monomer type is either an amine N-oxide or not. The amine oxide unit of the polyamine N-oxides has a PKa < 10, preferably PKa < 7, more preferred PKa <
6.
The polyamine oxides can be obtained in almost ainy degree of polymerisation.
The degree of polymerisation is not critical provided the material has the desired water-solubility and dye-suspending power.
Typically, the average molecular weight is within the range of 500 to 1000,000;
preferably from 1,000 to 50,000, more preferably from 2,000 to 30,000, most preferably from 3,000 to 20,000.
b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole The N-vinylimidazole N-vinylpyrrolidone polymers used in the present invention have an average molecular weight range from 5,000-1,000,000, preferably from 5,000-200,000.
Highly preferred polymers for use in detergent compositions according to the present invention comprise a polymer selected from N-vinylimidazole N-vinylpyrrolidone copolymers wherein said polymer has an average molecular weight range from 5,000 to 50,000 more preferably from 8,000 to 30,000, most preferably from 10,000 to 20,000.
The average molecular weight range was determined by light scattering as described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113;"Modern Methods of Polymer Characterization".
Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an average molecular weight range from 5,000 to 5C?,000; more preferably from 8,000 to 30,000; most preferably from 10,000 to 20,000.
The N-viny(imidazole N-vinylpyrrolidone copolymers characterized by having said average molecular weight range provide excellent dye transfer inhibiting properties while not adversely affecting the cleaning performance of detergent compositions formulated therewith.
The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has a molar ratio of N-viny(imidazole to N-vinylpyrrolidone from 1 to 0.2, more preferably from 0.8 to 0.3, most preferably from 0.6 t~o 0.4 .
c) Polyvinylpyrrolidone The detergent compositions of the present invention may also utilize polyvinylpyrrolidone ("PVP") having an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000. Suitable polyvinylpyrrolidone~s are commercially vailable from ISP Corporation, New York, NY and Montreal, Canada under the product names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average molecular weight of 40,000), PVP K-60 (average molecular weight of 160,000), and PVP K-90 (average molecular weight of 360,000). Other suitable polyvinylpyrrolidones which are commercially available from BASF Cooperation include Sokalan HP 165 and Soka(an HP 12; polyvinylpyrrolidones known to WO 99/57259 PCT/iJS99/09409 persons skilled in the detergent held {see for example EP A-262,897 and EP A-256,696).
d) Polyvinyloxazolidone The detergent compositions of the present invention may also utilize polyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Said polyvinyloxazolidones have an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000.
e) Polyvinylimidazole The detergent compositions of the present iinvention may also utilize polyvinylimidazole as polymeric dye transfer inhibiting agent. Said polyvinylimidazoles have an average of about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, mores preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000.
f) Cross-linked polymers Cross-linked polymers are polymers whose backbone are interconnected to a certain degree; these links can be of chemical or physical nature, possibly with active groups n the backbone or on branches; cross-linked polymers have been described in the Journal of Polymer Science, volume 22, pages 1035-1039.
In one embodiment, the cross-linked polymers are rr~ade in such a way that they form a three-dimensional rigid structure, which can entrap dyes in the pores formed by the three-dimensional structure. In another embodiment, the cross-tinked polymers entrap the dyes by swelling.
Such cross-linked polymers are described in the co-pending patent application 94870213.9 WO 99!57259 PCT/US99/09409 Method of washing The compositions of the invention may be used in essentially any washing, cleaning andlor fabric care methods, including soaking methods, pre-treatment methods, methods with rinsing steps for which a sE:parate rinse aid composition may be added and post-treatment methods.
The process described herein comprises contacting fabrics with a laundering solution in the usual manner and exemplified hereunder. A conventional laundry method comprises treating soiled fabric with an aqueous liquid having dissolved or dispensed therein an effective amount of the laundry detergent andlor fabric care composition. The process of the invention is conveniently carried out in the course of the cleaning process. The method of cleaning is preferably carried out at 5°C to 95°C, especially between 10°C and 6Ci°C.
The pH of the treatment solution is preferably from 7 to 12.
The following examples are meant to exemplify compositions of the present invention, but are not necessarily meant to limit or otherwise define the scope of the invention.
In the detergent compositions, the enzymes levels are expressed by pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are expressed by weight of the total compositions. The abbreviated component identifications therein have the following meanings:
Sodium linear 011_13 alkyl benzene sulphonate.
TAS : Sodium tallow alkyl sulphaite.

CxyAS ; Sodium C1x - C1y alkyl sullfate.

CxySAS ; Sodium C1x - C1y secondary (2,3) alkyl sulfate.

CxyEz : C1x - C1y predominantly linear primary alcohol condensed with an average of z moles of ethylene oxide.

CxyEzS : C1x - C1y sodium alkyl sulfate condensed with an average of z moles of ethyf~ene oxide.
QAS : R2.N+(CH3)2(C2H4~H) with R2 = C12-C14~
QAS 1 : R2~N+(CH3)2(C2H4~H) wilth R2 = Cg-011.
APA ~ Cg_1 p amido propyl dimethyl amine.

Soap : Sodium linear alkyl carbo~;ylate derived from a 80/20 mixture of tallow and coconut fatty acids.

STS : Sodium toluene sulphonat:e.

CFAA : C12-C14 alkyl N-methyl glucamide.

TFAA ; C1 g-C' g alkyl N-methyl glucamide.

TPKFA : C12-C14 topped whole cut fatty acids.

DEQA : Di-(tallow-oxy-ethyl) dimetlhyl ammonium chloride.

DEQA (2) : Di-(soft-tallowyloxyethyl) hydroxyethyl methyl ammonium methylsulfate.

DTDMAMS : Ditalllow dimethyl ammonin.~m methylsulfate.

SDASA : 1:2 ratio of stearyldimethyl amineariple-pressed stearic acid.

Silicate ; Amorphous Sodium Silicate (Si~2:Na20 ratio = 1.6-3.2).

Zeolite A : Hydrated Sodium Aluminosilicate of formula Nal2(A102Si02)12. 27H2;0 having a primary particle size in the range from 0.1 to 10 micrometers (Weight expressed on an anhydrous basis).

Na-SKS-6 ; Crystalline layered silicate of formula 8-Na2Si205.

Citrate : Tri-sodium citrate dihydratE~ of activity 86.4%
with a particle size distribution between 425 and 850 micrometres.

Citric : Anhydrous citric acid.

Borate : Sodium borate Carbonate : Anhydrous sodium carbonate with a particle size between 200 and 900 micrometres.

Bicarbonate : Anhydrous sodium hydrogen carbonate with a particle size distribution between 400 and 1200 micrometres.

Sulphate : Anhydrous sodium sulphate:.

Mg Sulphate : Anhydrous magnesium sulfate.

STPP : Sodium tripolyphosphate.

TSPP : Tetrasodium pyrophosphate.

M~AA : Random copolymer of 4:1 acrylatelmaleate, average molecular weight about 70,1700-80,000.

MAIAA 1 : Random copolymer of 6:4 a~crylatelmaleate, average molecular weight about 10,t)00.

I, AA : Sodium poiyacrylate polymer of average malecular weight 4,500:
PB1 : Anhydrous sodium perborate monohydrate of nominal formula NaB02.H202.
PB4 : Sodium perborate tetrahy~drate of nominal formula NaB02.3H20. H202.
Percarbonate : Anhydrous sodium percarbonate of nominal formula 2Na2C03.3H202 .
TAED : Tetraacetylethylenediamine.
NOBS : Nonanoyloxybenzene sulfonate in the form of the sodium salt.
NACA-OBS : {6-nonamidocaproyl) oxybenzene sulfonate.

DTPA : Diethylene triamine penta;acetic acid.

HEDP : 1,1-hydroxyethane diphosphonic acid.

DETPMP : Diethyltriamine penta (me~thylene) phosphonate, marketed by Monsanto under the Trade name bequest 2060.

EDDS : Ethylenediamine-N,N'-disuccinic acid, (S,S) isomer in the form of its sodium salt Photoaetivated : Sulfonated zinc phtalocyanine encapsulated in dextrin Bleach soluble polymer.

Photoactivated : Sulfonated alumino phtalocyanine encapsulated in Bleach 1 dextrin soluble polymer.

Protease : Proteolytic enzyme sold under the tradename Savinase, Alcalase, Durazym by Novo Nordisk AIS, Maxacal, Maxapem sold by Gist-Brocades and proteases described in patents W091/06637 andlor W095110591 andlor EP 251 446.

Amylase : Amylolytic enzyme sold under the tradename Purafact Ox AmR described in WO 94/18314, W096105295 sold by Genencor; Termamyl~,. Fungamyl~ and Duramyl~, all available from Novo Nordisk A!S and those described in WO95126397.

Lipase : Lipolytic enzyme sold undE~r the tradename Lipolase, Lipolase Ultra by Novo Nordisk AlS and Lipomax by Gist-Brocades.

CBD-Cellulase : Cellulytic enzyme core derived tram the enzyme sold under the tradename CarE:zyme by Novo Nordisk AlS
linked to the CBD of the CenC cellulase of Cellulomonas frmi, either the tandem CBDN1 N2 or the single CBDN1 or CBDN2 and/or linked to the CBD from the cellulase .
E3 of Thermomonospora ~Fusca; and/or Cellulytic enzyme core derived from the enzyme sold under the tradename Care:zyme by Novo Nordisk A/S
linked by the f-lumicola lns;olens family 45 cellulase linker to the CBD of the CenC cE;llulase of Cellulomonas firm, either the tandem CBDN11V2 or the single CBDN1 or CBDN2; and/or Cellulytic enzyme core derived from the enzyme sold under the tradename Carezyme by Novo Nordisk AlS
linked by the E3 cellulase Thermomonospora fusca linker to the CBD from the cellulase E3 of Thermomonospora fusca.
Cellulase : Celluiytic enzyme sold undier the tradename Carezyme, Endolase by Novo Nordisk A/S; and/or Clazinase, Puradex HAI, EGIII cellula:;e from Trichoderma reseei by Genencor.
CMC : Sodium carboxymethyl cellfulose.
PVP : Polyvinyl polymer, with an average molecular weight of 60, 000.
PVNO : Polyvinylpyridine-N-Oxide, with an average molecular weight of 50,000.
PVPVI : Copolymer of vinylimidazole and vinylpyrrolidone, with an average molecular weight of 20,000.
Brightener 1 : Disodium 4,4'-bis(2-sulphoatyryl)biphenyl.
Brightener 2 : Disodium 4,4'-bis(4-anilino-~6-morpholino-1.3.5-triazin-2-yl) stilbene-2:2'-disulfonate.
Silicone antifoam : Polydimethylsiloxane foam controller with siloxane-oxyalkylene copolymer as dispersing agent with a ratio of said foam controller to said dispersing agent of 10:1 to 100:1.

Suds Suppressor : 12% Silicone/silica, 18% stearyl alcoho1,70% starch in granular form.
Opacifer : Water based monostyren~e latex mixture, sold by BASF
Aktiengesellschaft under ilhe tradename Lytron 621.
SRP 1 : Anionically end capped poly esters.
SRP 2 : niethoxylated poly (1,2 propylene terephtalate) short block polymer. .~
QEA : bis((C2H50)(C2H40)n)(C~H3) -N+-C6H12-N~'-(CH3) bis((C2H50)-(C2H40))n, 'wherein n = from 20 to 30.
PEI : Polyethyleneimine with an average molecular weight of 1800 and an average ethoxylation degree of 7 ethyleneoxy residues per nitrogen.
SCS : Sodium cumene sulphona;te.
HMWPEO : High molecular weight polyethylene oxide.
PEGx : Polyethylene glycol, of a nnoiecular weight of x .
PEO : Polyethylene oxide, with an average molecular weight of 5,000.
TEPAE : TetreaethylenepentaaminE: ethoxylate.
Example 1 The following high density laundry detergent compositions were prepared according to the present invention I II III IV V VI

1-AS 8.0 8.0 8.0 2.0 6.0 6.0 TAS - 0.5 - 0.5 1.0 0.1 C46(S)AS 2.0 2.5 - - - _ C25AS - - - 7.0 4.5 5.5 C68AS 2.0 5.0 7.0 - -C25E5 - - 3.4 10.0 4.6 4.6 C25E7 3.4 3.4 1.0 - - -C25E3S - - - 2.0 5.0 4.5 QAS - 0.8 - .- _ _ QAS 1 - - - 0.8 0.5 1.0 Zeolite A 18.1 18.0 14.1 18.1 20.0 18.1 WO 99!57259 PCT/~JS99/09409 r a ur rv v yr Citric - - - 2.5 - 2.5 Carbonate 13.0 13.0 27.0 10.0 10.0 13.0 Na-SKS-6 - - - 10.0 - 10.0 Silicate 1.4 1.4 3.0 0.3 0.5 0.3 Citrate - 1.0 - 3.0 _ _ Sulfate 26.1 26.1 26.1 6.0 - -Mg sulfate 0.3 _ - 0.2 - 0.2 M~~ 0.3 0.3 0.3 4.0 1.0 1.0 CMC 0.2 0.2 0.2 0.2 0.4 0.4 PB4 9.0 9.0 5.0 - - -Percarbonate - - - - 18.0 18.0 TAED 1.5 0.4 1.5 - 3.9 4.2 NACA-OBS - 2.0 1.0 - - _ DETPMP 0.25 0.25 0.25 0.25 - -SRP 1 - - - 0.2 - 0.2 EDDS - 0.25 0.4 - 0.5 0.5 CFAA - 1.0 - 2.0 - _ HEDP 0.3 0.3 0.3 0.3 0.4 0.4 QEA - - - 0.2 - 0.5 Protease 0.009 0.009 0.01 0.04 0.05 0.03 Amylase 0.002 0.002 0.002 0.006 0.008 0.008 CBD-cellulase 0.0007 0.01 0.0007 0.008 0.0008 0.001 Cellulase - - 0.0007 - 0.0007 0.0001 Lipase 0.006 - - 0.01 0.01 0.01 Photoactivated 15 15 15 - 20 20 bleach (ppm) PVNO/PVPVI - - - 0.1 - -Brightener 1 0.09 0.09 0.09 - 0.09 0.09 Perfume 0.3 0.3 0.3 0.4 0.4 0.4 Silicone antifoam0.5 0.5 0.5 - 0.3 0..3 Density in g/litre850 850 850 850 850 850 Miscellaneous Up to 100%
and minors Example 2 WO 99/5'1259 PCT/US99/09A09 The following granular laundry detergent compositions of particular utility under European machine wash conditions were prepared according to the present invention I II III IV V Vt LAS 5.5 7.5 5.0 5.0 6.0 7.0 TAS 1.25 1.9 - 0.8 0.4 0.3 C24AS/C25AS - 2.2 5.0 5.0 5.0 2.2 C25E3S - 0.8 1.0 1.5 3.0 1.0 C45E7 3.25 = - - - 3.0 TFAA _ _ 2.0 - - _ C25E5 - 5.5 - - - _ QAS 0.8 - - - .. _ QAS 1 - 0.7 1.0 0.5 1.0 0.7 STPP 19.7 - - - - -Zeolite A - 19.5 25.0 19.5 20.0 17.0 NaSKS-6/citric ~- 10.6 - 10.6 - -acid (79:21 ) Na-SKS-6 - - 9.0 - 10.0 10.0 Carbonate 6.1 21.4 9.0 10.0 10.0 18.0 Bicarbonate - 2.0 7.0 5.0 - 2.0 Silicate 6.8 - - 0.3 0.5 -Citrate - - 4.0 4.0 -Sulfate 39.8 - - 5.0 ~ - 12.0 Mg sulfate - - 0.1 0.2 0.2 MAIAA 0.5 1.6 3.0 4.0 1.0 1.0 CMC 0.2 0.4 1.0 1.0 0.4 0.4 PB4 5.0 12.7 - _ _ _ Percarbonate - - - - 18.0 15.0 TAED 0.5 3.1 - - 5.0 -NACA-OBS 1.0 3.5 - - - 2.5 DETPMP 0.25 0.2 0.3 0.4 - 0.2 HEDP - 0.3 - 0.3 0.3 0.3 QEA - - 1.0 'I.0 1.0 -Protease 0.009 0.03 0.03 0.05 0.05 0.02 Lipase 0.003 0.003 0.006 0.006 0.006 0.004 CBD-cellulase 0.01 0.005 0.005 0.005 0.01 0.008 WO 99/57259 PCT/fJS99/09409 Cellulase 0.0006 - 0.0005 - - 0.0007 Amylase 0.002 0.002 0.006 0.006 0.01 0.003 PVNOIPVPVI - - 0.2 0.2 - -PVP 0.9 1.3 - _ - 0.9 SRP 1 - - 0.2 0.2 0.2 -Photoactivated 15 27 - - 20 20 bleach (ppm) Photoactivated 15 -: - - -bleach 1 (ppm) Brightener 1 0.08 0.2 - - 0:09 0.15 Brightener 2 - 0.04 - - _ _ Perfume 0.3 0:5 0.4 0.3 0.4 0.3 Silicone antifoam 0.5 2.4 0.3 0.5 0.3 2.0 Density in gllitre 750 750 750 750 750 750 Miscellaneous and minors Up i :o 100%

Example 3 The following detergent formulations ility European of particular ut under machine wash conditions were prepared ntion according to the present inve I II III IV

Blown Powder LAS 6.0 5.0 11.0 6.0 TAS 2.0 - - 2.0 Zeoiite A 24.0 - - 20.0 STPP - 27.0 24.0 -Sulfate 4.0 6.0 13.0 -MAJAA 1.0 4.0 6.0 2.0 Silicate 1.0 7.0 3.0 3.0 CMC 1.0 1.0 ~ 0.5 0.6 Brightener 1 0.2 0.2 0.2 0.2 Silicone antifoam 1.0 1.0 1.0 0:3 DETPMP 0.4 0.4 0.2 0.4 Spray On WO 99/5759 PCT/iJS99/09409 I II III IV

Brightener 0.02 - - 0.02 C45E7 - - - 5,0 C45E2 2.5 2.5 2.0 C45E3 2.6 2.5 2.0 -Perfume 0.5 0.3 0.5 0.2 Silicone antifoam 0.3 0.3 0.3 -Dry additives QEA - _ - 1.0 EDDS 0.3 - -Sulfate 2.0 3.0 5.0 10.0 Carbonate 6.0 13.0 15.0 14.0 Citric 2.5 - - 2,0 QAS 1 0.5 - - 0.5 Na-SKS-6 '! 0.0 - - -Percarbonate 18.5 - -PB4 - 18.0 10.0 21.5 TAED 2.0 2.0 - 2.D

NACA-OBS 3.0 2.0 4.0 -CBD-cellulase 0.0005 0.01 0.005 0.01 Cellulase 0.0004 - - 0.0008 Protease 0.03 0.03 0.03 0.03 Lipase 0.008 0.008 0.008 0.004 Amylase 0.003 0.003 0.003 0.006 Brightener 1 0.05 - - 0.05 Miscellaneous and Up to minors 100%

Example 4 The following granular preparedaccording detergent formulations to the were present invention I 11 Ill IV V VI

Blown Powder LAS 23.0 8.0 7.0 9.0 7.0 7.0 TAS - - - - 1.0 -I II Ill IV V VI

c45AS s.o s.o 5.o s.o - _ C45AES - 1.0 1.0 1.0 - -C45E35 - - - - 2.0 4.0 Zeolite A 10.0 18.0 14.0 12.0 10.0 10.0 MA/AA - 0.5 - - - 2.0 MA/AA 1 7.0 - _ _ _ -AA - 3.0 3.0 2.0 3.0 3.0 Sulfate 5.0 5.3 14.3 11.0 15.0 19.3 Silicate 10.0 1.0 1.0 1.0 1.0 1.0 Carbonate 15.0 20.0 10.0 20.7 8.0 6.0 PEG 4000 0.4 1.5 1.5 1.0 1.0 1.0 DTPA - 0.9 0.5 - - 0, Brightener 2 0.3 0.2 0.3 - 0.1 0.3 Spray On C45E7 - 2.0 - - 2.0 2.0 C25E9 3.0 - - - _ _ C23E9 - - 1.5 2.0 - 2.0 Perfume 0.3 0.3 0.3 2.0 0.3 0.3 Agglomerates C45AS ~- 5.0 5.0 2.0 - 5_0 LAS - 2.0 2.0 - - 2.0 Zeolite A - 7.5 7.5 8.0 - 7.5 Carbonate - 4.0 4.0 5.0 - 4.0 PEG 4000 - 0.5 0.5 - - 0.5 Misc (Water etc.) - 2.0 2.0 2:0 - 2.0 Dry additives QAS - - _ - 1.0 -Citric - - - _ 2.0 -PB4 - - - - 12.0 1.0 PB1 4.0 1.0 3.0 2.0 - _ Percarbonate - - - - 2.0 10.0 Carbonate - 5.3 1.8 - 4.0 4.0 NOBS 4.0 - 6.0 - - 0.6 Methyl cellulose 0.2 - - _ _ -Na-SKS-6 8.0 - - _ _ _ I II III IV V VI

sTS - - 2. a - 1.0 -Culmene sulfonic - 1.0 - - - 2.0 acid Protease 0.02 0.02 0.02 0.01 0.02 0.02 Lipase 0.004 - 0.004 - 0.004 0.008 Amylase 0.003 - 0.002 - 0.003 -CB~-cellulase 0.0005 0.01 0.0005 0.01 0.01 0.0005 Celiulase - - a.o005 0.0007 - 0.0008 PVPVI - - - - 0.5 0.1 PVP - - _ - 0.5 -PVNO - - 0.5 0.3 - -QEA - - - - 1.0 -SRP 1 0.2 0.5 0.3 - 0.2 -Silicone antifoam0.2 0.4 0.2 0.4 0.1 -Mg sulfate - - 0.2 - 0.2 -Miscellaneous Up ~to 100%
and minors Example 5 The following nil bleach-containing detergentformulations of particular use in the washing of coloured clothingre prepared we according to the present invention I II III
Blown Powder Zeolite A 15.0 15.0 -Sulfate - ;5.0 -LAS 3.0 :3.0 -DETPMP 0.4 17.5 -CIVIC 0.4 t).4 -MA/AA 4.0 4.0 -Agglomerates C45AS - - 11.0 LAS 6.0 fi.0 -TAS 3.0 2.0 -I ll Ill Silicate 4.0 ~4.0 -Zeolite A 10.0 15.0 13.0 CMC - - 0.5 MA/AA - - 2.0 Carbonate 9.0 7.0 7.0 Spray-on Perfume 0.3 0.3 0.5 C45E7 4:0 ~L0 4.0 C25E3 2.0 2.0 2.0 Dry additives MA/AA - - 3.0 Na-SKS-6 - - 12.0 Citrate 10.0 - 8,p Bicarbonate 7.0 3.0 5.0 Carbonate 8.0 5.0 7.0 PVPVUPVNO 0.5 (1i.5 0.5 Protease 0.03 0.02 0.05 Lipase 0.008 0.t708 0.008 Amylase 0.01 0.01 '0.01 CBD-cellulase 0.0005 0.01 0.005 Ceiluiase 0.0008 O.t)01 -Silicone antifoam 5.0 5.0 5.0 Sulfate - 9.0 -Density (gllitre) 700 7n0 700 Miscellaneous and minors Up tc> 100%

Exam~ole fi The following detergent prepared .according formulations were to the present invention I II III IV

Base granule Zeolite A 30.0 22.0 24.0 10.0 Sulfate 10.0 5.0 10.0 7.0 MA/AA 3.0 - - -I II III IV

AA - 1.6 2.0 -MA/AA 1 - 12.0 - 6.0 LAS 14.0 10.0 9.0 20.0 C45AS 8.0 7.0 9.0 7.0 C45AES - 1.0 1.0 Silicate - 1.0 0.5 10.0 Soap - 2.0 -Brightener 1 0.2 0.2 0.2 0.2 Carbonate 6.0 9.0 10.0 1 ~.0 PEG 4000 - 1.0 1.5 -DTPA - 0.4 -Spray On C25E9 - - - 5.0 C45E7 1.0 1.0 - _ C23E9 - 1.0 2.5 Perfume 0.2 0.3 0.3 Dry additives Carbonate 5.0 10.0 18.0 8.0 PVPVI/PVNO 0.5 - 0.3 -Protease 0.03 0.03 0.03 0.02 Lipase 0.008 - - 0.008 Amylase 0.002 - - 0.002 CBD-cellulase 0.01 0.0005 0.01 0.0005 Cellulase 0.0002 0.0005 - _ NOBS - 4.0 - 4.5 PB 1 1.0 5.0 1.5 6.0 Sulfate 4.0 5.0 - 5.0 SRP 1 - 0.4 - _ Suds suppresser - 0.5 0.5 Miscellaneous and minors Up to 100%

Example 7 The following granular detergent formulations werE; prepared according to the present invention WO 99!57259 PCT/US99/09409 I II lil Blown Powder Zeolite A 20.0 - 15.0 STPP - 20.0 -Sodium sulfate - - 5.0 Carbonate - - 5.0 TAS - - 1.0 LAS 6.0 6.0 6.0 C68AS 2.0 2.0 -Silicate 3.0 8.0 MA/AA 4.0 2.0 2.0 CMC 0.6 0.6 0.2 Brightener 1 0.2 0.2 0.1 DETPMP 0.4 0.4 0.1 STS - - 1.0 Spray On c45E7 5.0 5.0 4.a Silicone antifoam0.3 0.3 0.1 Perfume 0.2 0.2 0.3 Dry additives QEA - - 1.0 Carbonate 14.0 9.0 10.0 PB1 1.5 2.0 -PB4 18.5 13.0 13.0 TAED 2.0 2.0 2.0 QAS - - 1.0 Photoactivated 15 ppm 15 ppm 15 ppm bleach Na-SKS-6 - - 3.0 Protease 0.03 0.03 0.007 Lipase 0.004 0.004 0.004 Amylase 0.006 0.006 0.003 CBD-cellulase 0.0005 0.01 0.005 Cellulase 0.0002 - -Sulfate 10.0 20.0 5.0 Density (g/litre) 700 700 700 WO 99/57259 PCTlCJS99/09409 Miscellaneous and minors Up to 100%
Exami~le 8 The following detergent formulations were prepared according to the present invention Blown Powder Zeolite A 15.0 15.0 15.0 Sulfate - 5.0 LAS 3.0 3.0 3.0 QAS - 1.5 1.5 DETPMP 0.4 0.2 0.4 EDDS - 0.4 0.2 CMC 0.4 0.4 0.4 MAIAA 4.0 2.0 2.0 Agglomerate LAS 5.0 5.0 5.0 TAS 2.0 2.0 1.0 Silicate 3.0 3.0 4.0 Zeolite A 8.0 8.0 8.0 Carbonate 8.0 8.0 4.0 Spray 4n Perfume 0.3 0.3 0.3 C45E7 2.0 2.0 2.0 C25E3 2.0 - -~ry Additives Citrate 5.0 - 2.0 Bicarbonate - 3.0 -Carbonate 8.0 15.0 10.0 TAED 6.0 2.0 5.0 PB1 14.0 7.0 10.0 PEO - - 0_2 Bentonite clay- - 10.0 Protease 0.03 0.03 0.03 WO 99/57259 PCT/~JS99/09409 I II III
Lipase 0.008 0.008 0.008 CBD-cellulase 0.005 0.01 0.0005 Cellulase - 0.0007 0.001 Amylase 0.01 0.01 0.01 Silicone antifoam 5.0 5.0 5.0 Sulfate - 3.0 -Density (gllitre) 850 850 850 Miscellaneous and minors Up to 100%

Example 9 The following detergent formulations were prepared according to the present invention I II III IV' LAS 18.0 14.0 24.0 20.0 QAS 0.7 1.0 - 0.7 TFAA - 1, 0 _ C23E56.5 - - 1.0 -C45E7 - 1.0 _ _ C45E3S 1.0 2.5 1.0 -STPP 32.0 18.0 30.0 22.0 Silicate ~ 9.0 5.0 9.0 8.0 Carbonate 11.0 7.5 10.0 5.0 Bicarbonate - 7,5 _ _ PB1 3.0 1.0 - -PB4 - 1.0 -NOBS 2.0 1.0 - -DETPMP - 1.0 - -DTPA 0.5 - 0.2 0.3 SRP 1 0.3 0.2 - 0,1 M~~ 1.0 1.5 2.0 0.5 CMC 0.8 0.4 0.4 0.2 PEI - - 0.4 -Sulfate 20.0 10.0 20.0 30.0 I II III IV

Mg sulfate 0.2 - 0.4 0.9 Protease 0.03 0.03 0.02 0.02 Amylase 0.00$ 0.007 - 0.004 Lipase 0.004 - 0.002 -CBD-cellulase 0.0005 0.01 0.0005 0.005 Cellulase - - 0.003 0.001 Photoactivated bleach 30 ppm 20 ppm - 10 ppm Perfume 0.3 0.3 0.1 0.2 Brightener 1/2 0.05 0.02 0.08 0.1 Miscellaneous and Minors up to 100%

Example 10 The following liquid detergent formulations were prepared according to the present invention (Levels are given in parts per weiight) I II III IV V

LAS 11.5 8.8 - 3.9 -C25E2.5S - 3.0 18.0 - 16.0 C45E2.25S 11.5 3.0 - 15.7 -C23E9 - 2.7 1.8 2.0 1.0 C23E7 3.2 - - - -CFAA - - 5.2 - 3.1 TPKFA 1.6 - 2.0 0.5 2.0 Citric (50%) 6.5 1.2 2.5 4.4 2.5 Ca formate 0.1 0.06 0.1 - -Na formate 0.5 0.06 0.1 0.05 0.05 SCS 4.0 1.0 3.0 1.2 -Borate 0.6 - 3.0 2.0 2.9 Na hydroxide 5.8 2.0 3.5 3.7 2.7 Ethanol 1.75 1.0 3.6 4.2 2.9 1,2 Propanediol 3.3 2.0 8.0 7.9 5.3 Monoethanolamine 3.0 1.5 1.3 2.5 0.8 TE PAE 1.6 - 1.3 1.2 1:2 Protease 0.03 0.01 0.03 0.02 0.02 II III IV V

Lipase - - 0.002 - -Amylase - - - 0.002 -CBD-cellulase 0.0005 0.01 0.005 0.01 0.005 Cellulase 0.001 - - 0.0005 -SRP 1 0.2 - 0.1 -DTPA _ _ 0.3 _ PVNO - - 0.3 - 0.2 Brightener 1 0.2 0.07 0.1 - _ Silicone antifoam 0.04 0.02 0.1 0.1 0.1 Miscellaneous and Up to 100%
water Example 11 The following liquid detergent formulations werE: prepared according to the present invention (Levels are given in parts per weiight) I II III IV

~S 10.0 '13.0 9.0 -C25AS 4.0 1.0 2.0 '10.0 C25E3S 1.0 _ _ 3.0 C25E7 6.0 8.0 13.0 2.5 TFAA - - - 4.5 APA - 1.4 - _ TPKFA 2.0 - 13.0 7.0 Citric 2.0 3.0 1.0 1.5 Dodecenyl ! tetradecenyl 12.0 10.0 - -succinic acid Rapeseed fatty acid 4.0 2.0 1.0 Ethanol 4.0 ~4.0 7.0 2.0 1,2 Propanediol 4.0 4.0 2.0 ~,0 Monoethanolamine - _ _ 5.0 Triethanolamine _ _ g.~

TEPAE 0.5 - 0.5 0.2 DETPMP 1.0 'I.0 0.5 1.p Protease 0.02 0.02 0.01 0.008 Lipase - 0.002 - 0.002 I ll lil IV

Amylase 0.004 0.004 0.01 0.008 CBD-cellulase 0.0005 i).0008 0.003 0.002 Cellulase - 0.0007 0.0007 -SRP 2 0.3 - 0.3 0.1 Boric acid 0.1 0.2 1.0 2.0 Ca chloride - 0.02 - 0.01 Brightener 1 - 0.4 - _ Suds suppressor ~ 0.1 0.3 - 0.1 Opacifier 0.5 0.4 - 0.3 NaOH up to pH 8.0 8.0 7.6 7.7 Miscellaneous and water Up to 100%

Example 12 The following liquid detergent formulations werE: prepared according to the present invention (Levels are given in parts per weight) I II III iV

~S 25.0 - _ _ C25AS - 13.0 18.0 15.0 C25E3S - s>_.0 2.0 4.0 C25E7 - - 4.0 4.0 TFAA - Ei.O 8.0 8.0 APA 3.0 1.0 2.0 -TPKFA - 1.5.0 11.0 11.0 Citric 1.0 1.0 1.0 1.0 Dodeceny! J tetradecenyi 15.0 - - ,_ succinic acid Rapeseed fatty acid 1.0 _ 3.5 Ethanol 7.0 2.0 3.0 2.0 1,2 Propanediol 6.0 8.0 10.0 13.0 Monoethanalamine _ _ 9.0 9.0 TEPAE - ~- 0.4 0.3 DETPMP 2.0 1..2 1.0 Protease 0.08 0.02 0.01 0.02 Lipase - -~ 0.003 0.003 WO 99/57259 PCT/US99/09a09 I II III IV

Amylase 0.004 0.01 0.01 0.01 CBD-cellulase 0.0003 0.0006 0.004 0.003 Cellulase 0.0003 - _ _ SRP 2 - - 0.2 0.1 Boric acid 1.0 1.5 2.5 2.5 Bentonite clay 4.0 4.0 - _ Brightener 1 0.1 0.2 0.3 Suds suppressor 0.4 - _ _ Opacifier 0,8 0.7 - -NaOH up to pH 8.0 7.5 8.0 g,2 Miscellaneous and wafer Up to 100%

Example 13 The following liquid detergent compositions were prepared according to the present invention {Levels are given in parts by weic,~ht) I It ~S 27.6 18.9 C45AS 13.8 5.9 C13E8 3.0 3.1 Oleic acid 3.4 2.5 Citric 5.4 5.4 Na hydroxide 0.4 3.6 Ca Formate 0.2 0.1 Na Formate _ 0.5 Ethanol 7.0 -Monoethanolamine 16.5 g_0 1,2 propanediol 5.9 5.5 Xylene sulfonic acid - 2.4 TEPAE 1.5 0.8 Protease 0.05 0.02 CBD-cellulase 0.0003 0.0006 Cellulase - 0.0002 PEG _ 0.7 I II
Brightener 2 0.4 0.1 Perfume 0.5 0.3 Miscellaneous and water Up to 100%
Example 14 The following granular fabric detergent compositions which provide '°softening through the wash" capability were prepared according to the present invention t II
C45AS - 10.0 ~S 7.fi C6$AS 1.3 -C45E7 4.0 C25E3 - 5.0 Coco-alkyl-dimethyl hydroxy-1.4 ~ 1.0 ethyl ammonium chloride Citrate 5.0 3.0 Na-SKS-6 - 11.0 Zeolite A 15.0 15.0 M~~ 4.0 4.0 DETPMP 0.4 0.4 PB1 15.0 -Percarbonate - 15.0 TAED 5.0 5.0 Smectite clay 10.0 10.0 HMWPEO - 0.1 Protease 0.02 0.01 Lipase 0.02 0.01 Amylase 0.03 0.005 CBD-celluiase 0.01 0.0009 Cellulase 0.005 0.001 Silicate 3.0 5,0 Carbonate 10.0 10.0 Suds suppressor 1.0 4,0 i WO 99/5'7259 PC'~'/US99/09409 I II
CMC
0.:?
0.1 WateNminors Up to 1100%
Example 15 The following rinse added fabric softener compositions were prepared according to the present invention I II
DEQA (2) 20.0 20.0 CBD-celluiase 0.001 0.001 Cellulase _ 0.0005 HCL 0.03 0.03 Antifoam agent 0.01 0.01 Blue dye 25ppm 25ppm CaCl2 0.20 0.20 Pertume 0.90 0.90 Miscellaneous and water Up to 1 Ci0%

Exam~te 10 The following fabric softener and fabric dryer added conditioner compositions were prepared according to the present invention I II lil IV V

DEQA 2.6 19.0 - _ _ DEQA(2) _ _ - - 51.8 DTMAMS - - - 26.0 -SDASA - - 70.0 42.0 40.2 Stearic acid of IV=0 0.3 - _ _ Neodol45-13 _ _ 13.0 - _ Hydrochloride acid 0.02 0.02 - _ Ethanol _ _ 1.0 - -CBD-celluiase 0.0001 0.001 0.0005 0.005 0.0003 Celiulase 0.001 - 0.0007 - 0.0003 WO 99/57259 PCTlUS99/09409 I II III IV V

Perfume 1.0 1.0 0.75 1.0 1.5 Glycoperse S-20 - - - - 15.4 Glycerol monostearate- - - 26.0 -Digeranyl Succinate - - 0.38 - _ Silicone antifoam 0.01 0.01 - _ _ Electrolyte - 0.1 _ _ _ Clay - - - 3.0 -Dye 10ppm 25ppm 0.01 - -Water and minors 100% 100% - - _ Example 17 The following laundry bar detergent compositions were prepared according to the present invention I 11 III VI V Ill VI V

~S - - 19.0 15.0 :? 6.75 8. -1.0 8 C28AS 30.0 13.5 - - - 15.75 11.2 22.5 Na Laurate 2.5 9.0 - - - _ _ _ Zeolite A 2.0 1.25 - - - 1.25 1.25 1.25 Carbonate 20.0 3.0 13.0 8.0 'I0.0 15.0 15.0 10.0 Ca Carbonate27.5 39.0 35.0 - - 40.0 - 40.0 Sulfate 5.0 5.0 3.0 5.0 3.0 - - 5.0 TSPP 5.0 - _ _ - 5.0 2.5 -STPP 5.0 15.0 10.0 - - 7.0 8.0 10.0 Bentonite - 10.0 - - :5.0 - - -clay DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7 CMC - 1.0 1.0 1.0 1.0 - - 1.0 Talc - - 10.0 15.0 10.0 - - -Silicate - - 4.0 5.0 3.0 - - -PVN4 0.02 0.03 - 0.01 - 0.02 - _ MA/AA 0.4 1.0 - - t).2 0.4 0.5 0.4 SRP 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3 Amylase - - 0.01 - _ - 0.002 -Protease - 0.004 - 0.003 0.003 - - 0.003 I II III Vl V III VI V

Lipase - 0.002 - 0.002 - - _ _ CBD-cellulase.0008 .0003 .0002 .0003 .0003 .0002 .0005 .0005 Cellulase - - - .0005 - .0002 .0004 -PEO - 0.2 - 0.2 0.3 - - 0.3 Perfume 1.0 0.5 0.3 0.2 0.4 - - 0.4 Mg sulfate - - 3.0 3.0 3.0 - - -Brightener 0.15 0.1 0.15 - - - - 0.1 Photoactivated- 15.0 15:0 15.0 '15.0 - - 15.0 bleach (ppm) Example 18 The following pre- or post treatment compositions were prepared in accord with the present invention I Il III ~IV

DEQA (2) - - 20.0 20.0 CBD-cellulase 0.0008 0.002 0.001 0.001 Cellufase 0.0005 - 0.0005 -HCL - - 0.03 0.03 Antifoam agent - - 0.01 0.01 Biue dye 25ppm 25ppm 25ppm 25ppm CaCl2 - - 0.20 0.20 Perfume 0.90 0.90 0.90 0.90 Water / minors Up to '! 00/~

Claims (25)

81

1. A modified enzyme comprising a catalytically active: amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a cellulose binding domain having a relative binding constant for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 4l/gcellulose.

2. A modified enzyme according to claim 1 wherein said catalytically active amino acid sequence derives from a cellulolytic enzyme having a specific activity above 50 CEVU/mg.

3. A modified enzyme according to claims 1 to 2 wherein the catalytically active amino acid sequence derives from a cellulolytic enzyme deriving from a fungal strain, preferably from a Humicola Insolens strain.

4. A modified enzyme according to claim 3 wherein the said catalytically active amino acid sequence derives from a 43kD endoglucanase derived from Humicola insolens, DSM 1800 strain.

5. A modified enzyme according to any of the preceding claims wherein the amino acid sequence comprising a cellulose binding domain is derived from a fungal or bacterial strain, preferably a bacterial strain.

6. A modified enzyme according to claim 5 wherein said amino acid sequence comprising a cellulose binding domain is selected from the cellulose binding domains of family II and/or family IV.

7. A modified enzyme according to claim 6 wherein said amino acid sequence comprising a cellulose binding domain is selected from the family IV
cellulose binding domain, preferably derived from organisms selected from the group consisting of Cellulomonas fimi, Clostridium cellulolyticum, Myxoccus xanthus, Streptomyces reticuli, Clostridium stecorarium (NCIMB11754) and/or Thermomonospora fusca.

8. A modified enzyme according to claim 7 wherein said amino acid sequence comprising a cellulose binding domain is selected from the N-terminal CBDs from Cellulomonas fimi .beta.-1,4-glucanase CenC, CBD-dimer from Clostridium stecorarium (NCIMB11754) XynA and/or the CBD E3 from Thermonospora fusca.

9. A modified enzyme according to any of the preceding claims wherein the amino acid sequence comprising a cellulose Binding Domain is further characterised by having a relative binding constant for binding bacterial microcrystalline cellulose lower than 1l/gcellulose, preferably lower than 0.5l/gcellulose.

10. A modified enzyme according to claim 9 wherein the amino acid sequence comprising a cellulose binding domain is further characterised by having a relative binding constant for binding to amorphous cellulose to a relative binding constant for crystalline cellulose ratio above 3.

11. A modified enzyme according to any of the preceding claims providing an enzymatic hydrolysis activity on phosphoric acid-swollen cellulose higher than 60 moles glucose equivalents released per minute and per mole enzyme.

12. A modified enzyme according to any of the preceding claims further comprising a linking region between the catalytically active amino acid sequence of a cellulolytic enzyme and the amino acid sequence comprising a cellulose binding domain.

13. A modified enzyme according to claim 12 wherein the linking region is an amino acid linking region.

14. A modified enzyme according to claim 12 wherein the linking region is a non-amino acid linking region, preferably a polymer selected from PEG(NPC)2, (NH2)2-PEG, t-BOC-NH-PEG-NH2, MAL-PEG-NHS, and/or VS-PEG-NHS polymers.

15. A modified enzyme according to any of the preceding claims wherein said catalytically active amino acid sequence of a cellulolytic enzyme is alkaline.

16. A laundry detergent and/or fabric care composition comprising a laundry detergent and/or fabric care ingredient and a modified enzyme according to claims 1-15.

17. A laundry detergent and/or fabric care composition according to claim 16 wherein said modified enzyme is present at a level of from 0.0001 % to 2%, preferably from 0.0001 % to 0.5%, more preferably from 0.0005% to 0.1 pure modified enzyme by weight of total composition.

18. A laundry detergent and/or fabric care composition according to any of the preceding claims further comprising a builder component, preferably a zeolite A and/or sodium tripolyphophate.

19. A laundry detergent and/or fabric care composition according to any of the preceding claims further comprising a smectite clay.

20. A laundry detergent and/or fabric care composition according to any of the preceding further comprising one or more cationic surfactants.

21. A laundry detergent and/or fabric care composition according to claim 20 wherein the cationic surfactant comprises two long alkyl chain lengths.

22. A laundry detergent and/or fabric care composition according to any of the preceding claims further comprising a dye transfer inhibiting polymer.

23. A laundry detergent and/or fabric care composition according to any of the preceding claims which is in the form of an additive, a pre-treatment, a post-treatment, a soaking treatment and/or a rinsing treatment composition.

24. A method comprising the step of contacting a fabric with a laundry detergent and/or fabric care composition according to claims 16-23 for fabric care, including anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, for static control, fabric softness, colour appearance and fabric anti-wear properties and benefits.

25. A method comprising the step of contacting a fabric with a laundry detergent and/or fabric care composition according to claims 16-23 for fabric cleaning and/or fabric stain removal andlor fabric whiteness maintenance.