HUE032793T2 - Detergent compositions - Google Patents

Abstract

A composition comprising a modified cellulose derivative having a molecular weight of 20,000 to 500,000 kDaltons or mixtures thereof and a cellulase enzyme characterized in that the weight ratio of the modified cellulose derivative and the active cellulase enzyme protein is 20 : 1 to 10,000: 1 and wherein the composition does not contain from 0.7 to 0.9% by weight of the total composition, of sodium nonanoyloxybenzenesulfonate, and does not contain 10% by weight, based on the total composition, of sodium perborate monohydrate, in which the enzyme is a bacterial alkaline enzyme exhibiting endo-beta-1,4-glucanase activity (EC 3.2.1.4).

Description

Description

FIELD OF THE INVENTION

[0001] This invention relates to cleaning compositions comprising cellulose derivatives. The invention also relates to detergent compositions comprising cellulose enzyme, such as bacterial alkaline enzyme exhibiting endo-beta-1,4-glu-canase activity (E.C. 3.2.1.4). The invention also relates to processes for making and using such products.

BACKGROUND OF THE INVENTION

[0002] Cellulase enzymes have been used in detergent compositions for many years now for their known benefits of depilling, softness and colour care. However, the use of most of cellulases has been limited because of the negative impact that cellulase may have on the tensile strength of the fabrics’ fibers by hydrolysing crystalline cellulose. Recently, cellulases with a high specificity towards amorphous cellulose have been developed to exploit the cleaning potential of cellulases while avoiding the negative tensile strength loss. Especially alkaline endo-glucanases have been developed to suit better the use in alkaline detergent conditions.

[0003] For example, Novozymes in W002/099091 discloses a novel enzyme exhibiting endo-beta-glucanase activity (EC 3.2.1.4) endogenous to the strain Bacillus sp., DSM 12648; for use in detergent and textile applications. Novozymes further describes in W004/053039 detergent compositions comprising an anti-redeposition endo-glucanase and its combination with certain cellulases having increased stability towards anionic surfactant and/or further specific enzymes. Kao’s EP 265 832 describes novel alkaline cellulase K, CMCase I and CMCase II obtained by isolation from a culture product of Bacillus sp KSM-635. Kao further describes in EP 1 350 843, alkaline cellulase which acts favourably in an alkaline environment and can be mass produced readily because of having high secretion capacity or having enhanced specific activity.

[0004] Anionically modified cellulose derivatives such as carboxymethyl cellulose (CMC) are established anti-redepo-sition polymers in detergent compositions. The combination of celluloses with CMC has been disclosed, for example in GB-A-2095275. The present inventors have found that the combination of a specific alkaline bacterial cellulose and specific modified celluloses leads to a significant improvement in cotton stain repellency. Whilst not wishing to be bound by theory, it is believed that over multiple wash cycles, the modified cellulose derivatives deposit on cotton items and are acted upon by the bacterial alkaline cellulose so as to seal pores in the fibres of the laundered fabric surface. This results in a fabric surface which is less likely to form strong associations with particulate soils. There is therefore an improvement in the appearance of the laundered fabric and improved cleaning.

SUMMARY OF THE INVENTION

[0005] The present invention relates to a composition comprising a modified cellulose derivative having a molecular weight from 20 000 to 500 000 kDaltonsand a cellulase enzyme, characterised in that the cellulase enzyme is a bacterial alkaline enzyme exhibiting endo-beta 1,4-glucanase activity (E.C.3.2.1.4) and the weight ratio of the modified cellulose component to the active cellulose enzyme protein is from 20:1 to 10000:1. The compositions of the invention do not contain 0.7 to 0.9 wt % sodium nonanoyloxybenzene sulphonate. The compositions of the invention do not contain 10 wt % sodium perborate monohydrate. The compositions of the invention typically do contain less than 8 % by weight and/or greater than 8.5 % by weight sodium sulphate (anhydrous), more specifically do not contain 8.0 to 8.3 wt% sodium sulphate. The present invention also includes a composition comprising a modified cellulose derivative or mixtures thereof and a cellulase enzyme characterised in that the weight ratio of the modified cellulose derivative to the active cellulase enzyme protein is from 1:1 to 10000:1 and wherein the composition does not contain 0.7 to 0.9 % by weight of the total composition, of sodium nonanoyl oxybenzene sulfonate, and does not contain 10 % by weight based on the total composition, of sodium perborate monohydrate, the enzyme producing reducing ends levels of greater than 5mM in the Enzyme Test defined below.

Enzyme Test [0006] The inventors have found that the effectiveness of the endo-beta-(1,4)-glucanase/modified cellulose derivative combination is driven by short oligosaccharide products formed on hydrolysis of the polymer. The present inventors have found that the most effective combinations involve the use of modified cellulose derivative as described herein and an endo-beta-(1,4)-glucanase which provides effective hydrolysis of CMC polymer down to small oligosaccharides as measured using reducing ends analysis as follows, adapted from J. Karlsson et al., Biopolymers, 2002, v63, pp. 32-40 [0007] CMC (250kDa weight average molecular mass, DS 0.7, supplied by Aldrich, Stenheim, Germany), 10g/L, in 50mM sodium acetate pH 5.0 was hydrolysed with an excess of enzyme, 2betaM, for a prolonged hydrolysis time, 72hours. The hydrolysates were then cooled to +4°C before carrying out reducing ends analysis using thedinitrosalicyclic acid reagent, according to the protocol described in M. Bailey et al, Enzyme Microb. Technoi.,1981, v3, pp 153-157, with glucose being used for the standard curve.

[0008] The endo-beta-(1,4)-glucanase enzymes required for the present invention produce reducing ends levels of greater than 5mM in this test, which correlates to -10% reducing ends. Preferred enzymes produce reducing end levels of greater than 10%, preferably greater than 12% or even greater than 15%, using the Enzyme Test.

SEQUENCE LISTINGS

[0009] SEQ ID NO: 1 shows the amino acid sequence of an endoglucanase from Bacillus sp. AA349 SEQ ID NO: 2 shows the amino acid sequence of an endoglucanase from Bacillus sp KSM-S237

DETAILED DESCRIPTION OF THE INVENTION

Definitions [0010] As used herein, the term "cleaning composition" includes, unless otherwise indicated, granular or powder-form all-purpose or "heavy-duty" washing agents, especially laundry detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called heavy-duty liquid types; liquid fine-fabric detergents; as well as cleaning auxiliaries such as bleach additives and "stain-stick" or pre-treat types.

As used herein the term "modified cellulose derivative" comprises polymers comprising a cellulose backbone wherein the cellulose is substituted with at least one substituent or modifying group. A monomer of cellulose is shown below.

R1, R2 and R3 show the positions in the cellulose monomer available for substitution. In the natural cellulose polymer, these groups comprise a hydrogen atom. The modified cellulose derivative required according to the present invention comprise a substituent at one or more of these positions in the polymer. Typically the modifying groups will be non-ionic or anionic groups, producing nonionically or anionically modified cellulose, respectively. Alternatively, the modified cellulose derivative may be provided by other beta-1,4-linked polysaccharides such as xyloglucan (e.g. derived from Tamarind seed gum), glucomannan (e.g. Konjac glucomannan), galactomannan (e.g. derived from guar gum or locust bean gum), side-chain branched galactomannan (e.g. Xanthan gum), chitosan or a chitosan salt. Derivatives of starch, an alpha-1,4-linked polysaccharide may also be present. The natural polysaccharides, whether beta-1,4 or alpha-1,4, can be modified with amines (primary, secondary, tertiary), amides, esters, ethers, urethanes, alcohols, carboxylic acids, tosylates, sulfonates, sulfates, nitrates, phosphates and mixtures thereof. Examples of suitable derivatives are given in WO 06/117071 (Unilever), such as carboxymethyl Locust Bean gum and Locust Bean gum ethyl sulfonate.

Preferred are anionically modified cellulose derivatives such as carboxymethyl cellulose.

COMPOSITIONS

[0011] The compositions of the present invention typically may contain from 0.00002% to 0.15%, from 0.00005% to 0.12%, or even from 0.0002% to 0.02% or even 0.005% to 0.025% by weight of pure enzyme, of one or more endoglu-canase(s). The balance of any aspects of the aforementioned cleaning compositions is made up of cellulose derivative and one or more adjunct materials.

SUITABLE ENDOGLUCANASE

[0012] The endoglucanase to be incorporated into the detergent composition of the present invention is one or more bacterial alkaline enzyme(s) exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4).

[0013] As used herein, the term "alkaline endoglucanase", shall mean an endoglucanase having an optimum pH above 7 and retaining greater than 70% of its optimal activity at pH 10.

[0014] Preferably, the endoglucanase is a bacterial polypeptide endogenous to a member of the genus Bacillus. More preferably, the alkaline enzyme exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4), is a polypeptide containing (i) at least one family 17 carbohydrate binding module (Family 17 CBM) and/or (ii) at least one family 28 carbohydrate binding module (Family 28 CBM). Please refer for example to: Current Opinion in Structural Biology, 2001, 593-600 by Y. Bourne and B. Henrissat in their article entitled: "Glycoside hydrolases and glycosyltransferases: families and functional modules" for the definition and classification of CBMs. Please refer further to Biochemical Journal, 2002, v361,35-40 by A.B. Boraston et al in their article entitled: "Identification and glucan-binding properties of a new carbohydrate-binding module family" for the properties of the family 17 and 28 CBM’s.

[0015] In a more preferred embodiment, said enzyme comprises a polypeptide (or variant thereof) endogenous to one of the following Bacillus species:

[0016] Suitable endoglucanases for the compositions of the present invention are: 1 ) An enzyme exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4), which has a sequence of at least 90%, preferably 94%, more preferably 97% and even more preferably 99%, 100% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:1 (Corresponding to SEQ ID NO:2 in W002/099091); or a fragment thereof that has endo-beta-1,4-glucanase activity, when identity is determined by GAP provided in the GCG program using a GAP creation penalty of 3.0 and GAP extension penalty of 0.1. The enzyme and the corresponding method of production is described extensively in patent application W002/099091 published by Novozymes A/S on December 12, 2002. Please refer to the detailed description pages 4 to 17 and to the examples page 20 to page 26. One of such enzyme is commercially available under the tradename Celluclean™ by Novozymes A/S. GCG refers to the sequence analysis software package provided by Accelrys, San Diego, CA, USA. This incorporates a program called GAP which uses the algorithm of Needleman and Wunsch to find the alignment of two complete sequences that maximises the number of matches and minimises the number of gaps. 2) Also suitable are the alkaline endoglucanase enzymes described in EP 1 350 843A published by Kao corporation on October 8, 2003. Please refer to the detailed description [0011] to [0039] and examples 1 to 4 [0067] to [0077] for a detailed description of the enzymes and its production. The alkaline cellulase variants are obtained by substituting the amino acid residue of a cellulase having an amino acid sequence exhibiting at Ieast90%, preferably 95%, more preferably 98% and even 100% identity with the amino acid sequence represented by SEQ. ID NO:2 (Corresponding to SEQ. ID NO:1 in EP 1 350 843 on pages 11-13) at (a) position 10, (b) position 16, (c) position 22, (d) position 33, (e) position 39, (f) position 76, (g) position 109, (h) position 242, (i) position 263, (j) position 308, (k) position 462, (1) position 466, (m) position 468, (n) position 552, (o) position 564, or (p) position 608 in SEQ ID NO:2 or at a position corresponding thereto with another amino acid residue

Examples of the "alkaline cellulase having the amino acid sequence represented by SEQ. ID NO:2" include Eg1-237 [derived from Bacillus sp. strain KSM-S237 (FERM BP-7875), Hakamada, et al., Biosci. Biotechnol. Biochem., 64, 2281-2289, 2000], Examples of the "alkaline cellulase having an amino acid sequence exhibiting at least 90% homology with the amino acid sequence represented by SEQ. ID NO:2" include alkaline cellulases having an amino acid sequence exhibiting preferably at least 95% homology, more preferably at least 98% homology, with the amino acid sequence represented by SEQ. ID NO:2. Specific examples include alkaline cellulase derived from Bacillus sp. strain 1139 (Eg1 -1139) (Fukumori, et al., J. Gen. Microbiol., 132, 2329-2335) (91.4% homology), alkaline cellulases derived from Bacillus sp. strain KSM-64 (Eg1-64) (Sumitomo, et al., Biosci. Biotechnol. Biochem., 56, 872-877, 1992) (homology: 91.9%), and cellulase derived from Bacillus sp. strain KSM-N131 (Eg1-N131b) (Japanese Patent Application No. 2000-47237) (homology: 95.0%).

The amino acid is preferably substituted by: glutamine, alanine, proline or methionine, especially glutamine is preferred at position (a), asparagine or arginine, especially asparagine is preferred at position (b), proline is preferred at position (c), histidine is preferred at position (d), alanine, threonine or tyrosine, especially alanine is preferred at position (e), histidine, methionine, valine, threonine or alanine, especially histidine is preferred at position (f), isoleucine, leucine, serine or valine, especially isoleucine is preferred at position (g), alanine, phenylalanine, valine, serine, aspartic acid, glutamic acid, leucine, isoleucine, tyrosine, threonine, methionine or glycine, especially alanine, phenylalanine or serine is preferred at position (h), isoleucine, leucine, proline or valine, especially isoleucine is preferred at position (i), alanine, serine, glycine or valine, especially alanine is preferred at position (j), threonine, leucine, phenylalanine or arginine, especially threonine is preferred at position (k), leucine, alanine or serine, especially leucine is preferred at position (1), alanine, aspartic acid, glycine or lysine, especially alanine is preferred at position (m), methionine is preferred at position (n), valine, threonine or leucine, especially valine is preferred at position (o) and isoleucine or arginine, especially isoleucine is preferred at position (p).

The "amino acid residue at a position corresponding thereto" can be identified by comparing amino acid sequences by using known algorithm, for example, that of Lipman-Pearson’s method, and giving a maximum similarity score to the multiple regions of similarity in the amino acid sequence of each alkaline cellulase. The position of the homologous amino acid residue in the sequence of each cellulase can be determined, irrespective of insertion or depletion existing in the amino acid sequence, by aligning the amino acid sequence of the cellulase in such manner (Fig. 1 of EP 1 350 843). It is presumed that the homologous position exists at the three-dimensionally same position and it brings about similar effects with regard to a specific function of the target cellulase.

With regard to another alkaline cellulase having an amino acid sequence exhibiting at least 90% homology with SEQ. ID NO:2, specific examples of the positions corresponding to (a) position 10, (b), position 16, (c) position 22, (d) position 33, (e) position 39, (f) position 76, (g) position 109, (h) position 242, (i) position 263, (j) position 308, (k) position 462, (1) position 466, (m) position 468, (n) position 552, (o) position 564 and (p) position 608 of the alkaline cellulase (Eg1-237) represented by SEQ. ID NO: 2 and amino acid residues at these positions will be shown below:

(continued)

3) Also suitable is the alkaline cellulase K described in EP 265 832A published by Kao on May 4, 1988. Please refer to the description page 4, line 35 to page 12, line 22 and examples 1 and 2 on page 19 for a detailed description of the enzyme and its production. The alkaline cellulase K has the following physical and chemical properties: • (1) Activity: Having a Cx enzymatic activity of acting on carboxymethyl cellulose along with a weak C1 enzymatic activity and a weak beta-glucoxidase activity; • (2) Specificity on Substrates: Acting on carboxymethyl cellulose(CMC), crystalline cellulose, Avicell, cellobiose, and p-nitrophenyl cellobioside(PNPC); • (3) Having a working pH in the range of 4 to 12 and an optimum pH in the range of 9 to 10; • (4) Having stable pH values of 4.5 to 10.5 and 6.8 to 10 when allowed to stand at 40°C for 10 minutes and 30 minutes, respectively; • (5) Working in a wide temperature range of from 10 to 65°C with an optimum temperature being recognized at about 40°C; • (6) Influences of chelating agents: The activity not impeded with ethylenediamine tetraacetic acid (EDTA), ethyl-eneglycol-bis-(ß-aminoethylether) Ν,Ν,Ν’,Ν''-tetraaceticacid (EGTA), N,N-bis(carboxymethyl)glycine(nitrilotriacetic acid) (NTA), sodium tripolyphosphate (STPP) and zeolite; • (7) Influences of surface active agents: Undergoing little inhibition of activity by means of surface active agents such as sodium linear alkylbenzenesulfonates (LAS), sodium alkylsulfates (AS), sodium polyoxyethylene alkylsulfates (ES), sodium alpha-olefinsulfonates (AOS), sodium alpha-sulfonated aliphatic acid esters (alpha-SFE), sodium alkylsulfonates (SAS), polyoxyethylene secondary alkyl ethers, fatty acid salts (sodium salts), and dimethyldialky-lammonium chloride; • (8) Having a strong resistance to proteinases; and • (9) Molecular weight (determined by gel chromatography): Having a maximum peak at 180,000 ± 10,000.

Preferably such enzyme is obtained by isolation from a culture product of Bacillus sp KSM-635.

Cellulase K is commercially available by the Kao Corporation: e.g. the cellulase preparation Eg-X known as KAC® being a mixture of E-H and E-L both from Bacillus sp. KSM-635 bacterium. Cellulases E-H and E-L have been described in S. Ito, Extremophiles, 1997, v1,61-66 and in S. Ito et al, Agric Biol Chem, 1989, v53, 1275-1278. 4) The alkaline bacterial endoglucanases described in EP271 004A published by Kao on June 15,1988 are also suitable for the purpose of the present invention. Please refer to the description page 9, line 15 to page 23, line 17 and page 31, line 1 to page 33, line 17 for a detailed description of the enzymes and its production. Those are:

Alkaline Cellulase K-534 from KSM 534, FERM BP 1508,

Alkaline Cellulase K-539 from KSM 539, FERM BP 1509,

Alkaline Cellulase K-577 from KSM 577, FERM BP 1510,

Alkaline Cellulase K-521 from KSM 521, FERM BP 1507,

Alkaline Cellulase K-580 from KSM 580, FERM BP 1511,

Alkaline Cellulase K-588 from KSM 588, FERM BP 1513,

Alkaline Cellulase K-597 from KSM 597, FERM BP 1514,

Alkaline Cellulase K-522 from KSM 522, FERM BP 1512,

Alkaline Cellulase E-ll from KSM 522, FERM BP 1512,

Alkaline Cellulase E-Ill from KSM 522, FERM BP 1512.

Alkaline Cellulase K-344 from KSM 344, FERM BP 1506, and Alkaline Cellulase K-425 from KSM 425, FERM BP 1505. 5) Finally, the alkaline endoglucanases derived from Bacillus species KSM-N described in JP2005287441 A, published by Kao on the October 20th, 2005, are also suitable for the purpose of the present invention. Please refer to the description page 4, line 39 to page 10, line 14 for a detailed description of the enzymes and its production. Examples of such alkaline endoglucanases are:

Alkaline Cellulase Egl-546H from Bacillus sp. KSM-N546 Alkaline Cellulase Egl-115 from Bacillus sp. KSM-N115 Alkaline Cellulase Egl-145 from Bacillus sp. KSM-N145 Alkaline Cellulase Egl-659 from Bacillus sp.KSM-N659 Alkaline Cellulase Egl-640 from Bacillus sp.KSM-N440

Also encompassed in the present invention are variants of the above described enzymes obtained by various techniques known by persons skilled in the art such as directed evolution.

MODIFIED CELLULOSE DERIVATIVE

[0017] The modified cellulose derivative required in the present invention comprises a polymer comprising a cellulose backbone. The cellulose may be anionically or nonionically modified, preferably anionically modified. A monomer of cellulose is shown below.

[0018] R1, R2 and R3 show the positions in the cellulose monomer available for substitution. In the natural cellulose polymer, these groups comprise a hydrogen atom. The modified cellulose derivative useful herein comprises substituents at one or more of these positions. For example for anionic substitution, one or more of these positions in the polymer are substituted with an anionic group for example, one of the following anionic groups, in its acid or salt form, preferably sodium (given here) or potassium salt form. -L-C02Na -L-SOsNa -P03Na -S03Na [0019] Wherein: L is C.|_e alkyl, more preferably C^ alkyl [0020] The anionically modified cellulose derivative may also comprise non-ionic substituent groups in which one or more of positions R1, R2 and R3 may be substituted with nonionic groups, for example,

-A

-L-OH

-L-CN

-C(=0)A -C(=0)NH2

-C(=0)NHA

-C(=0)N(A)B

-C(=0)0A

-(CH2CH2CH20)nZ

-(CH2CH20)nZ

-(CH2CH(CH3)0)nZ

-(CH20)nZ

[0021] Wherein: A and B are alkyl L is C-|_g alkyl n = 1 to 100 Z is H or C-|_g alkyl [0022] Non-limiting examples of suitable modified cellulose derivatives are the sodium or potassium salts of car-boxymethyl cellulose, carboxyethyl cellulose, sulfoethyl cellulose, sulfopropyl cellulose, cellulose sulfate, phosphorylated cellulose, carboxymethyl hydroxyethyl cellulose, carboxymethyl hydroxypropyl cellulose, sulfoethyl hydroxyethyl cellulose, sulfoethyl hydroxypropyl cellulose, carboxymethyl methyl hydroxyethyl cellulose, carboxymethyl methyl cellulose, sulfoethyl methyl hydroxyethyl cellulose, sulfoethyl methyl cellulose, carboxymethyl ethyl hydroxyethyl cellulose, carboxymethyl ethyl cellulose, sulfoethyl ethyl hydroxyethyl cellulose, sulfoethyl ethyl cellulose, carboxymethyl methyl hydroxypropyl cellulose, sulfoethyl methyl hydroxypropyl cellulose, carboxymethyl dodecyl cellulose, carboxymethyl do-decoyl cellulose, carboxymethyl cyanoethyl cellulose and sulfoethyl cyanoethyl cellulose,

Nonionically modified cellulose [0023] The modified cellulose derivative may be provided by a nonionically modified cellulose derivative instead of or in addition to the anionically modified cellulose polymer. Examples of nonionically modified cellulose polymers include methyl cellulose, ethyl cellulose, propyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, methyl hydroxyethyl cellulose, ethyl hydroxyethyl cellulose, dodecyl hydroxyethyl cellulose, ethyl hydroxypropyl cellulose, cellulose acetate, methyl hydroxypropyl cellulose, methyl ethyl hydroxyethyl cellulose, butyl glycidyl ether-hydroxyethyl cellulose, and lauryl glycidyl ether-hydroxyethyl cellulose [0024] Specific examples include Finnfix BDA(from Noviant), Tylose CR1500 G2 (from Clariant), Carbose codes D65, D72, LT-30 and LT-20 (from Penn Carbose); hydrophobically modified cellulose derivatives for example as described in W099/61479 (Noviant); cellulose derivatives modified with polyethylene glycol, for example as described in DE102004063766 [0025] Particularly preferred modified cellulose derivatives have a weight average molecular mass of at least 20 000 or at least 50 000 or even at least 100 000 or even at least 150 000 kDaltons. The weight average molecular mass of the modified cellulose derivative will generally be no greater than 500 000, or no greater than 300 000 or no greater than 250 OOOkDa. Preferred degrees of substitution (DS) are from 0.3, or 0.4, or 0.45 up to for example 0.7 or even 0.8 or even 0.9. Particularly preferred are modified methyl celluloses, such as CMC, with such molecularweights and/or degrees of substitution and/or levels as described herein.

[0026] The level of modified cellulose derivative in the detergent compositions of the invention is typically from at least 0.005 or 0.01 wt% or 0.02 or at least 0.05wt% or even at least 0.1 wt% based on the total weight of detergent composition. Typically, the levels will be no greater than 5% by weight or even no greater than 2% by weight or even no greater than 1.5% by weight of the detergent composition. In a particularly preferred embodiment of the invention the weight ratio of modified cellulose derivative to active cellulase enzyme protein is from 1:1 to 10000:1, preferably 20:1 to 1000:1, most preferably 30:1 to 800:1.

[0027] Cellulose derivatives such as methyl celluloses have been incorporated into detergent compositions for many years. They deposit onto cotton fabric surfaces to form a negatively charged soil-repellant layer, which repels soils reducing deposition onto a fabric surface. The present inventors have found that cellulose derivatives having a much lower molecular weight than is traditionally used can provide further surprising benefits as they act as anti-redeposition aids by suspending soils in the wash liquor. These cellulose derivatives may be formed in situ by reaction of specific cellulose agent pre-cursors.

[0028] The modified cellulose derivative may be added as a dry particulate component comprising for example greater than 50 % or even greater than 60 % or 70 % or 80% by weight, up to 100 % by weight modified cellulose derivative. The modified cellulose derivative may be incorporated into the detergent compositions of the invention as part of a processed particle formed by a conventional detergent particle-making process, such as spray-drying, agglomeration or extrusion. In such cases, the amount of modified cellulose derivative in such particle will be at least 0.1 % or 0.5 or 1 % by weight and is likely to be less than 70% and more likely, less than 60 % or 50 %, 40%, 30% or even less than 20 % or 10% by weight of the processed particle. Introducing the modified cellulose derivative as part of a processed detergent particle may be particularly preferred especially for detergent compositions containing low levels of phosphate and/or zeolite builders; for example less than 15% by weight of the total detergent composition or even less than 14% or 12 % or 10 % or 8 % down to 0 % by weight phosphate and/or zeolite builders. This may be preferred as it may promote uniform distribution of the cellulose throughtout the wash liquor on addition of the detergent composition to water, by helping solubility of the cellulose derivative. Where the modified cellulose derivative is present in a processed detergent particle, the processed detergent particle may comprise any other conventional detergent ingredients or components thereof such as any of the adjunct materials described below or, for example as described in JP 2002 265999 (Kao) or in any of the processes described below under the sub-heading "Processes of Making Compositions". In particular such particles may comprise at least 1, or at least 5 or 10 % by weight up to 15 or 20 or 30 % by weight polymeric polycarboxylate polymer such as acrylic acid and/or maleic acid-based homo- or co- polymers (e.g. Sokalan polymers from BASF), based on the weight of the processed particle. The processed particles may comprise anionic, non-ionic, cationic, zwitterionic and/or amphoteric surfactants or mixtures thereof. Amounts may be form 1 to 70 % by weight, or 2 to 60% or from5 to 850 % by weight based on the total weight of the processed particle. For example, processed particles may comprise non-ionic surfactant optionally in combination with anionic and/or cationic surfactants. Suitable surfactants are described in the "Surfactants" section of the description. In particular, suitable non-ionic surfactants include alkyl alkoxylated surfactant, e.g ethoxylated surfactants having a degree of alkoxylation from 3 to 20 or even higher such as 20 to 50.

Processed particles may comprise sodium silicate (especially 1 to 2 ratio) in amounts from 1 to 30 % by weight or 2 to 25 % by weight or from 5 to 20 % by weight.

Preferred compositions according to the invention comprise polymeric polycarboxylate polymers and in such an amount that the weight ratio of polymeric polycarboxylate to modified cellulose derivative is at least 2:1, more preferably at least 2.5:1 and most preferably at least 3:1 or even 4:1 or 5:1. Such ratios may also be preferred in the processed particles discussed above, where polymeric polycarboxylate is present.

The bulk density of the composition of the invention and/or more specifically the modified cellulose derivative-containing particles is typically at least 450 g/l or at least 550g/l or 650g/l or at least 700g/l, up to 1500g/l. Bulk density is measured by means of a simple funnel and cup device consisting of a conical funnel mounted rigidly on a base and provided with a flap valve at its lower extremity to allow the contents of the funnel to be emptied into an axially aligned cylindrical cup disposed below the funnel. The funnel is 130 mm high and has internal diameters of 130 mm and 40 mm at its respective upper and lower extremities. It is mounted so that the lower extremity is 140 mm above the upper surface of the base. The cup has an overall height of 90 mm, an internal height of 87 mm and an internal diameter of 84 mm. Its nominal volume is 500 ml. To carry out a measurement, the funnel is filled with powder by hand pouring, the flap valve is opened and powder is allowed to overfill the cup. The filled cup is removed from the frame and excess powder is removed from the cup by passing a straight edged implement eg. a knife, across its upper edge. The filled cup is then weighed and the value obtained for the weight of powder doubled to provide a bulk density of g/litre. Replicate measurements are made and an average of three results provides the bulk density.

[0029] The present inventors have further provided detergent compositions which provide soil suspension properties. In accordance with a further embodiment of the invention, there is therefore provided a detergent composition comprising oligosaccharides having a weight average molecular mass of less than 20 000 kDa, such oligosaccharide being obtainable by reaction of an enzyme as defined above with an anionically modified cellulose having an average molecular weight from 30 000 to 500 000 kDa. In a further embodiment of said invention, there is provided an aqueous wash liquor comprising a detergent composition wherein the oligosaccharide is comprised in amounts from 0.5ppm to 1000 ppm, or from 0.8 to 1500 ppm or from 1.0 to 1000ppm.

In accordance with a further embodiment of the invention, there is provided use of oligosaccharide having a weight average molecular mass of less than 20 000 kDa, such oligosaccharide being obtainable by reaction of an enzyme as described above, with an anionically or nonionically, preferably anionically modified cellulose derivative having a weight average molecular mass from 30 000 to 500 000 kDa, for preparation of a detergent composition, for soil suspension. In accordance with a further aspect of the invention there is also provided a detergent composition comprising an enzyme as described above and at least 2 wt%, or even at least 5 wt%, 10 wt%, 15, 20 wt% or higher for example up to 50 wt% or 40 wt% or 30 wt% or 25 wt% , of a phosphate builder salt, at least 25, or 30 or 40 or 45 or 50 or even 55 wt% up to 100 wt% or 90 wt% or 80 wt% of said phosphate builder comprising pyrophosphate builder.

This pyrophosphate builder may be formed in situ by spray drying a composition comprising sodium or other salt of tri polyphosphate or acid form in a spray drying process in which the temperature and/or air flow and/or other chemical constituents in the spray drying slurry are controlled to provide the desired reaction of the tripolyphosphate to pyrophosphate salt. The process may be operated for example as described in W003/091378 or US4310431.

Adjunct Materials [0030] While not essential for the purposes of the present invention, the non-limiting list of adjuncts illustrated hereinafter are suitable for use in the instant compositions and may be desirably incorporated in certain embodiments of the invention, for example to assist or enhance cleaning performance, for treatment of the substrate to be cleaned, or to modify the aesthetics of the cleaning composition as is the case with perfumes, colorants, dyes or the like. The 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. Suitable adjunct materials include, but are not limited to, surfactants, builders, chelating agents, dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabricsofteners, carriers, hydrotropes, processing aids, solvents and/or pigments. In addition to the disclosure below, suitable examples of such other adjuncts and levels of use are found in U.S. Patent Nos. 5,576,282, 6,306,812 B1 and 6,326,348 B1 that are incorporated by reference. When one or more adjuncts are present, such one or more adjuncts may be present as detailed below:

Bleaching Agents - The cleaning compositions of the present invention may comprise one or more bleaching agents. Suitable bleaching agents other than bleaching catalysts include other photobleaches, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, pre-formed peracids and mixtures thereof. In general, when a bleaching agent is used, the compositions of the present invention may comprise from about 0.1 % to about 50% or even from about 0.1 % to about 25% bleaching agent by weight of the subject cleaning composition. Examples of suitable bleaching agents include: (1) other photobleaches for example Vitamin K3; (2) preformed peracids: Suitable preformed peracids include, but are not limited to, compounds selected from the group consisting of percarboxylic acids and salts, percarbonic acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts, for example, Oxone ®, and mixtures thereof. Suitable percarboxylic acids include hydrophobic and hydrophilic peracids having the formula R-(C=0)0-0-M wherein R is an alkyl group, optionally branched, having, when the peracid is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when the peracid is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and M is a counterion, for example, sodium, potassium or hydrogen; (3) sources of hydrogen peroxide, for example, inorganic perhydrate salts, including alkali metal salts such as sodium salts of perborate (usually mono-ortetra-hydrate), percarbonate, persulphate, perphosphate, persilicate salts and mixtures thereof. In one aspect of the invention the inorganic perhydrate salts are selected from the group consisting of sodium salts of perborate, percarbonate and mixtures thereof. When employed, inorganic perhydrate salts are typically present in amounts of from 0.05 to 40 wt%, or 1 to 30 wt% of the overall composition and are typically incorporated into such compositions as a crystalline solid that may be coated. Suitable coatings include, inorganic salts such as alkali metal silicate, carbonate or borate salts or mixtures thereof, or organic materials such as water-soluble or dispersible polymers, waxes, oils or fatty soaps; and (4) bleach activators having R-(C=0)-L wherein R is an alkyl group, optionally branched, having, when the bleach activator is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when the bleach activator is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and L is leaving group. Examples of suitable leaving groups are benzoic acid and derivatives thereof - especially benzene sulphonate. Suitable bleach activators include dodecanoyl oxybenzene sulphonate, decanoyl oxybenzene sulphonate, de-canoyl oxybenzoic acid or salts thereof, 3,5,5-trimethyl hexanoyloxybenzene sulphonate, tetraacetyl ethylene diamine (TAED) and nonanoyloxybenzene sulphonate (NOBS). Suitable bleach activators are also disclosed in WO 98/17767. While any suitable bleach activator may be employed, in one aspect of the invention the subject cleaning composition may comprise NOBS, TAED or mixtures thereof.

[0031] When present, the peracid and/or bleach activator is generally present in the composition in an amount of from about 0.1 to ab out 60 wt%, from about 0.5 to about 40 wt% or even from about 0.6 to about 10 wt% based on the composition. One or more hydrophobic peracids or precursors thereof may be used in combination with one or more hydrophilic peracid or precursor thereof.

[0032] The amounts of hydrogen peroxide source and peracid or bleach activator may be selected such that the molar ratio of available oxygen (from the peroxide source) to peracid is from 1:1 to 35:1, or even 2:1 to 10:1.

[0033] Surfactants - The cleaning compositions according to the present invention may comprise a surfactant or surfactant system wherein the surfactant can be selected from nonionic surfactants, anionic surfactants, cationic surfactants, ampholytic surfactants, zwitterionic surfactants, semi-polar nonionic surfactants and mixtures thereof. When present, surfactant is typically present at a level of from about 0.1 % to about 60%, from about 1 % to about 50% or even from about 5% to about 40% by weight of the subject composition.

[0034] Builders - The cleaning compositions of the present invention may comprise one or more detergent builders or builder systems. When a builder is used, the subject composition will typically comprise at least about 1 %, from about 5% to about 60% or even from about 10% to about 40% builder by weight of the subject composition.

[0035] Builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates, alkali metal silicates, alkaline earth and alkali metal carbonates, aluminosilicate builders and polycarboxylate compounds, ether hydroxypolycarboxylates, copolymers of maleic anhydride with ethylene or vinyl methyl ether, 1, 3, 5-trihydroxy benzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid, the various alkali metal, ammonium and substituted ammonium salts of polyacetic acids such as ethylenediamine tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid, citric acid, oxydisuccinic acid, polymaleic acid, benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts thereof.

[0036] Chelating Agents - The cleaning compositions herein may contain a chelating agent. Suitable chelating agents include copper, iron and/or manganese chelating agents and mixtures thereof. When a chelating agent is used, the subject composition may comprise from about 0.005% to about 15% or even from about 3.0% to about 10% chelating agent by weight of the subject composition.

[0037] Dye Transfer Inhibiting Agents - The cleaning compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001% to about 10%, from about 0.01% to about 5% or even from about 0.1 % to about 3% by weight of the composition.

[0038] Fluorescent whitening agent - The cleaning compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent. Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulphonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulphonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4’-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2’-disulphonate, 4,4’-bis-(2,4-dianilino-s-triazin-6-ylamino) stilbene-2.2’-disulphonate, 4,4’-bis-(2-anilino-4(N-methyl-N-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2’-disulphonate, 4,4’-bis-(4-phenyl-2,1,3-triazol-2-yl)stilbene-2,2’-disulphonate, 4,4’-bis-(2-anilino-4(1-methyl-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2’-disulphonate and, 2-(stilbyl-4"-naptho-1 ,,2’:4,5)-1,2,3-trizole-2"-sulphonate.

Preferred fluorescent whitening agents are Tinopal® DMS and Tinopal® CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal® DMS is the disodium salt of 4,4’-bis-(2-morpholino-4 anilino-s-triazin-6-ylamino) stilbene disul-phonate. Tinopal® CBS is the disodium salt of 2,2’-bis-(phenyl-styryl) disulphonate.

[0039] Also preferred are fluorescent whitening agents of the structure:

wherein R1 and R2, together with the nitrogen atom linking them, form an unsubstituted or C1-C4 alkyl-substituted morpholino, piperidine or pyrrolidine ring, preferably a morpholino ring (commercially available as Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India)

Other fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines and the 7-alkylaminocoumarins.

[0040] Suitable fluorescent brightener levels include lower levels of from about 0.01, from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt %.

[0041] Fabric hueing agents- dyes or pigments which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions thus altering the tint of said fabric through absorption of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.l.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in W02005/03274,W02005/03275,W02005/03276 and co-pending European application noo6116780.5filed 7 July 2006.

[0042] Dispersants - The compositions of the present invention can also contain dispersants. Suitable water-soluble organic materials include 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.

[0043] Enzymes - In addition to the bacterial alkaline endoglucanase, the cleaning compositions can comprise one or more other enzymes which provide cleaning performance and/or fabric care benefits. Examples of suitable enzymes include, but are not limited to, hemicellulases, peroxidases, proteases, other cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxi-dases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, ß-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, and amylases, or mixtures thereof. In a preferred embodiment, the compositions of the present invention will further comprise a lipase, for further improved cleaning and whitening performance. Atypical combination is an enzyme cocktail that may comprise, for example, a protease and lipase in conjunction with amylase. When present in a cleaning composition, the aforementioned additional enzymes may be present at levels from about 0.00001% to about 2%, from about 0.0001% to about 1% or even from about 0.001% to about 0.5% enzyme protein by weight of the composition.

[0044] Enzyme Stabilizers - Enzymes for use in detergents can be stabilized by various techniques. The enzymes employed herein can be stabilized by the presence of water-soluble sources of calcium and/or magnesium ions in the finished compositions that provide such ions to the enzymes. In case of aqueous compositions comprising protease, a reversible protease inhibitor, such as a boron compound, can be added to further improve stability.

[0045] Catalytic Metal Complexes - Applicants’ cleaning compositions may include catalytic metal complexes. One type of metal-containing bleach catalyst is a catalyst system comprising a transition metal cation of defined bleach catalytic activity, such as copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations, an auxiliary metal cation having little or no bleach catalytic activity, such as zinc or aluminum cations, and a sequestrate having defined stability constants for the catalytic and auxiliary metal cations, particularly ethylenediaminetetraacetic acid, ethylenediaminetetra(methylenephosphonic acid) and water-soluble salts thereof. Such catalysts are disclosed in U.S. 4,430,243.

[0046] If desired, the compositions herein can be catalyzed by means of a manganese compound. Such compounds and levels of use are well known in the art and include, for example, the manganese-based catalysts disclosed in U.S. 5,576,282.

[0047] Cobalt bleach catalysts useful herein are known, and are described, for example, in U.S. 5,597,936; U.S. 5,595,967. Such cobalt catalysts are readily prepared by known procedures, such as taughtfor example in U.S. 5,597,936, and U.S. 5,595,967.

[0048] Compositions herein may also suitably include a transition metal complex of ligands such as bispidones (WO 05/042532 A1) and/or macropolycyclic rigid ligands - abbreviated as "MRLs". As a practical matter, and not by way of limitation, the compositions and processes herein can be adjusted to provide on the order of at least one part per hundred million of the active MRL species in the aqueous washing medium, and will typically provide from about 0.005 ppm to about 25 ppm, from about 0.05 ppm to about 10 ppm, or even from about 0.1 ppm to about 5 ppm, of the MRL in the wash liquor.

[0049] Suitable transition-metals in the instant transition-metal bleach catalyst include, for example, manganese, iron and chromium. Suitable MRLs include 5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane.

[0050] Suitable transition metal MRLs are readily prepared by known procedures, such as taught for example in WO 00/32601, and U.S. 6,225,464.

[0051] Solvents - Suitable solvents include water and other solvents such as lipophilic fluids. Examples of suitable lipophilic fluids include siloxanes, other silicones, hydrocarbons, glycol ethers, glycerine derivatives such as glycerine ethers, periluorinated amines, perfluorinated and hydrofluoroether solvents, low-volatility nonfluorinated organic solvents, diol solvents, other environmentally-friendly solvents and mixtures thereof.

[0052] Softening system - the compositions of the invention may comprise a softening agent such as clay and optionally also with flocculants and enzymes; optionally for softening through the wash.

Processes of Making Compositions [0053] The compositions of the present invention can be formulated into any suitable form and prepared by any process chosen by the formulator, non-limiting examples of which are described in Applicants’ examples and in U.S. 4,990,280; U.S. 20030087791A1; U.S. 20030087790A1 ; U.S. 20050003983A1 ; U.S. 20040048764A1 ; U.S. 4,762,636; U.S. 6,291,412; U.S. 20050227891A1 ; EP 1070115A2; U.S. 5,879,584; U.S. 5,691,297; U.S. 5,574,005; U.S. 5,569,645; U.S. 5,565,422; U.S. 5,516,448; U.S. 5,489,392; U.S. 5,486,303 all of which are incorporated herein by reference.

Method of Use [0054] The present invention includes a method for laundering a fabric. The method comprises the steps of contacting a fabric to be laundered with a said cleaning laundry solution comprising at least one embodiment of Applicants’ cleaning composition, cleaning additive or mixture thereof. The fabric may comprise most any fabric capable of being laundered in normal consumer use conditions. The solution preferably has a pH of from about 8 to about 10.5. The compositions may be employed at concentrations of from about 500 ppm to about 15,000 ppm in solution. The water temperatures typically range from about 5 °C to about 90 °C. The water to fabric ratio is typically from about 1:1 to about 30:1.

EXAMPLES

[0055] Unless otherwise indicated, materials can be obtained from Aldrich, P.O. Box 2060, Milwaukee, Wl 53201, USA. (a) Examples 1-6 [0056] Granular laundry detergent compositions designed for handwashing or top-loading washing machines.

(continued)

Examples 7-12 [0057] Granular laundry detergent compositions designed for front-loading automatic washing machines.

(continued)

[0058] Any of the above compositions is used to launder fabrics at a concentration of 7000 to 10000 ppm in water, 20-90 °C, and a 5:1 watencloth ratio. The typical pH is about 10.

[0059] The ratio of CMC to active enzyme protein in the above formulations is shown in the table below:

Raw Materials and Notes For Composition Examples 1-12 [0060]

Linear alkylbenzenesulfonate having an average aliphatic carbon chain length C^-C^ supplied by Stepan, North-field, Illinois, USA

C12_14 Dimethylhydroxyethyl ammonium chloride, supplied by Clariant GmbH, Sulzbach, Germany AE3S is C12_15 alkyl ethoxy (3) sulfate supplied by Stepan, Northfield, Illinois, USA

AE7 is C12_15 alcohol ethoxylate, with an average degree of ethoxylation of 7, supplied by Huntsman, Salt Lake City, Utah, USA

Sodium tripolyphosphate is supplied by Rhodia, Paris, France Zeolite A was supplied by Industrial Zeolite (UK) Ltd, Grays, Essex, UK 1.6R Silicate was supplied by Koma, Nestemica, Czech Republic Sodium Carbonate was supplied by Solvay, Houston, Texas, USA Polyacrylate MW 4500 is supplied by BASF, Ludwigshafen, Germany

Carboxy Methyl Cellulose is Finnfix® BDA supplied by the Noviant division of CPKelco, Arnhem, Netherlands Savinase®, Natalase®, Lipex®, Termamyl®, Mannaway®, Celluclean® supplied by Novozymes, Bagsvaerd, Denmark

Protease (examples 7-12) described in patent application US 6312936B1 was supplied by Genencor International, Palo Alto, California, USA

Fluorescent Brightener 1 is Tinopal® AMS, Fluorescent Brightener 2 is Tinopal® CBS-X. Sulphonated zinc phthalo-cyanine supplied by Ciba Specialty Chemicals, Basel, Switzerland

Diethylenetriamine pentacetic acid was supplied by Dow Chemical, Midland, Michigan, USA Sodium percarbonate

supplied by Solvay, Houston, Texas, USA

Sodium perborate was supplied by Degussa, Hanau, Germany NOBS is sodium nonanoyloxybenzenesulfonate, supplied by Eastman, Batesville, Arkansas, USA TAED is tetraacetylethylenediamine, supplied under the Peractive® brand name by Clariant GmbH, Sulzbach, Germany Soil release agent is Repel-o-tex® PF, supplied by Rhodia, Paris, France

Acrylic Acid/Maleic Acid Copolymer is molecular weight 70,000 and acrylate:maleate ratio 70:30, supplied by BASF, Ludwigshafen, Germany

Na salt of Ethylenediamine-N,N’-disuccinic acid, (S,S) isomer (EDDS) was supplied by Octel, Ellesmere Port, UK Hydroxyethane di phosphonate (HEDP) was supplied by Dow Chemical, Midland, Michigan, USA Suds suppressor agglomerate was supplied by Dow Corning, Midland, Michigan, USA

SEQUENCE LISTING

[0061] <110> The Procter &amp; Gamble Company <120> Detergent Compositions

<130> CM3146F <140> EP06124858.9 <141 > 2006-11-27 <150> EP06115574.3 <151 > 2006-06-16 <150> US60/819155 <151 > 2006-07-07 <150> EP06116784.7 <151 > 2006-07-07 <150> EP06116782.1 <151 > 2006-07-07 <150 EP06116780.5 <151 > 2006-07-07 <160>2 <170> Patentln version 3.3 <210> 1 <211> 773 <212> PRT <213> bacillus sp. <400> 1

Ala 61u Gly ash Thr Arg Glu Asp Asn Phe Lys His leu Leu Gly ash

1 5 ' 10 IS

Asp Asn Val Lvs Arg Pro Ser Glu Ala Gly Ala Leu Gin Leu Gin Glu 20 25 30

Val Asp Gly Gin Met Thr Leu Val Asp Gin His Gly Glu Lys lie Gin 35' 40 45

Leu Arg Gly Met Ser Thr His Gly Leu Gin Trp Phe Pro Glu île Leu 50 55 60

Asn Asp Asn Ala Tyr Lys Ala Lau Ala Asn Asp Trp Glu Ser Asn Met 65 70 75 80 lie Arg Leu Ala Met Tyr val Gly Glu Asn Gly Tyr Ala Ser Asn Pro 85 * 90 95

Glu Leu lie Lvs Ser Arg Val Ile Lys Gly Ile Asp Leu Ala île Glu 1Ö0 ' 105 ‘ " 110

Asn Aso Met Tyr val lia Val Asp Trp Hi s Val Hi s Ala Pro Gly Asp lis 120 125

Pro Aril Asp Pro val Tyr Ala Gly Ala tílu Asp Phe Phe Arg Asp lie 130 135 ' 140

Ala Ala Leu Tyr Pro Asn as« Pro His lie Ile Tyr Glu Leu Ala Asn 143 ISO 155 160

Glu Pro Ser ser Asn Asn Asn Gly Gly Ala Gly lie Pro Asn Asn Glu 165 17x0 175

Glu Gly Trp Asn Ala Val Lys Glu Tyr Ala Asp Pro lie val Glu Met 180 185 190

Leu Arg Asp Ser Gly Asn Ala Asp Asp Asn lie lie lie val Gly ser 195 200 205

Pro Asn Trp ser Gin Arg pro Asp leu Ala Ala Asp Asn Pro lie Asn 210 ' 215 220

Asp His His Thr Met Tyr Thr val His Phe Tyr Thr Gly ser His Ala 225 230 235 240

Ala ser ihr Glu Ser Tyr pro Prö Glu Thr Pro Asn Ser Glu Arg cly 245 250 255

Asn val Met $er Asn Thr Arg Tyr Ala Leu Glu Asn Gly Val Ala val 260 265 270

Phe Ala Thr Glu Trp Gly Thr ser Gin Ala Asn Gly Asp Gly Gly Pro 275 280 285

Tyr Phe Asp Glu Ala Asp val Trp lie Glu Phe Leu Asn Glu Asn Asn 290 295 300 lie Ser Trp Ala Asn Trp ser Leu Thr Asn Lys Asn Glu val Ser Gly 305 310 315 320

Ala Phe Thr Pro Phe Glu Leu Gly Lys Ser Asn Ala Thr Asn Leu Asp 325 330 335

Pro Gly Pro Aso His val Trp Ala Pro Glu Glu Leu Ser Leu Ser Gly 340 345 350

Glu Tyr val Arg Ala Arg île Lys Gly Val Asn Tyr Glu Pro lie Asp '355 " 360 365

Arg Thr Lys Tyr Thr Lys val Leu Trp Asp Phe Asn Asp Gly Thr Lys 370 ' 375 380

Gin Gly phe Gly val Asn ser Asp Ser Pro Asn Lys Glu Leu lie Ala 385 ' 390 395 400 val Asp Assi Glu Asn Asn Tbr l. eu Lys val ser Gl y Leu Asp val Ser 405 410 415

Asn Asp val ser Asp Gly Asn Phe Trp Ala Asn Ala Arq Leu Ser Ala 420 42S 430

Asp Gly Trp Gly lys Ser Val Asp Ile Leu Gly Ala Glu Lvs Leu Thr 435 440 445 '

Met As}3 Val Ile Val Asp Glu Pro Thr Thr val Ala île Ala Ala île 450 455 460

Pro Gin ser ser Lys Ser Gly Trp Ala Asn Pro Glu Arg Ala val Arc 465 470 475 480 val Asn Ala Glu Asp Phe val Gin Gin Thr Asp Gly Lys Tyr Lys Ala 485 490 495

Gly Leu Thr île Thr Gly Glu Asp Ala Pro Asn Leu Lys Asn Ile Ala 500 505 510

Phe ni s Glu Glu Asp Asn Asn Met Asn Asn île île Lêu Phe val Glv 515 520 525

Thr Asp Ala Alá A$p Val île Tyr Leu Asp Asn île Lys Val île Gly 530 535 540

Thr Glu val Glu île Pro val val Hi s Asp Pro lys Gly Glu Ala val 545 550 555 560 s.eu Pro ser val Phe Glu Asp Gly Thr Arg Gin Gly Trp Asp Trp Ala 56$ 570 575

Glv Glu ser Gly Val Lys Thr Ala Leu Thr île Glu Glu Aîa Asn Gly 580 585 590 ser Asn Ala Leu Ser Trp Glu Phe Gly Tyr pro Glu val Lys Pro ser ' 595 ' SOÖ 605 asp Asn Trp Ala Thr Ala Pro Arg Leu Asp phe Trp Lys ser Asp leu 610 61.5 620 val Ara Glv Glu Asn asp Tyr Val Ala Phe Asp Phe Tyr Leu Asp Pro 625 630 635 640 val Arq Ala Thr 61 u Gly Ala Met Asn He Asn Leu val Phe Gin Pro 645 650 655 pro thr A^n Gly Tyr Trp val Gin Ala Pro Lys Thr Tyr Thr lie ash 660 665 670

Phë Asp Glu Leu Glu Glu Ala Asn Gin val As.it Gly Leu xyr Hfs Tyr Q7S 680 6S5

Glu val Lys lie Asn val Arg Asp île Thr Asn Ile Gin Asp Asp Thr 690 695 7ÖG Lëu Leu Arg Asn Met Met île Ile Phé Ala Asp val Glu Ser Asp çh| 7Ö5 710 71-5 7 lii

Ala Gly Ara val Phe val Asp Asn val Arg Phe Glu Gly Ala Ala Thr 725 730 735

Thr Glu Pro val Glu pro Glu Pro val Asp Pro Gly Glu Glu Thr Pro 740 745 /50 pro val ASP Glu lvs Glu Alá Lys Lys Glu Gin Lys Glu Ala Glu Lys 755 " 760 765

Glu Glu Lys Glu Glu 770

<210>2 <211> 824 <212> PRT <213> Bacillus sp. KSM-s237 <400 2

Met Met Leu Arg Lys Lvs Thr Lys Gin Leu Ile Ser ser île Leu Ile I * 5 ‘ 10 15

Leu Val I eu Leu Leu Ser Leu Phe Pro Ala Ala Leu Ala Ala Glu Gly 20 25 30

Asn ihr Arg Glu as» tón Phe Lys His Leu Leu Gly Asn Asp Asn val 35 40 45

Lys Arg Pro Ser Glu Ala Gly Ala Leu Gin Leu Gin Glu Val Asp Gly " SO 55 60

Gin Met Thr leu va1 asp Gin His Gly Glu Lys Ile Gin Leu Arg Gly 65 70 75 80

Met ser Thr His Glv ieu Gin Trp Phe Pro Glu Ile Leu Asn Asp Asn ' SS' 90 95

Ala Tÿr Lys Ala Leu ser Asn Asp Trp Asp ser Asn Met Ile Arg Leu 100 1Ö5 110

Ala Met Tyr val Glv Glu Asn Gly Tyr Ala Thr Asn Pro Glu Leu Ile 115 120 125

Lys Gin Arg Val île Asp Gly Ile Glu Leu Ala île Glu Asn Asp Met HO 135 140

Tyr val îl e Val Asp Trp His val Hi s Ala Pro Gly Asp Pro Arg Asp 145 150 155 ΙδΟ

Pro val Tyr Ala Glv Ala Lys Asp Phe Phe Arg Glu lie Ala Ala Leu 165 170 175

Tyr Pro Asn Asn pro His île Ile Tyr Glu Leu Ala Asn 6lu Pro *er 180 18 S 130

Ser Asn Asn Asn Glv cil y Ala Gly lie Pro Asn Asn Glu Glu 6ly Trp 195 ' 200 205 lys Ala Val Lys Glu Tyr Ala Asp Pro île val Glu Met Leu Arg Lys 210 215 220

Ser Gly Asn Ala Aso Asp Asn île Ile Ile Val Gly Ser Pro Asn Trp 225 ' 230 235 240

Ser Gin Arg Pro asb Leu Ala Ala Asp" Asn Pro Ile Asp asp His His 245 250 255

Thr Met Tyr Thr val His Phe Tyr Thr Gly Ser His Ala Ala Ser Thr 260 265 270

Glu Ser Tyr Pro Ser Glu Thr Pro Asn Ser Glu Arg Gly A$n Val Met 275 280 285

Ser Asn Thr Arq Tyr Ala Leu Glu Asn Gly Val Ala Val Phe Ala Thr 290 ' 295 300

Glu Tfó Gly Thr ser Gin Ala ser Gly Asp Gly Gly pro Tyr Phe Asp 305 ' 310 315 320

Glu Ala Asp val trp île Glu Phe Leu Asn Glu Asn Asn Ile Ser Trp 325 330 335

Ala Asn Trp ser Leu Thr Asn Lys Asn Glu val Ser Gly Ala Phe Thr 340 345 350 pro Phe Glu Leu Gly Lys Ser Asn Ala Thr Asn Leu Asp Pro Gly Pro 355 3SO 365

Asp His val Trp Ala Pro Glu Glu Leu Ser Leu ser Gly Glu Tyr val 370 375 380

Ara Ala Arg Ile Lys Gly Val Asn Tyr Glu Pro île Asp Arg Thr Lys 385 390 395 400 τντ Thr Lys val Leu TrD Asp Phe Àsn Asp Gly Thr Lys Gin Gly Pne 4Q5 ' 410 4·5·5 gly val Asn Ser Asp Ser pro Asn Lys Glu Leu Ile Al.a Val Asp Asn 420 425 430 glu Asn Asn Thr Leu Lys val Ser Gly Lêu Asp val Ser As« Asp Vas 435 440 445

Aer as» Gly Asn Phe Trp Ala Asn Ala Arg Leu Ser Ala Asn Giy Trp 450 455 460

Gly Lys Ser val Asp Tie Leu sly a!a Glu tvs Leu Thr Met Asp va: 465 470 475 4§0 tTs val Asp Glu Pro Thr Thr val Ala Ile Ala Ala île Pro- Gj^n Ser 485 490 495 ser Lys Ser Gly Trp Ala Asn Pro Glu Arg Ala val Arg val Asn Ala 5ÖÖ 505 510 glu Asp Phe Val Gin Gin Thr Asp Glv Lys Tyr Lys Ala Gly Leu Thr 515 520 525 île Thr Gly Glu Asp Ala Pro Asn Leu Lys Asn Ile Ala Phe hts- Glu 530 535 540 glu A$p Asn Asn Met Asn Asn île île Leu Phe val Gly Thr Asp Ala 545 550 555 560

Ala Asp Val Ile Tyr Leu Asp Asn île tvs Val lie Gly Thr Glu val 565 570 5/3

Glu île Pro val val Hi s Asp Pro Lys Gly Glu Ala Val Leu Pro Ser 580 585 590 val Phe Glu Asp Gly Thr Arq Gin Gly Trp Asp Trp Ala Gly Glu ser 595 " 600 605

Gly val Lys Thr Ala Leu Thr île Glu Glu Ala Asn Gly Ser Asn Ala 610 615 620

Leu Ser Trp Glu Phe Gly Tvr Pro Glu val Lys Pro Ser Asp Asn Trp 625 630 635 640

Ala Thr Ala Pro Arg Leu Asp Phe Trp tys Ser Asp Leu val Arg Gly 645 650 •61u Asn Asp Tyr val Ala Phe Asp Phe Tyr Leu Asp Pro val Arg Ala 660 665 670 ihr Glu sly Als Met Asrs île asîï Leu val Phe Gin Pro Pro Thr ash 67S S80 685

Gly Tyr Trp val Gin Ala Pro Lys Thr xyr Thr lie ash Phe Asp Glu 69Ö 695 700 teu Glu Glu Ala Asn Gin val Asn Gly Leu Tyr His Tyr Glu val Lys 705 710 715 720 lie Asn val Arg Asp lie Thr Asn lie Gin Asp Asp Thr Leu Leu Arg 725 730 735

Asn Met Met lie lie Phe Ala Asp val Glu Ser Asp Phe Ala Gly Arg 740 745 75Ö val Phe val Asp Asn val Arg Phe Glu Gly Ala Ala Thr Thr Glu Pro 755 760 765 val Glu Pro Glu Pro val Asp Pro Gly Glu Glu Thr Pro Pro val Asp 770 775 780

Glu Lys Glu Ala Lys Lys Glu Gin Lys Glu Ala Glu Lys Glu Glu tvs 785 790 795 800

Glu Ala val Lys Glu Glu Lys Lys Glu Ala Lys Glu Glu Lys Lys Ala 805 810 815 val Lys Asn Glu Ala Lys Lvs lys 820

Claims 1. A composition comprising a modified cellulose derivative having a molecular weightfrom 20 000 to 500 000 kDaltons or mixtures thereof and a cellulase enzyme characterised in that the weight ratio of the modified cellulose derivative to the active cellulase enzyme protein is from 20:1 to 10000:1 and wherein the composition does not contain 0.7 to 0.9 % by weight of the total composition, of sodium nonanoyl oxybenzene sulfonate, and does not contain 10 % by weight based of the total composition, of sodium perborate monohydrate, in which the enzyme is a bacterial alkaline enzyme exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4). 2. A composition according to claim 1 wherein the enzyme is a bacterial polypeptide endogenous to a member of the genus Bacillus. 3. A composition according to any of claims 1 or 2 wherein the enzyme is a polypeptide containing (i) at least one family 17 carbohydrate binding module and/or (ii) at least one family 28 carbohydrate binding module. 4. A composition according to any of claims 1 to 3 wherein the enzyme comprises a polypeptide endogenous to one of the following Bacillus species selected from the group consisting of: AA349 (DSM 12648), KSM S237,1139, KSM 64, KSM N131, KSM 635 (FERM BP 1485), KSM 534 (FERM BP 1508), KSM 53 (FERM BP 1509), KSM 577 (FERM BP 1510), KSM 521 (FERM BP 1507), KSM 580 (FERM BP 1511), KSM 588 (FERM BP 1513), KSM 597 (FERM BP 1514), KSM 522 (FERM BP 1512), KSM 3445 (FERM BP 1506), KSM 425 (FERM BP 1505), and mixtures thereof. 5. A composition according to any of claims 1 to 4 wherein the enzyme is selected from the group consisting of: (i) the endoglucanase having the amino acid sequence of positions 1 to position 773 of SEQ ID NO:1 ; (ii) an endoglucanase having a sequence of at least 90%, preferably 94%, more preferably 97% and even more preferably 99%, 100% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:1 ; or a fragment thereof has endo-beta-1,4-glucanase activity, when identity is determined by GAP provided in the GCG program using a GAP creation penalty of 3.0 and GAP extension penalty of 0.1 ; (iii) mixtures thereof. 6. A composition according to any of claims 1 to 5 wherein the enzyme is an alkaline endoglucanase variant obtained by substituting the amino acid residue of a cellulase having an amino acid sequence exhibiting at least 90%, preferably 95%, more preferably 98%, 100% identity with the amino acid sequence represented by SEQ. ID NO:2 at (a) position 10, (b) position 16, (c) position 22, (d) position 33, (e) position 39, (f) position 76, (g) position 109, (h) position 242, (i) position 263, (j) position 308, (k) position 462, (1) position 466, (m) position 468, (n) position 552, (o) position 564, and/or (p) position 608 in SEQ ID NO:2 and/or at a position corresponding thereto with another amino acid residue. 7. A composition according to claim 5 wherein the enzyme is characterised by at least one of the following substitutions: (a) at position 10: glutamine, alanine, proline or methionine, preferably glutamine; (b) at position 16: asparagine or arginine, preferably asparagine; (c) at position 22: proline; (d) at position 33: histidine; (e) at position 39: alanine, threonine or tyrosine, preferably alanine; (f) at position 76: histidine, methionine, valine, threonine or alanine, preferably histidine; (g) at position 109: isoleucine, leucine, serine or valine, preferably isoleucine; (h) at position 242: alanine, phenylalanine, valine, serine, aspartic acid, glutamic acid, leucine, isoleucine, tyrosine, threonine, methionine or glycine, preferably alanine, phenylalanine or serine; (i) at position 263: isoleucine, leucine, proline or valine, preferably isoleucine; (j) at position 308: alanine, serine, glycine or valine, preferably alanine; (k) at position 462: threonine, leucine, phenylalanine or arginine, preferably threonine; (l) at position 466: leucine, alanine or serine, preferably leucine; (m) at position 468: alanine, aspartic acid, glycine or lysine, preferably alanine; (n) at position 552: methionine; (o) at position 564: valine, threonine or leucine, preferably valine; an/or (p) at position 608: isoleucine or arginine, preferably isoleucine. 8. A composition according to claim 6 or claim 7 wherein the enzyme is selected from the group consisting of the following endoglucanase variants: Egl-237, Egl-1139, Egl-64, Egl-N131band mixtures thereof. 9. A composition according to any of claims 1 to 3 wherein the enzyme is an alkaline cellulase K having the following physical and chemical properties: (1) Activity: Having a Cx enzymatic activity of acting on carboxymethyl cellulose along with a weak C1 enzymatic activity and a weak beta-glucoxidase activity; (2) Specificity on Substrates: Acting on carboxymethyl cellulose(CMC), crystalline cellulose, Avicell, cellobiose, and p-nitrophenyl cellobioside(PNPC); (3) Having a working pH in the range of 4 to 12 and an optimum pH in the range of 9 to 10; (4) Having stable pH values of 4.5 to 10.5 and 6.8 to 10 when allowed to stand at 40°C for 10 minutes and 30 minutes, respectively; (5) Working in a wide temperature range of from 10 to 65°C with an optimum temperature being recognized at about 40°C; (6) Influences of chelating agents: The activity not impeded with ethylenediamine tetraacetic acid (EDTA), ethyleneglycol-bis-(ß-aminoethylether) Ν,Ν,Ν’,Ν''-tetraacetic acid (EGTA), N,N-bis(carboxymethyl)glycine (ni-trilotriacetic acid) (NTA), sodium tripolyphosphate (STPP) and zeolite; (7) Influences of surface active agents: Undergoing little inhibition of activity by means of surface active agents such as sodium linear alkylbenzenesulfonates (LAS), sodium alkylsulfates (AS), sodium polyoxyethylene alkyl-sulfates (ES), sodium alphaolefinsulfonates (AOS), sodium alpha-sulfonated aliphatic acid esters (alpha-SFE), sodium alkylsulfonates (SAS), polyoxyethylene secondary alkyl ethers, fatty acid salts (sodium salts), and dimethyldialkylammonium chloride; (8) Having a strong resistance to proteinases; and (9) Molecular weight (determined by gel chromatography): Having a maximum peak at 180,000 ± 10,000. 10. A composition according to any preceding claim wherein the bacterial alkaline enzyme exhibiting endo-beta-1,4-glucanase activity is comprised at a level of from 0.00005% to 0.15%, preferably from 0.0002% to 0.02%, or more preferably from 0.0005% to 0.01 % by weight of pure enzyme. 11. A composition according to any preceding claim wherein the weight ratio of modified cellulose derivative to active cellulase enzyme protein is up to 1000:1, preferably from 30:1 to 800:1. 12. A composition according to any preceding claim in which the modified cellulose derivative has a molecular weight from 100 000 to 300 000 kDaltons. 13. A composition according to any preceding claim in which the modified cellulose derivative is comprised in the composition at a level of from 0.02 to 5 %, preferably from 0.05 to 2 % by weight or more preferably from 0.1 to 1.5 % by weight. 14. A composition according to any preceding claim wherein the modified cellulose derivative is selected from the group consisting of anionically and nonionically modified celluloses, preferably being anionically modified. 15. A composition according to any preceding claim wherein the modified cellulose derivative has an average degree of substitution of 0.3 to 0.9, preferably 0.4 to 0.8. 16. A process of cleaning and/or treating a surface or fabric comprising the steps of optionally washing and/or rinsing said surface or fabric, contacting said surface or fabric with the composition of any of the preceding claims, then optionally washing and/or rinsing said surface or fabric.

Patentansprüche 1. Zusammensetzung, umfassend ein modifiziertes Cellulose-Derivat mit einem Molekulargewicht von 20000 bis 500000 kDaltons, oder Mischungen davon, und ein Cellulaseenzym, dadurch gekennzeichnet, dass das Gewichtsverhältnis des modifizierten Cellulose-Derivats zu dem aktiven Cellulaseenzymprotein von 20:1 bis 10000:1 beträgt und, wobei die Zusammensetzung nicht 0,7 bis 0,9 Gew.-% der Gesamtzusammensetzung an Natriumno-nanoyloxybenzolsulfonat enthält, und nicht 10 Gew.-%, bezogen auf die Gesamtzusammensetzung, an Natriumperboratmonohydrat enthält, in der das Enzym ein bakterielles alkalisches Enzym ist, das endo-beta-1,4-Glucana-seaktivität aufweist (E.C. 3.2.1.4). 2. Zusammensetzung nach Anspruch 1, wobei das Enzym ein auf ein Mitglied der Gattung Bacillus endogenes bakterielles Polypeptid ist. 3. Zusammensetzung nach einem der Ansprüche 1 oder 2, wobei das Enzym ein Polypeptid ist, enthaltend (i) mindestens ein Familie-17-Kohlenhydrat-Bindungsmodul und/oder (ii) mindestens ein Familie-28-Kohlenhydrat-Bin-dungsmodul. 4. Zusammensetzung nach einem der Ansprüche 1 bis 3, wobei das Enzym ein Polypeptid umfasst, das auf eine der folgenden Bacillus-Species endogen ist, die ausgewählt sind aus der Gruppe bestehend aus: AA349 (DSM 12648), KSM S237, 1139, KSM 64, KSM N131, KSM 635 (FERM BP 1485), KSM 534 (FERM BP 1508), KSM 53 (FERM BP 1509), KSM 577 (FERM BP 1510), KSM 521 (FERM BP 1507), KSM 580 (FERM BP 1511), KSM 588 (FERM BP 1513), KSM 597 (FERM BP 1514), KSM 522 (FERM BP 1512), KSM 3445 (FERM BP 1506), KSM 425 (FERM BP 1505), und Mischungen davon. 5. Zusammensetzung nach einem der Ansprüche 1 bis 4, wobei das Enzym ausgewählt ist aus der Gruppe bestehend aus: (i) der Endoglucanase mit der Aminosäuresequenz von Positionen 1 bis Position 773 von SEQ-ID Nr. 1 ; (ii) einer Endoglucanase mit einer Sequenz von mindestens 90 %, vorzugsweise 94 %, mehr bevorzugt 97 % und noch mehr bevorzugt 99 %, 100 % Identität mit der Aminosäure-Sequenz von Position 1 bis Position 773 von SEQ-ID Nr. 1; oderein Fragment davon hat Endo-beta-1,4-Glucanase-Aktivität, wenn die Identität mittels dem im GCG-Programm bereitgestellten GAP mit einer GAP Creation Penalty von 3,0 und einer GAP Extension Penalty von 0,1 bestimmt wird; (iii) Mischungen davon. 6. Zusammensetzung nach einem der Ansprüche 1 bis 5, wobei das Enzym eine alkalische Endoglucanase-Variante ist, die durch Ersetzen des Aminosäurerests einer Cellulase mit einer Aminosäuresequenz erhalten wird, die mindestens 90 %, vorzugsweise 95 %, mehr bevorzugt 98 %, 100 % Identität mit der Aminosäuresequenz aufweist, die durch SEQ-ID Nr. 2 dargestellt ist, in (a) Position 10, (b) Position 16, (c) Position 22, (d) Position 33, (e) Position 39, (f) Position 76, (g) Position 109, (h) Position 242, (i) Position 263, (j) Position 308, (k) Position 462, (I) Position 466, (m) Position 468, (n) Position 552, (o) Position 564, und/oder (p) Position 608 in SEQ-ID Nr. 2 und/oder in einer damit entsprechenden Position mit einem anderen Aminosäurerest aufweist. 7. Zusammensetzung nach Anspruch 5, wobei das Enzym gekennzeichnet ist durch mindestens eine derfolgenden Substitutionen: (a) an Position 10: Glutamin, Alanin, Prolin oder Methionin, vorzugsweise Glutamin; (b) an Position 16: Asparagin oder Arginin, vorzugsweise Asparagin; (c) an Position 22: Prolin; (d) an Position 33: Histidin; (e) an Position 39: Alanin, Threonin oder Tyrosin, vorzugsweise Alanin; (f) an Position 76: Histidin, Methionin, Valin, Threonin oder Alanin, vorzugsweise Histidin; (g) an Position 109: Isoleucin, Leucin, Serin oder Valin, vorzugsweise Isoleucin; (h) an Position 242: Alanin, Phenylalanin, Valin, Serin, Asparaginsäure, Glutaminsäure, Leucin, Isoleucin, Tyrosin, Threonin, Methionin oder Glycin, vorzugsweise Alanin, Phenylalanin oder Serin; (i) an Position 263: Isoleucin, Leucin, Prolin oder Valin, vorzugsweise Isoleucin; (j) an Position 308: Alanin, Serin, Glycin oder Valin, vorzugsweise Alanin; (k) an Position 462: Threonin, Leucin, Phenylalanin oder Arginin, vorzugsweise Threonin; (l) an Position 466: Leucin, Alanin oder Serin, vorzugsweise Leucin; (m) an Position 468: Alanin, Asparaginsäure, Glycin oder Lysin, vorzugsweise Alanin; (n) an Position 552: Methionin; (o) an Position 564: Valin, Threonin oder Leucin, vorzugsweise Valin; und/oder (p) an Position 608: Isoleucin oder Arginin, vorzugsweise Isoleucin. 8. Zusammensetzung nach Anspruch 6 oder Anspruch 7, wobei das Enzym ausgewählt ist aus der Gruppe bestehend aus den folgenden Endoglucanase-Varianten: Egl-237, Egl-1139, Egl-64, Egl-N131b und Mischungen davon. 9. Zusammensetzung nach einem der Ansprüche 1 bis 3, wobei das Enzym eine alkalische Cellulase K mit den folgenden physikalischen und chemischen Eigenschaften ist: (1 ) Aktivität: Mit einer Cx-Enzymaktivität der Wirkung auf Carboxymethylcellulose zusammen mit einer schwachen C-j-Enzymaktivität und einer schwachen beta-Glucoxidase-Aktivität; (2) Spezifität auf Substraten: Wirkung auf Carboxymethylcellulose (CMC), kristalline Cellulose, Avicell, Cello-biose, und p-Nitrophenylcellobiosid (PNPC); (3) Mit einem Arbeits-pH-Wert im Bereich von 4 bis 12 und einem pH-Wert-Optimum im Bereich von 9 bis 10; (4) Mit stabilen pH-Werten von 4,5 bis 10,5 und 6,8 bis 10, beim Stehenlassen bei 40 °C 10 Minuten bzw. 30 Minuten; (5) Wirkt in einem breiten Temperaturbereich von 10 bis 65 °C mit einer optimalen Temperatur bei etwa 40 °C; (6) Einflüsse von Chelatbildnern: Die Aktivität wird nicht beeinträchtigt durch Ethylendiamintetraessigsäure (EDTA), Ethylenglycol-bis-(ß-aminoethylether)N,N,N’,N"-tetraessigsäure (EGTA), N,N-bis(carboxymethyl)gly-cin (Nitriltriessigsäure) (NTA), Natriumtripolyphosphat (STPP) und Zeolit; (7) Einflüsse von oberflächenaktiven Mitteln: Unterliegt wenig Hemmung der Aktivität mittels oberflächenaktiven Mitteln, wie linearen Natriumalkylbenzolsulfonaten (LAS), Natriumalkylsulfaten (AS), Natriumpolyoxyethylenal-kylsulfaten (ES), Natrium-alpha-olefinsulfonaten (AOS), Natrium-alpha-sulfonierten aliphatischen Säureestern (alpha-SFE), Natriumalkylsulfonaten (SAS), sekundären Polyoxyethylenalkylethern, Fettsäuresalzen (Natriumsalzen), und Dimethyldialkylammoniumchlorid; (8) Weist eine starke Beständigkeit gegenüber Proteinasen auf; und (9) Molekulargewicht (bestimmt durch Gelchromatographie): Mit einen Maximumpeak bei 180.000 ± 10.000, 10. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das bakterielle alkalische Enzym, das endo- beta-1,4-Glucanaseaktivität aufweist, aus reinem Enzym in einer Konzentration von 0,00005 % bis 0,15 %, vorzugsweise von 0,0002 % bis 0,02 %, oder mehr bevorzugt von 0,0005 % bis 0,01 Gew.-% besteht. 11. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das Gewichtsverhältnis von modifiziertem Cellulose-Derivat zu aktivem Cellulaseenzymprotein bis zu 1000:1, vorzugsweise von 30:1 bis 800:1, beträgt. 12. Zusammensetzung nach einem der vorstehenden Ansprüche, in der das modifizierte Cellulose-Derivat ein Molekulargewicht von von 100 000 bis 300 000 kDaltons aufweist. 13. Zusammensetzung nach einem der vorstehenden Ansprüche, in der das modifizierte Cellulose-Derivat in der Zusammensetzung aus einer Konzentration von 0,02 bis 5 %, vorzugsweise von 0,05 bis 2 Gew.-% oder mehr bevorzugt von 0,1 bis 1,5 Gew.-% besteht. 14. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das modifizierte Cellulose-Derivat ausgewählt ist aus der Gruppe bestehend aus anionisch und nichtionisch modifizierten Cellulosen, die vorzugsweise anionisch modifiziert sind. 15. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das modifizierte Cellulose-Derivat einen durchschnittlichen Substitutionsgrad von 0,3 bis 0,9, vorzugsweise 0,4 bis 0,8 aufweist. 16. Verfahren zum Reinigen und/oder Behandeln einer Oberfläche oder eines Stoffes, umfassend die Schritte des wahlweisen Waschens und/oder Spülens der Oberfläche oder des Stoffes, Kontaktierens der Oberfläche oder des Stoffes mit der Zusammensetzung nach einem der vorstehenden Ansprüche, dann wahlweise Waschen und/oder Spülen der Oberfläche oder des Stoffes.

Revendications 1. Composition comprenant un dérivé de cellulose modifiée ayant une masse moléculaire allant de 20 000 à 500 000 kDaltons ou des mélanges de celle-ci et une enzyme cellulase, caractérisée en ce que le rapport pondéral du dérivé de cellulose modifiée à la protéine d’enzyme cellulase active va de 20:1 à 10000:1 et où la composition ne contient pas 0,7 à 0,9 % en poids de la composition totale, de nonanoyl-oxybenzène-sulfonate de sodium, et ne contient pas 10 % en poids sur la base de la composition totale, de perborate de sodium monohydraté, dans laquelle l’enzyme est une enzyme alcaline bactérienne présentant une activité d’endo-bêta-1,4-glucanase (E.C. 3.2.1.4). 2. Composition selon la revendication 1, dans laquelle l’enzyme est un polypeptide bactérien endogène à un membre du genre Bacillus. 3. Composition selon l’une quelconque des revendications 1 ou 2, dans laquelle l’enzyme est un polypeptide contenant (i) au moins un module de liaison d’hydrate de carbone de famille 17 et/ou (ii) au moins un module de liaison d’hydrate de carbone de famille 28. 4. Composition selon l’une quelconque des revendications 1 à 3, dans laquelle l’enzyme comprend un polypeptide endogène à une des espèces de Bacillus suivantes choisies dans le groupe constitué de : AA349 (DSM 12648), KSM S237, 1139, KSM 64, KSM N131, KSM 635 (FERM BP 1485), KSM 534 (FERM BP 1508), KSM 53 (FERM BP 1509), KSM 577 (FERM BP 1510), KSM 521 (FERM BP 1507), KSM 580 (FERM BP 1511), KSM 588 (FERM BP 1513), KSM 597 (FERM BP 1514), KSM 522 (FERM BP 1512), KSM 3445 (FERM BP 1506), KSM 425 (FERM BP 1505), et des mélanges de ceux-ci. 5. Composition selon l’une quelconque des revendications 1 à 4, dans laquelle l’enzyme est choisie dans le groupe constitué de : (i) l’endoglucanase ayant la séquence d’acides aminés de la position 1 à la position 773 de SEQ ID No. : 1 ; (ii) une endoglucanase ayant une séquence d’une identité d’au moins 90 %, de préférence 94 %, plus préférablement 97 % et encore plus préférablement 99 %, 100 % par rapport à la séquence d’acides aminés de la position 1 à la position 773 de SEQ ID No. : 1 ; ou un fragment de celle-ci a une activité d’endobêta-1,4-glucanase, lorsque l’identité est déterminée par le GAP (trou) fourni dans le programme GCG en utilisant une pénalité de création de GAP de 3,0 et une pénalité d’extension de GAP de 0,1 ; (iii) des mélanges de celles-ci. 6. Composition selon l’une quelconque des revendications 1 à 5, dans laquelle l’enzyme est un variant d’endoglucanase alcalin obtenu en remplaçant le résidu d’acide aminé d’une cellulase ayant une séquence d’acides aminés présentant au moins 90 %, de préférence 95 %, plus préférablement 98 %, 100 % d’identité avec la séquence d’acides aminés représentée par SEQ. ID No. : 2 à (a) la position 10, (b) la position 16, (c) la position 22, (d) la position 33, (e) la position 39, (f) la position 76, (g) la position 109, (h) la position 242, (i) la position 263, (j) la position 308, (k) la position 462, (I) la position 466, (m) la position 468, (n) la position 552, (o) la position 564, et/ou (p) la position 608 dans SEQ ID No. : 2 et/ou à une position correspondant à celle-ci par un autre résidu d’acide aminé. 7. Composition selon la revendication 5, dans laquelle l’enzyme est caractérisée par au moins une des substitutions suivantes : (a) à la position 10 : glutamine, alanine, proline ou méthionine, de préférence glutamine ; (b) à la position 16 : asparagine ou arginine, de préférence asparagine ; (c) à la position 22 : praline ; (d) à la position 33 : histidine ; (e) à la position 39 : alanine, thréonine ou tyrosine, de préférence alanine ; (f) à la position 76 : histidine, méthionine, valine, thréonine ou alanine, de préférence histidine ; (g) à la position 109 : isoleucine, leucine, sérine ou valine, de préférence isoleucine ; (h) à la position 242 : alanine, phénylalanine, valine, sérine, acide aspartique, acide glutamique, leucine, isoleucine, tyrosine, thréonine, méthionine ou glycine, de préférence alanine, phénylalanine ou sérine ; (i) à la position 263 : isoleucine, leucine, praline ou valine, de préférence isoleucine ; (j) à la position 308 : alanine, sérine, glycine ou valine, de préférence alanine ; (k) à la position 462 : thréonine, leucine, phénylalanine ou arginine, de préférence thréonine ; (l) à la position 466 : leucine, alanine ou sérine, de préférence leucine ; (m) à la position 468 : alanine, acide aspartique, glycine ou lysine, de préférence alanine ; (n) à la position 552 : méthionine ; (o) à la position 564 : valine, thréonine ou leucine, de préférence valine ; et/ou (p) à la position 608 : isoleucine ou arginine, de préférence isoleucine. 8. Composition selon la revendication 6 ou la revendication 7, dans laquelle l’enzyme est choisie dans le groupe constitué des variants d’endoglucanase suivants : Egl-237, Egl-1139, Egl-64, Egl-N131 b et des mélanges de ceux-ci. 9. Composition selon l’une quelconque des revendications 1 à 3, dans laquelle l’enzyme est une cellulase alcaline K ayant les propriétés physiques et chimiques suivantes : (1) Activité : ayant une activité enzymatique Cx pour agir sur la carboxyméthylcellulose en même temps qu’une faible activité enzymatique C1 et une faible activité de bêta-glucoxydase ; (2) Spécificité sur les substrats : agissant sur la carboxyméthylcellulose (CMC), la cellulose cristalline, l’Avicell, la cellobiose, et le p-nitrophényl cellobioside (PNPC) ; (3) Ayant un pH de travail dans la gamme de 4 à 12 et un pH optimal dans la gamme de 9 à 10 ; (4) Ayant des valeurs de pH stables de 4,5 à 10,5 et 6,8 à 10 lorsqu’on laisse reposer à 40 °C pendant 10 minutes et 30 minutes, respectivement ; (5) Fonctionnant dans un large intervalle de température allant de 10 à 65 °C avec une température optimale étant reconnue à environ 40 °C ; (6) Influences des agents chélatants : l’activité n’est pas entravée avec l’acide éthylène-diamine tétra-acétique (EDTA), l’acide éthylèneglycol-bis-(P-aminoéthyléther) N,N,N’,N"-tétra-acétique (EGTA), le N,N-bis(carboxy-méthyl)glycine (acide nitrilotriacétique) (NTA), le tripolyphosphate de sodium (STPP) et une zéolite ; (7) Influences des agents tensioactifs : subissant une petite inhibition d’activité au moyen d’agents tensioactifs tels que les sulfonates d’alkylbenzène linéaires de sodium (LAS), les alkylsulfates de sodium (AS), les poly-oxyéthylène alkylsulfates de sodium (ES), les alpha-oléfine-sulfonates de sodium (AOS), les esters d’acide aliphatique alpha-sulfonés de sodium (alpha-SFE), les alkylsulfonates de sodium (SAS), les alkyléthers secondaires de polyoxyéthylène, les sels d’acide gras (sels de sodium), et le chlorure de diméthyldialkylammonium ; (8) Ayant une forte résistance aux protéinases ; et (9) Masse moléculaire (déterminée par chromatographie sur gel) : ayant un pic maximum à 180 000 ± 10 000. 10. Composition selon l’une quelconque des revendications précédentes, dans laquelle l’enzyme alcaline bactérienne présentant une activité d’endo-bêta-1,4-glucanase est comprise à un taux allant de 0,00005 % à 0,15 %, de préférence de 0,0002 % à 0,02 %, ou plus préférablement de 0,0005 % à 0,01 % en poids d’enzyme pure. 11. Composition selon l’une quelconque des revendications précédentes, dans laquelle le rapport pondéral du dérivé de cellulose modifiée à la protéine d’enzyme cellulase active va jusqu’à 1000:1, de préférence de 30:1 à 800:1. 12. Composition selon l’une quelconque des revendications précédentes, dans laquelle le dérivé de cellulose modifiée a une masse moléculaire allant de 100 000 à 300 000 kDaltons. 13. Composition selon l’une quelconque des revendications précédentes, dans laquelle le dérivé de cellulose modifiée est compris dans la composition à un taux allant de 0,02 à 5 %, de préférence de 0,05 à 2 % en poids ou plus préférablement de 0,1 à 1,5 % en poids. 14. Composition selon l’une quelconque des revendications précédentes, dans laquelle le dérivé de cellulose modifiée est choisi dans le groupe constitué de celluloses modifiées par voie anionique et non ionique, étant de préférence modifiées par voie anionique. 15. Composition selon l’une quelconque des revendications précédentes, dans laquelle le dérivé de cellulose modifiée a un degré moyen de substitution de 0,3 à 0,9, de préférence 0,4 à 0,8. 16. Procédé de nettoyage et/ou de traitement d’une surface ou d’un tissu comprenant les étapes consistant à facultativement laver et/ou rincer ladite surface ou ledit tissu, mettre en contact ladite surface ou ledit tissu avec la composition selon l’une quelconque des revendications précédentes, puis à facultativement laver et/ou rincer ladite surface ou ledit tissu.

REFERENCES CITED IN THE DESCRIPTION

This list of references cited by the applicant is for the reader's convenience only. It does not form part of the European patent document. Even though great care has been taken in compiling the references, errors or omissions cannot be excluded and the EPO disclaims all liability in this regard.

Patent documents cited in the description • WO 02099091 A [0003] [0016] · WO 05042532 A1 [0048] • WO 04053039 A [0003] · WO 0032601 A [0050] • EP 265832 A [0003] [0015] [0016] · US 6225464 B [0050] • EP 1350843 A [0003] [0015] [0016] · US 4990280 A [0053] • GB 2095275 A [0004] · US 20030087791 A1 [0053] • WO 06117071 A, Unilever [0010] · US 20030087790 A1 [0053] • WO 2002099091 A [0015] · US 20050003983 A1 [0053] • WO 2004053039 A [0015] · US 20040048764 A1 [0053] • EP 0271044 A [0015] · US 4762636 A [0053] • J P 2000047237 A [0016] · U S 6291412 B [0053] • EP 271004 A, Kao [0016] · US 20050227891 A1 [0053] • JP 2005287441 A, Kao [0016] · EP 1070115 A2 [0053] • WO 9961479 A, Noviant [0024] · US 5879584 A [0053] • DE 102004063766 [0024] · US 5691297 A [0053] • JP 2002265999 A, Kao [0028] · US 5574005 A [0053] • WO 03091378 A [0029] · US 5569645 A [0053] • US 4310431 A [0029] · US 5565422 A [0053] • US 5576282 A [0030] [0046] · US 5516448 A [0053] • US 6306812 B1 [0030] · US 5489392 A [0053] • US 6326348 B1 [0030] · US 5486303 A [0053] • WO 9817767 A [0030] · US 6312936 B1 [0060] • WO 200503274 A [0041] · EP 06124858 A [0061] • WO 200503275 A [0041] · EP 06115574 A [0061] • WO 200503276 A [0041] · US 60819155 B [0061] • EP 06116780 A [0041] · EP 06116784 A [0061] • US 4430243 A [0045] · EP 06116782 A [0061] • US 5597936 A [0047] · EP 06116780 A [0061] • US 5595967 A [0047]

Non-patent literature cited in the description • J. KARLSSON et al. Biopolymers, 2002, vol. v63, · HAKAMADA et al. Biosci. Biotechnol. Biochem., 32-40 [0006] 2000, vol. 64, 2281-2289 [0016] • M. BAILEY et al. Enzyme Microb. Technoi., 1981, · FUKUMORI et al. J. Gen. Microbiol., vol. 132, vol. v3, 153-157 [0007] 2329-2335 [0016] • Y. BOURNE. Current Opinion in Structural Biology, · SUMITOMO et al. Biosci. Biotechnol. Biochem., 2001,593-600 [0014] 1992, vol. 56, 872-877 [0016] • A.B. BORASTON. Glycoside hydrolases and glyco- · S. ITO. Extremophiles, 1997, vol. v1,61-66 [0016] syltransferases: families and functional modules. · S. ITO et al. Agric Biol Chem, 1989, vol. v53, CBMs. Please refer further to Biochemical Journal, 1275-1278 [0016] 2002, vol. v361,35-40 [0014]

Claims (4)

RELIABLE RELATED RELATED FACTORY # 20 00CK * 50 0000 FULL MOTAKACOMOMATIC OVERFLOWER FUNCTIONALIZATION OF ACTIVITIES : ®: 1 - 1 () 000: 1. and that the Composition does not contain 0.7 --- 0.0% sodium Naoalkoxfeazia azuite based on the weight of the ointment composition, nor does it contain 10M of the weight of the yeast and the compound in the composition. Enzyme-EnhancedMs-Enzyme Enzyme, which exhibits endo-beta-1,4-gyrase activity. 0.2,1,4¾. Composition according to claim 1, wherein the azenzyme is an endogenous bacterial potipeptide in a given member of the Bacillus genus, 3. Any one of claims 1, 2, free litter claims, wherein the enzyme is oiyssipotipepticl (i) of at least one family of 17 sanbitrite-like thymodyls and / or $ 1: a more subtle one of the 26 Cold Carbon Degradation Modules. The composition according to any one of claims: $ * #, wherein m is an enzyme: Bacilli: a brain transducer: which is an endogenous bacterial pepper peptide tafteim, which is a species of the group comprising the following; AA349 (DSM 12648), KSM $ 23 ?. 1189, KSM 64, K $ M N131, KSM 635 (FORM SP I486). K8M 834 | PIRM 8P Í8Í> 6 | KM 53 (FERM 8P 1509), KSM 577 (PERM BP 1810). KSM 521 (FIRM: BF 1507), KSM 580 (PERM 8P1S11), KSM 588 (piRf 8P1S13}, K K517 (FERM BP 1514), KSM 622 (PERM 8P 1312). KSM 3448 (FERM 8P i808)) , i <S: M 425 (FERM: BP 1505} oh these are blending 8. Patent Claims, wherein the enzyme is selected from the group consisting of the following: ti): endoglycase containing the amino acid derivative of S1010: NP :: 1 in SiO1; CM ') - - an endogenous channel containing a sequence of at least 98%, preferably M? 4,: more preferably, more than 1%, more preferably 1, 1% 1; -773. poaiel in the βεο? D ND: 1 anOnvsvmzmermermst; or a fragment thereof having AndePétie 1: 4 - gliokanase activity having a potentiation effect of pm $ mtÉbm! gaps ΑΨ®ΑΨ%. 0 | to create a gap between the seeded S..Ö-e§ penalty point pAP sreatien penalty) and an existing penalty point of 0.1 to increase the gap between GAP ectenalen panaltyl, (iln and mixtures thereof. S,: 1 * "patent claims composition, where the enzyme is an alkaline enooglùkanâz variant that is obtained by an eetiulla amihosac → Dldailsniasa subspecies: which is (i) iQ ^ pylase, · $$ $ 1, posioidbam (c) 22, position f) 33 pczleidbim tf 09; position (f>? $ .Power, (g) at position 109. fe) 242; at position, e.g., at 213, §} at position 398, (k) at position 432, ILL; at position 082, pbzfiii, (o) 584, in position at the position, with an arsenic aspirin equivalent at least 90% in H, preferably fS% bam, and more preferably 28% feao 100% identical to S1Q, ÏD! 90> 2 ~ νοί fcífe | with a lymphatic reflux, or a fun match with a mystery of an amniotic acid superconductor, T, A sylaceae according to the invention wherein the enzymes are the following substitutions by hand! at least one metal sheet (a) at position 10: gfuamln, alanine, proline or methionyl. preferably glutamic; b) in position 1i>; aspartic or arginyl:, preferably aezparagin ;;; (c) at position 22; (cl) at position 33; híszisóín; (e) at position 39; aln, threonine, or tlrozine, preferably eianfnt | f) at position 70, histidine, mst; omn. cognate, thidonin, or alanine, preferably bisosine; (g) the phephase 102 is isohexyl, sececin, sarin, or, preferably, p is m at position 242; alanine, femalanine, valine, serine, ace paraffin, gfutsmic acid, leucine, iziíeadn, ilrozlrt, tréöín, eononln desire glioln. preferably alanine, phenylphenam or serine; (I): at position 203: Isefegcin, Lecine, Proline or Vatim are preferably isoenzymes? # «In position 308« Μη, ezpin, glloth wiîriŸ --- ®g ^ fSsô ^ ii '· - | k) at position 463: ireon. leuoo, ferÉalánt or arpinjn, caring for treoojm fi | at position 468 · lauem, alanln or szenn. dearly: â € 468 pancáéban: aianin. asaparagic acid, yion orzine, at position 562; meconim (o) ai: 564, in position: ready vmmn desire leuoic, oitoylpn only; | slv or (p | a: 60S, position; tpleuao or aryihtm elonyôaao à, AS ** Patent No. 7, Aozlm: selected from the following tndpgsbap ygpps to êilä group: Eg * M ¥ i: M®fc 1139 , Ifki4, EgkN13lb and their keyerfel 3, any of Claims 1-3 Composition is defined by the term "Im an allyl olaliol, wherein the latter is chemically bonded; rrtWfe: ti) Activity" by means of a cyclization cycle; Cx anzimaktlvltêssah and weak Cl anxiolactic Pi have a beta-glyco-xxdase activity; (3) IzübÂà ^ aëia ^ Mjksrbôkimaïii ^ ÂZôb: · (CMC), kfltylpa cellulose, Avicelen "chiloblone, and p-nitrophenyl cellbiosone (PHPC); (3) the percentage of the pH is 4-12ms, the pH optimum for the pape is about 10; (4) Stable pH value 4.5461 10.5%. if 10 minutes at 40 "C, being 6.8% at 10% if 30 patPif 40" Cmn is left; (5) A wide range of temperature ranges for the ICMS *%%% supply is found at about 4 ° C; (6) Six pepper sprays; the activity is not inhibited by ethylenediamine tetraacetic acid (EDTAI ethylene glycol / methyl-B-aminoethyl) -N, NH-1H-tetraacetic acid (ECITA), N: .H-bis (karPoxymethyl). y-Cplkl | pi | eeetaay}), sodium tripollophosphate (STFP), and zeolite, (7) Effect of surfactants: low activity inhibition in the state of Mtlietectives, min? straight chain sodium alkylbenzene sulphurplate (LASl nasal sodium sulfate {AS}, cold-polio> netemic acid; bovine (ES), alpha-alpha-leirizulfonates {AOS}, sodium α-aiphosphonates, predominantly acidic thiols, mmi pmmm mkmm mmm & greaves | rtetrierns); : ^ aisrïimt. (8) Fmteinlzbk is an encephalopathy ;; and m ooo ± 10 ooo, IP, te first »WsW Claims MrnáfyM is a bacterial alkaline enzyme which exhibits activity of m / m α-1 H -glucase activity of 0.00005 to 0.15%. more preferably from 2% to 0: 02% to m seed, more preferably from 0.0005 to 0.01% of mangle composition according to any one of the preceding Claims, wherein the ophthalmic cavity of the cotyledon is present at a temperature of more than 100 °; 1, preferably 30, 1, and 000: t, is the composition of the foregoing claims, wherein the QQ is as defined above. 13, according to the foregoing claims, transcends this modified path; i u small dry glaze in this composition 0.01 to 5% by weight. preferably 0.05% to 1% or more preferably 0.1% to 1.5% by weight · composition according to any one of the preceding claims is selected from the group consisting of nonionic modified celluloses, preferably anionically. composition according to any one of the preceding claims, wherein the mean degree of substitution of the modified cai vapor serum is from 0.3 to 0.0, preferably from 0.4 to 0.8, and the composition according to any of the preceding claims is given by Milet: or mammal liked from the steps of washing and / or burrs of the honeycomb: the steps of sitting, contacting the material in the room or contacting the material with the rivers and the washing of the wax or material, and / or flushing of the material, as desired.