NZ241700A - Detergent containing quaternary ammonium compound and a cellulase - Google Patents

Description

New Zealand Paient Spedficaiion for Paient Number £41 700 CH 7 / Priority Dat^s): Cuj.-ipieie Specification riled: .^rV".

Ci^s: .£I'.tejsaLf. tr'AOl/Ml.... , //..C'.'IMiSi/Sk.., ? V FEB 1995 Publication Date: ..4.7.

P.O. Journal, No: NO 7 A. v**-' No.: Date: NEW ZEALAND PATENTS ACT, 1953 COMPLETE SPECIFICATION UJ-. PATENT OFF!C~ 2 : FEB DETERGENT COMPOSITIONS WITH HIGH ACTIVITY CELLULASE AND QUATERNARY AMMONIUM COMPOUNDS We, THE PROCTER & GAMBLE COMPANY, a corporation organised under the laws of the State of Ohio, United States of America, located at One Procter & Gamble Plaza, Cincinnati, Ohio 45202, United States of America hereby declare the invention for which we pray that a patent may be granted to us, and the method by which it is to be performed, to be particularly described in and by the following statement:- - 1 -(followed by page la) - la - DETERGENT COMPOSITIONS WITH HIGH ACTIVITY CELLULASE AND QUATERNARY AMMONIUM COMPOUNDS Technical field The present invention relates to detergent compositions having cleaning and softening benefits.

Background of the Invention The need for detergent compositions which exhibit not only good cleaning properties, but also good fabric-softening performance, and other fabric care benefits, is well-established in the art.

EP 0 02 6 529 describes detergent compositions containing smectite-type clays and certain cationic compounds having cleaning and textile softening performance.

The efficiency of cellulolytic enzymes, i.e. cellulases, in terms of textile cleaning and harshness- 2 reducing agent for fabrics has been recognized for some time; GB-A-2,075,028, GB-A-2,095,275 and GB-A-2,094,826, disclose detergent compositions with cellulase for improved cleaning performance; GB-A-1,368,599 discloses the use of cellulase for reducing the harshness of cotton-containing fabrics; U.S. 4,435,307 teaches the use of a cellulolytic enzyme derived from Humicola insolens as well as a fraction thereof, designated ACXI, as a harshness-reducing detergent additive.

EP-A-0 269 168 discloses optimized detergent compositions containing cellulase, which are formulated at a mild alkaline pH range and provide combined fabric cleaning, fabric softening, and fabric care performance.

EP-B-0 125 122 discloses a detergent composition which combines cleaning and textile softening performance by using a synergetic mixture of a long-chain tertiary amine and cellulase.

In WO 89109259 have been disclosed cellulase preparations useful for reducing the harshness of cotton-containing fabrics, comprising an endoglucanase component with a high endoase activity and affinity towards cellulose.

The practical exploitation of cellulases has however, been set back by the fact that cellulase preparations such as those disclosed in the above-mentioned prior art documents, are complex mixtures, of which only a certain fraction is effective in the fabric-care context; it was thus difficult to implement cost effective industrial production of cellulase for the detergent industry; and large quantities of such cellulase preparations would need to be applied, in order to obtain the desired effect on fabrics.

Improvements in cellulase production also often have not proven to be sufficiently identifiable in terms of applicability in detergents. Defining a cellulase 241 3 selection criterium relevant for detergent application of cellulase was made possible by the C14CMC-method disclosed in EP-A-350 098. A minimum of 10% removal of immobilized radioactive labelled carboxymethylcellulose at 25 x 10-6% by weight of cellulase protein in the laundry test solution has been found to provide high activity cei.ulase. A preferred group of cellulase falling under the high activity definition according to the present invention has been disclosed in European Publication 0531372.

There is disclosed a cellulase preparation consisting essentially of a homogeneous endoglucanase component which is immunoreactive with a monoclonal antibody raised against a partially purified 43kD cellulase derived from Humicola insolens DM1800.

The finding that this particular endoglucanase component of cellulase is advantageous for the treatment of cellulose-containing materials now permits to produce the cellulase cost-effectively, e.g. by employing recombinant DNA techniques, and allows to apply only a small quantity of the cellulase preparation, and obtain the desired effect on fabrics.

It has surprisingly been found that an improved detergent composition can be formulated which combine superior cleaning and softening performance by using a synergestic mixture of water soluble quaternary ammonium compounds and high active cellulase. Said cellulase having at least 10% CMC removal at 25 x 10-6% by weight of cellulase protein in the laundry test solution.

It is another object of the present invention to provide a method for treating fabrics in a washing machine, comprising the utilization of the present detergent compositions, for the main wash cycle. 4 Summary of the Invention 24 A j The present invention provides a detergent composition comprising a quaternary ammonium compound of formula r1r2r3r4n+ x- wherein R^ is C8-C16 alkyl, each of R2, R3 and R4 is independently C2-C4 alkyl or hydroxy alkyl, benzyl, or -(c2h4o)xh where x has a value from 2 to 5, not more than one of R2' R3 or R4 being benzyl, and X is an anion, and a cellulase characterized in that said cellulase provides at least 101 removal of immobilized radio-active labelled carboxymethylcellulose according to the C14 CMC-method at 25 x 10-6% by weight of cellulase protein in the laundry test solution.

According to the present invention, a preferred cellulase consists of a homogeneous endoglucanase component which is immunoreactive with a monoclonal antibody raised against a partially purified = 43 kD cellulase derived from Humicola insolens DM 1800.

Detailed Description of the Invention CELLULASE The activity of enzymes and particularly the activity of cellulase enzyme has been defined for various applications by different analytical methods. These methods all attempt to provide a realistic assessment of the expected in use performance or at least a measurement correlating with the in use performance. As has been detailed in European Patent Application EP-A-350098, many of the methods, particularly these frequently used by cellulase manufacturers, are not sufficiently correlated with the in use performance of cellulase in laundry detergent compositions. This is due to the various other usage conditions for which these activity measurement methods have been developed.

The method described in EP-A-350098, has been developed to be and to have a predictive correlation for the ranking of cellulase activity in laundry detergent compositions.

The present invention therefore uses the method disclosed in EP-A-350098 to screen cellulases in order to distinguish cellulases which are useful in the present invention and those which would not provide the objectives of the present invention. The screening method, hereinafter referred to as C14CMC-Method, which has been adopted from the method disclosed in EP-A-350098, can be described as follows : Principle : The principle of the Cl4CMC-Method for screening is to measure at a defined cellulase concentration in a wash solution the removal of immobilized carboxy methyl cellulose (CMC) from a cloth substrate. The removal of CMC is measured by radio-active labelling of some of the CMC by using C14 radio-active carbon. Simple counting of the amount of radio-active C14 on the cloth substrate before and after the cellulase treatment allows the evaluation of the cellulase activity.

Sample preparation : CMC preparation : The radio-active CMC stock solution is prepared according to Table I. The radio-active CMC can be obtained by methods referred to in EP-A-350098.

Fabric substrates : The fabric substrates are muslin cotton swatches having a size of 5 cm x 5 cm. They are inocculated with 0.3 5 ml of the radio-active labelled CMC stock solution in their center. The muslin cotton swatches are then airdried.

■ © Immobilization of CMC : To immobilize the radio-active labelled CMC on the muslin cotton swatches, laundero-meter equipment " Linitest Original Haunau " made by Original Haunau, Germany, is used. A metal jar of the laundero-meter is filled with 400 ml of hard water (4 mmol/liter of Ca++ ions). A maximum number of 13 swatches can be used per jar. The jar is then incubated in a heat-up cycle from 20°C to 60°C over 40 minutes in the laundero-meter equipment. After incubation the swatches are rinsed under running city water for 1 minute. They are squeezed and allowed to airdry for at least 30 minutes.

According to EP-A-350098 samples of the swatches with immobilized radio-active CMC can also be measured as "blank samples" without washing.

Sample treatment : Laundry test solution : The laundry test solution is prepared according to the composition of Table II. It is balanced to pH 7.5. The laundry test solution is the basis to which a cellulase test sample is added. Care should be taken to not dilute the laundry test solution by adding water to a 100% balance prior to having determined the amount of cellulase to be added. The amount of cellulase which is used in this screening test should be added to provide 25 x 10~6 weight percent of cellulase protein in the laundry test solution (equivalent to 0.25 milligram/liter at 14.5 °C) .

Wash procedure : The swatches thus inocculated with radio-active labelled CMC are then treated in a laundry simulation process. The laundry process is simulated in the laundero-meter type equipment," Linitest, Original Haunau", by Original Haunau, Haunau Germany. An individual swatch is put into a 20 cm3 glass vial. The vial is filled with 10 ml of the laundry test solution and then sealed liquid tight. Up to 5 vials are put into each laundero-meter jar. The jar is filled with water as a heat tranfer medium for the laundering simulation. The laundering simulation is 7 conducted as a heat-up cycle from 20°C to 60°C over 40 minutes.

After the processing of the samples the vials are submerged in cold water and subsequently each swatch is taken out of its vial, rinsed in a beaker under running soft water, squeezed and allowed to airdry for at least 30 minutes.

Measurement : In order to measure radio-active labelled CMC removal, a scintillation counter, for example, a LKB 1210 Ultrabeta Scintillation Counter, is used. In order to obtain most accurate results, the instruction manual for optimum operation of the particular scintillation counter should be followed. For example, for the LKB 1210 Ultrabeta Scintillation Counter, the following procedure should be followed. The swatch to be measured is put into a plastic vial filled with 12 ml of scintillator liquid (e.g. scintillator 299 from Packard). The swatch is then allowed to stabilize for at least 30 minutes. The vial is then put into the LKB 1210 Ultrabeta Scintillation Counter and the respective radio-activity counts for the swatch is obtained.

In order to measure the amount of CMC removal due only to the cellulase, a measurement of a swatch which has been inocculated at the same time but has been treated in the laundry test solution without cellulase, is necessary. The activity of the cellulase is then expressed as percent of radio-active labelled CMC removal. This percentage is calculated by the following formula : % of radio-active CMC removal = XO - XC x 100 XO Wherein XO is the radioactivity scintillation count of a swatch treated with the laundry test solution without cellulase i 7 r s f XC is the radioactivity scintillation count of a swatch treated with the laundry test solution containing the cellulase to be evaluated Statistical considerations, procedure confirmation : In order to provide statistically sound results, standard statistical analysis should be employed. For the given example, using the LKB 1210 Ultrabeta Scintillation Counter, it has been found that a sample size of 3 swatches for each radioactivity scintillation count can be used.

In order to confirm the procedure by internal crosschecking, measurement and calculation of the "blank sample" according to EP-A-350098 are recommended. This will allow to detect and eliminate errors.

Interpretation of results : The described screening test does provide a fast, unique and reliable method to identify cellulases which satisfy the activity criteria of the present invention versus cellulases which are not part of the present invention.

It has been found that a removal of 10% or more of the immobilized radioactive labelled CMC according to the above C14CMC-method, indicates that the respective cellulase satisfies the requirements of the invention.

It will be obvious to those skilled in the art that removal percentages above 10% indicate a higher activity for the respective cellulase. It therefore is contemplated that cellulase providing above 25% or preferably above 50% removal of radioactive labelled CMC, at the protein concentration in the laundry test solution according to the C14CMC-method, would provide indication of an even better performance of the cellulase for use in laundry detergents.

It also has been contemplated that usage of higher concentrations of cellulase for C14CMC-method, would provide higher removal percentages. However, there exists no linear 241700 proven correlation between cellulase concentration and removal percentage obtained by it.

It also has been contemplated that usage of higher concentrations of cellulase for C14CMC-method, would provide higher removal percentages.

TABLE I : Radioactive C14 labelled CMC stock solution (all percentages by weight of total solution) Total CMC* (CMC should be detergent grade CMC with a degree of substitution from about 0.47 to about 0.7) 99.2 x 10~3% Ethanol 14985.12 X 10~3% Deionized Water 84915.68 X 10_3% Total : 100% * Total CMC contains non-radio-active and radio-active CMC to provide a radio-activity which allows sufficiently clear readings on the scintillation counter used. For example, the radio-active CMC can have an activity of 0.7 millicurie/g and be mixed with non-radio-active CMC at a ratio of 1:6.7. 24 1 7 0 TABLE II :Laundry test solution (all percentages by weight of total solution) Linear C12 alkyl benzene sulphonic acid 0.110% Coconut alkyl sulphate (TEA salt) 0.040% c12-15 alcohol ethoxylate (E07) 0.100% Coconut fatty acid 0.100% Oleic acid 0.050% Citric acid 0.010% Triethanolamine 0.040% Ethanol 0.060% Propanediol 0.015% Sodium hydroxide 0.030% Sodium formate 0.010% Protease 0.006% Water (2.5 mmol/liter Ca++), pH adjustment agent (HCL or NaOH solutions) and | cellulase balance to 100% '■/ 11 The water-soluble quaternary ammonium compound The water-soluble soluble quaternary ammonium compound has the formula : R1R2R3R4N+X~ wherein R^_ is Cg-C]_5 alkyl, each of R2, R3 and R4 is independently C]_-C4 alkyl, C]_-C4 hydroxy alkyl, benzyl, ana -(C2H4g)xK where x has a value from 2 to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl.

The preferred alkyl chain length for R]_ is C]_2-Ci_5 particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or 0X0 alcohols synthesis. Preferred groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X may be selected from halide, methosulpnate, acetate and phosphate ions.

Examples of suitable quaternary ammonium compounds are coconut trimethyl ammonium bromide coconut methyl dihydroxyethyl ammonium bromide decyl triethyl ammonium chloride aecyl dimethyl hydroxyethyl ammonium bromide nyristyl trimethyl ammonium methyl sulphate lauryl dimethyl benzyl ammonium bromide lauryl methyl (ethenoxy)4 ammonium bromide The water-soluble cationic component of the compositions of the present invention is capable of existing in cationic form in a 0.1% aqueous solution at pH 10. The water-soluble cationic compound will normally be present in an amount of from 0.2% to 10% by weight of the detergent composition.

Detergent adjuncts The detergent compositions of the present invention include components that are usually found in laundry detergents, these components being present in an amount of up to 95% by weight of the composition.

These include nonionic and zwitterionic surfactants, builder salts, bleaching agents and organic precursors therefor, suds suppression agents, soil suspending and anti-redeposition agents, enzymes, optical brighteners, colouring agents and perfumes.

A wide range of anionic surfactants can be used in the compositions of the present invention.

Suitable anionic non-soap surfactants are water soluble salts of alkyl benzene sulfonates, alkyl sulfates, alkyl polyethoxy ether sulfates, paraffin sulfonates, alphaolefin sulfonates, alpha-sulfocarboxylates and their esters, alkyl glyceryl ether sulfonates, fatty acid monoglyceride sulfates and sulfonates, alkyl phenol polyethoxy ether sulfates, 2-acdylozy-alkane-l-sulfonates, and beta-alkoxy alkane sulfonates. Soaps are also suitable anionic surfactants.

Especially preferred alkyl benzene sulfonates have 9 to 15 carbon atoms in a linear or branched alkyl chain, more especially 11 to 13 carbon atoms. Suitable alkyl sulfates have 10 to 22 carbon atoms in the alkyl chain, more especially from 12 to 18 carbon atoms. Suitable alkyl polyethoxy ether sulfates have 10 to 18 carbon atoms in the alkyl chain and have an average of 1 to 12 -CH2CH2O- groups per molecule, especially 10 to 16 carbon atoms in the alkyl chain and an average of 1 to 6 -CH2CH2O- groups per molecule.

Suitable paraffin sulfonates are essentially linear and contain from 8 to 24 carbon atoms, more especially from 14 to 18 carbon atoms. Suitable alphaolefin sulfonates have 10 to 24 carbon atoms, more especially 14 to 16 carbon atoms; alphaolefin sulfonates can be made by reaction with sulfur trioxide followed by neutralization under conditions such that any sultones present are hydrolyzed to the corresponding hydroxy alkane sulfonates. Suitable alphasulfocarboxylates contain from 6 to 20 carbon atoms; included herein are not only the salts of alphasulfonated fatty acids but also their esters made from alcohols containing 1 to 14 carbon atoms. 13 241700 Suitable alkyl glyceryl ether sulfates are ethers of alcohols having 10 to 18 carbon atoms, more especially those derived from coconut oil and tallow.

Suitable alkyl phenol polyethoxy ether sulfates have 3 to 12 carbon atoms in the alkyl chain and an average of 1 to 6 -CH2CH20- groups per molecule. Suitable 2-acyloxy-alkane-i-sulfonates contain from 2 to 9 carbon atoms in the acyl group and 9 to 23 carbon atoms in the alkane moiety. Suitable beta-alkyloxy alkane sulfonates contain 1 to 3 carbon atoms in the alkyl group and 8 to 20 carbon atoms in the alkane moiety.

The alkyl chains of the foregoing non-soap anionic surfactants can be derived from natural sources such as coconut oil or tallow, or can be made synthetically as for example using the Ziegler or 0x0 processes. Water solubility can be achieved by using alkali metal, ammonium, or alkanol-ammonium cations; sodium is preferred. Mixtures of anionic surfactants are contemplated by this invention; a satisfactory mixture contains alkyl benzene sulfonate having 11 to 13 carbon atoms in the alkyl group and alkyl sulfate having 12 to 18 carbon atoms in the alkyl group.

Suitable soaps contain 3 to 18 carbon atoms, more especially 12 to 18 carbon atoms. Soaps can be made by direct saponification of natural fats and oils such as coconut oil, tallow and palm oil, or by the neutralization of free fatty acids obtained from either natural or synthetic sources. The soap cation can be alkali metal, ammonium or alkanol-ammonium, sodium is preferred.

The compositions contain from 3 to 40% of anionic detergent, preferably from 4 to 15% of anionic detergent, more preferably, 5-10% of anionic surfactant.

As stated previously, the compositions of the present invention combine good softening and cleaning performance and in order to maintain the latter it is essential that the overall surfactant character be anionic. The molar ratio of the water-soluble quaternary ammonium compound to the anionic surfactant component should therefore be ^ /- 7 •wi. .F 14 ' ' less than 1:1 and desirably should be less than 1:1.5. In preferred embodiments of the invention such as heavy duty laundry detergent formulations, the molar ratio should be less than 1:2.

Subject to these constraints the cationic compound will normally be present in an amount of from 0.5% to 15% by weight of the composition, preferably from 1% to 5% and most preferably from 1.5% to 3% by weight.

Nonionic and zwitterionic surfactants may be incorporated in amounts of up to 50% by weight of the total surfactant but normally are present in amounts of less than 30% of the total surfactant. By "total surfactant" is meant the sum of the anionic surfactant (a) cationic component (b) and any added nonionic and/or zwitterionic surfactant. The incorporation of 15-25% nonionic surfactant based on the total surfactant weight (corresponding to 1-2% on a total composition basis) has been found to provide advantages in the removal of oily soils. Suitable nonionics are water soluble ethoxylated materials of HLB 11.5-177.0 and include (but are not limited to) C10-C2o primary and secondary alcohol ethoxy ethoxylates and C6-C10 alkylphenol ethoxylates. Ci4-Ci8 linear primary alcohols condensed with from seven to thirty moles of ethylene oxide per mole of alcohol are preferred, examples being C14~C15 (E°)7' ci6-cl8 (EO)25 and especially C16-C1S (EO)11.

Suitable zwitterionic surfactants include the C12-Cl6 alkyl betaines and sultaines. These and other zwitterionic and nonionic surfactants are disclosed in Laughlin & Heuring USP 3,929,678.

Detergent builder can be inorganic or organic in character. Non limiting examples of suitable water-soluble, inorganic alkaline detergent builder salts include the alkali metal carbonates, borates, phosphates, polyphosphates, bicarbonates, and silicates. Specific examples of such salts include the sodium and potassium tetraborates, bicarbonates, carbonates, tripolyphosphates, pyrophosphates, penta-polyphosphates and hexametaphosphates. Sulphates are usually also present.

Preferred water soluble builders are sodium tripolyphosphate and sodium silicate, and usually both are present. In particular, it is preferred that a substantial proportion, for instance for 3% to 15% by weight of the composition of sodium silicate (solids) or ratio (weights ratio Si02:Na20 from 1:1 to 3.5:1 be employed.

A further class of detergency builder materials useful in the present invention are insoluble sodium alumino silicates of the formula : Na2(A102)z (Si02)yxH20 wherein z and y are integers equal to at least 6, the molar ratio of z to y is in the range of from 1.0:1 to o.5:l and x is an integer from 15 to 264. A preferred material is Na12 (Si02Al02 ) 12 2 7H20. If present, incorporation of 5% to 25% by weight of aluminosilicate is suitable, partially replacing water-soluble builder salts, provided that sufficient water-soluble alkaline salts remain to provide the specified pH of the composition in aqueous solution.

Detergency builder salts are normally included in amounts of from 10% to 80% by weight of the composition preferably from 20% to 70% and most usually from 30% to 60% by weight.

Bleaching agents, suds controlling agents, soil suspending agents, proteolytic, amylolytic or lipolytic enzymes, especially proteolytic, and optical brighteners, may be present.

Colours, non-substantive, and perfumes, as required to improve the aesthetic acceptability of the product, are usually incorporated.

The detergent compositions according to the invention can be in liquid, paste or granular forms. Granular compositions according to the present invention can also 16 2 k be in "compact form", i.e. they may have a relatively higher density than conventional granular detergent compositions according to the present invention will contain a lower amount of "inorganic filler salt", compared to conventional granular detergents; typical filler salts are alkaline earth metal salts of sulphates and chlorides, typically sodium sulphate; "compact" detergents typically comprise not more than 10% filler salt.

Preparation of the compositions The detergent compositions may be prepared in any way, as appropriate to their physical form, as by mixing the components, co-agglomerating them cr dispersing them in a liquid carrier. In granular form a detergent salt builder can be incorporated and the granular is prepared by spray drying an aqueous slurry of the non-heat-sensitive components, and the builder salt to form spray dried granules into which may be admixed the heat sensitive components such as persalts, enzymes, perfumes. The water-soluble quaternary compound may be included in the slurry for spray drying or it may be incorporated by dissolving or dispersing the cationic component in water or another suitable volatile liquid and then spraying this solution of aisperion onto the spray dried granules before or after other heat sensitive solids have been dry mixed with them. Alternatively the water-soluble quaternary compound can be dry mixed together with the other heat sensitive solids. Clay components may be added to the slurry for spray drying or may be dry mixed, as preferred for reasons unrelated to its softening effect, such as for optimum colour of the product.

The invention is illustrated by the following non-limiting examples.

The following examples are meant to exemplify compositions of the present invention, but are not necessarily meant to limit or otherwise define the scope of the invention, said scope being determined according to claims which follow. 17 EXAMPLE I Criticality of the cellulase performance parameter of claim 1 The following test was conducted : Test conditions : Washing temperature : 60°C (heat up cycle) Washing time : 40 min. pH = 7.5 Water hardness : 4 mmol/L Detergent concentration : 1% Detergent composition : erf. EPA 350 098 ex. 1 Cellulases : 1) CelluzymeR supplied by Novo Nordisk = reference 2) 43kD endoglucanase = cellulase according to the invention Test Results : % CI4-CMC Removal by Cellulase Detergent without cellulase (= reference) 0 Detergent + CelluzymeR 1.5 mg protein/L (150 x 10-6%) 12.7 3.0 mg protein/L (300 x 10_6%) 17.7 4.5 mg protein/L (450 x 10"6%) 21.5 Detergent + 4 3kD endoglucanase 0.3 mg protein/L (30 x 10~6%) 20.3 Discussion of the results : The above data clearly demonstrate the criticality of the claimed parameter for the cellulases of the invention over the commercially available Celluzyme.

EXAMPLE II 18 24 1 70 Two sets of different detergent compositions are prepared, all based on a compact granular detergent composition.

Such a compact granular detergent composition typically contains the following ingredients : Linear alkyl benzene sulphonate (LAS) 9.5% Alkyl suphate 3% Nonionic 4% Trisodium citrate 21% Zeolite 33% Citric acid 6% Polymer 4% Chelant 0.2% Sodium sulphate 6% Sodium silicate 2% Perborate 0.5% Phenol sulphonate 0.1% The above detergent composition was supplemented as indicated below : SET 1 : With 4 3kD endoglucanase (*)Quaternary ammonium No Cellulase (PSU) 2.4 mg CelJulase/L wash liquor compounds level mg/I (240 x 10"6%) (PSU) 0 -2.5 0 ltd) ■2.5 1.5 200 -2.5 3.5 (*) C12~c14 dimethyl (hydroxyethyl) ammonium chloride 19 SET 2 : With CelluzymeR (*)Quaternarv ammonium No Cellulase (PSU) 92 mg Cellulase/L wash liquor compounds level me/'l (9200 x 10"6%) (PSU) 0 -0.3 0 100 -0.3 0 200 -0.3 0 ,") "i2_c14 dimethyl (hydroxyethyl) ammonium chloride Test procedure : Cellulase has the property to de-pill worn cotton fabrics. In a model test the measurement of de-pilling is used to assess cellulase performance.

Swatches of worn blue pyjama fabric were treated with different wash solutions in a Laundrometer (temperature 30°C). The water hardness was 2.5 mM Calcium. After tumble drying, the fabrics were graded for de-pilling by direct comparison of the different detergent matrices. Visual grading was performed by expert judges using a 0 to 4 scale (PSU). In this scale 0 is fiven for no difference and 4 is given for maximum difference. The PSU grading are statistical recount, an average of 4 replicates is made, LSD (least significant difference) is 0.5 PSU at 95% confidence level.

The above results demonstrate the synergy between the quaternary ammonium compound and the 43 kD cellulase in that the performance of the 43 kD cellulase is significantly improved by the quaternary ammonium compound.

EXAMPLE III-VI Test procedure : 3.5 kg of clean fabric laundry loads were washed in an automatic drum washing machine Miele 423 at 60°C. The hardness of the water was 2,5 mM Calcium and the composition concentration was 0.7% in the wash liquor. For softness evaluation swatches of terry towel were line dried prior for assessment of softness. Comparative softness assessment was done by expert judges using a scale of 0 to 4 panel-score-units (PSU). In this scale 0 is given for no difference and 4 is given for maximum difference. Softness was assessed after one and after one, four and eight wash cycles. LSD is 0.5 psu at the 95% confidence level. The following compositions are made : 21 ? k ' 1 Ingredients HI Surfactant Linear alkylbenzene sulfonate 8 Tallow alkvl sulphate 2 C]2"C 14 dimeth. hydroxyeth ammonium chlo 5 Fatty alcohol (C 12-C15) ethoxylate j « Builder/chelants Zeolite A 18.5 Copolymer of maieic and acrylic acid, sodium salt 5 Bleach Sodium perborate 11 N,N,N,T-Tetraacelvl ethylene diamine 4 Perfume 0.5 Enzymes Protease 1.6 Cellulase 43 kD 0.5 Softness system Smectite/montmonllonite clays 12.5 Polvethvlene oxide 0.3 Buffer Carbonate 10.6 Silicate (2.0) 4 CMC. chelants Admix and spray-on (suds suppression, miscellaneous,...) Percentage bv weight IV V VI 8 8 8 2 2 2 1.5 1.5 1.5 18.5 18.5 18.5 5 5 5 11 11 11 4 4 4 0.5 0.5 0.5 1.6 1.6 1.6 0.5 12.5 12.5 12.5 0.3 0.3 0.3 .6 10.6 10.6 4 4 4 balance to 100 04 22 Results : Detergent composition III 0.5% (= 40 .x 10~6% mg proteine wash liquor) 43 kD cellulase + 5% quaternary ammonium component versus detergent composition IV 0.5% (= 40 x 10_6% mg proteine wash liquor) 43 kD cellulase no quaternary ammonium component Cvcles 1 4 8 PSU 0 0.8s 1.8s Detergent composition V + 5% quaternary ammonium composition versus detergent composition VI no quaternary ammonium component Cycles 1 4 8 PSU - - 0.1 significant difference at 95% confidence Conclusion : The above results demonstate that the quaternary ammonium compound / 43 kD cellulase combination gives a statistical significant better performance than the sum of the individual actions of both ingredients.

Formulation examples : The following compositions are made 14 1 7 Ingredients Composition (% by weight) Regular products I II III IV ' alkvl benzene sulfonate Tallow alcohol sulfate (Na) C J4_15 alkyl sulfate (Na) A-Olefin (C 12-18) sulfonate (Na) Tallow alcohol ethoxylate (EO j j) q 5 r'jtty alcohol (C 1*1.151 i.'iho\vlatd (EO -) Hydrogenated tallow fatty acid C12-14 Dimethyl (hydroethyl) ammonium chlonde Sodium tnpolvphosphate 24 Zeolite A Sodium citrate Oleic fatty acid Citric acid C]4.]6 alkyl succinate 1,2-Propanediol Ethanol Na Metaborate Octahydrate Polyethylene oxide 5MM molecular weight 0.05 Polyethylene oxide 0.3MM molecular weight Sodium sulfate 12 iodium carbonate 5 Sodium silicate 4 Sodium perborate (1 aq.) 15 N.N.N.N-Tetraacetvlethylene diamine 3 CMC 0.3 Polyacrylate (MW 1000-20 000) Polyacrylate (MW 4000-5000) Maleic-acrylic copolymer 2 Cellulase 0.5 Smectite/montmonllomte clay 10.5 Phosphate Admix and sprav-on (perfumes, protease, amylase, lipolase, buffer, sud suppression, miscelaneous. moisture and minors) 0.5 5 0.3 7 4 3 0.3 1.5 0.5 10.5 5 4 18 0.3 0.5 10.5 balance to 100 4 0.5 0.5 0.05 4 3 0.3 3 1 .5 0.3 Ingredients Composition (% by weight) Compact product Liquid product C j benzene sulfonate Tallow alcohol sulfate (Na) C14-15 alkyl sulfate (Na) A-Olefin (C j2-1 sulfonate (Na) Tullim .iLohol L-thox\l.ile lEO | |) Fatty alcohol (C 12-15) ethoxylate (EO 7) Hydrogenated tallow fatty acid C12-14 Dimethyl (hydroethyl) ammonium chloride Sodium tnpolyphosphate Zeolite A Sodium citrate Oleic fatty acid Citric acid Cj4_j6a'kyl succinate 1,2-Propanediol Ethanol Na Metaborate Octahydrate Polyethylene oxide 5MM molecular weight Polyethylene oxide 0.3MM molecular weight -ul tundli: Sodium carbonate Sodium silicate Sodium perborate (1 aq.) N,N,N.N-Tetraacetyiethylene diamine CMC Polyacrylate (MW 1000-20 000) Polyacrylate (MW 4000-5000) Maleic-acrylic copolymer Cellulase Smectite/montmonllomte clay Layered silicate Admix and spray-on (perfumes, protease, amylase, lipolase. buffer, sud suppression, miscelaneous, moisture and minors) 0.3 II 4 11 4 0.4 3 1 12 7 19 6 0.3 Z. 11 3 12 3 0.3 4 0.5 12 1 2 10 3 7 1 .5 balance to 100 SEQUENCE DESCRIPTION: SEQ 10 NO:1: GGATCCAAG ATG CGT TCC TCC CCC CTC CTC CCG TCC GCC GTT GTG GCC 48 Met Arg Ser Ser Pro Leu Leu Pro Ser Ala Va1 Val Ala -21 -20 -15 -10 GCC CTG CCG GTG TTG GCC CTT GCC GCT GAT GGC AGG TCC ACC CGC TAC 96 Ala Leu Pro Val Leu Ala Leu Ala Ala Asp Gly Arg Ser Thr Arg Tyr -5 1 5 TGG GAC TGC TGC AAG CCT TCG TGC GGC TGG GCC AAG AAG GCT CCC GTG i44 Trp Asp Cys Cys Lys Pro Ser Cys Gly Trp Ala Lys Lys Ala Pro Val 10 15 20 AAC CAG CCT GTC TTT TCC TGC AAC GCC AAC TTC CAG CGT ATC ACG GAC 192 Asn Gin Pro Val Phe Ser Cys Asn Ala Asn Phe Gin Arg lie Thr Asp 25 30 35 40 TTC GAC GCC AAG TCC GGC TGC GAG CCG GGC GGT GTC GCC TAC TCG TGC 240 Phe Asp Ala Lys Ser Gly Cys Glu Pro Gly Gly Val Ala Tyr Ser Cys 45 50 55 GCC GAC CAG ACC CCA TGG GCT GTG AAC GAC GAC TTC GCG CTC GGT TTT 288 Ala Asp Gin Thr Pro Trp Ala Val Asn Asp Asp Phe Ala Leu Gly Phe 60 65 70 GCT GCC ACC TCT ATT GCC GGC AGC AAT GAG GCG GGC TGG TGC TGC GCC 336 Ala Ala Thr Ser lie Ala Gly Ser Asn Glu Ala Gly Trp Cys Cys Ala 75 80 85 TGC TAC GAG CTC ACC TTC ACA TCC GGT CCT GTT GCT GGC AAG AAG ATG 384 Cys Tyr Glu Leu Thr Phe Thr Ser Gly Pro Val Ala Gly Lys Lys Met 90 95 100 GTC GTC CAG TCC ACC AGC ACT GGC GGT GAT CTT GGC AGC AAC CAC TTC 432 Val Val Gin Ser Thr Ser Thr Gly Gly Asp Leu Gly Ser Asn His Phe 105 110 115 120 GAT CTC AAC ATC CCC GGC GGC GGC GTC GGC ATC TTC GAC GGA TGC ACT 480 Asp Leu Asn lie Pro Gly Glv Gly Val Gly He Phe Asp Gly Cys Thr :2 5 ' 130 135 CCC CAG TTC GGC GGT CTG CCC GGC CAG CGC TAC GGC GGC ATC TCG TCC 528 Pro Gin Phe Gly Gly Leu Pro Gly Gin Arg Tyr Gly Gly lie Ser Ser 140 145 150 CGC AAC GAG TGC GAT CGG TTC CCC GAC GCC CTC AAG CCC GGC TGC TAC 576 Arg Asn Glu Cys Asp Arg Phe Pro Asp Ala Leu Lys Pro Gly Cys Tyr 155 160 165 TGG CGC TTC GAC TGG TTC AAG AAC GCC GAC AAT CCG AGC TTC AGC TTC 624 Trp Arg Phe Asp Trp Phe Lys Asn Ala Asp Asn Pro Ser Phe Ser Phe 170 175 180 CGT CAG GTC CAG TGC CCA GCC GAG CTC GTC GCT CGC ACC GGA TGC CGC 672 Arg Gin Val Gin Cys Pro Ala Glu Leu Val Ala Arg Thr Gly Cys Arg 185 190 195 200 CGC AAC GAC GAC GGC AAC TTC CCT GCC GTC CAG ATC CCC TCC AGC AGC 720 Arg Asn Asp Asp Gly Asn Phe Pro Ala Val Gin lie Pro Ser Ser Ser 205 210 215 ACC AGC TCT CCG GTC AAC CAG CCT ACC AGC ACC AGC ACC ACG TCC ACC 768 Thr Ser Ser Pro Val Asn Gin Pro Thr Ser Thr Ser Thr Thr Ser Thr 220 225 230 TCC ACC ACC TCG AGC CCG CCA GTC CAG CCT ACG ACT CCC AGC GGC TGC 816 Ser Thr Thr Ser Ser Pro Pro Val Gin Pro Thr Thr Pro Ser Gly Cys 235 240 245 ACT GCT GAG AGG TGG GCT CAG TGC GGC GGC AAT GGC TGG AGC GGC TGC 864 Thr Ala Glu Arg Trp Ala Gin Cys Gly Gly Asn Gly Trp Ser Gly Cys 250 255 260 ACC ACC TGC GTC GCT GGC AGC ACT TGC ACG AAG ATT AAT GAC TGG TAC 912 Thr Thr Cys Val Ala Gly Ser Thr Cys Thr Lys lie Asn Asp Trp Tyr 265 270 275 280 CAT CAG TGC CTG TAGACGCAGG GCAGCTTGAG GGCCTTACTG GTGGCCGCAA 964 His Gin Cys Leu 285 CGAAATGACA CTCCCAATCA CTGTATTAGT TCTTGTACAT AATTTCGTCA TCCCTCCAGG 1024 GATTGTCACA TAAATGCAAT GAGGAACAAT GAGTAC 1060 'A. 1 700 SEQUENCE DESCRIPTION: SEQ ID N0:2: Met Arg Ser Ser Pro Leu Leu Pro Ser Ala Val Val Ala Ala Leu Pro -21 -20 -15 -10 Val Leu Ala Leu Ala Ala Asp Gly Arg Ser Thr Arg Tyr Trp Asp Cys -5 1 5 10 Cys Lys Pro Ser Cys Gly Trp Ala Lys Lys Ala Pro Val Asn Gin Pro 15 20 25 Val Phe Ser Cys Asn Ala Asn Phe Gin Arg He Thr Asp Phe Asp Ala 30 35 40 Lys Ser Gly Cys Glu Pro Gly Gly Val Ala Tyr Ser Cys Ala Asp Gin 45 50 55 Thr Pro Trp Ala Val Asn Asp Asp Phe Ala Leu Gly Phe Ala Ala Thr 60 65 70 75 Ser lie Ala Gly Ser Asn Glu Ala Gly Trp Cys Cys Ala Cys Tyr Glu 80 85 90 Leu Thr Phe Thr Ser Gly Pro Val Ala Gly Lys Lys Met Val Val Gin 95 100 105 Ser Thr Ser Thr Gly Gly Asp Leu Gly Ser Asn His Phe Asp Leu Asn 110 115 120 lie Pro Gly Glv Gly Val Gly lie Phe Asp Gly Cys Thr Pro Gin Phe 125 * 130 135 Gly Gly Leu Pro Gly Gin Arg Tyr Gly Gly lie Ser Ser Arg Asn Glu 140 145 150 155 Cys Asp Arg Phe Pro Asp Ala Leu Lys Pro Gly Cys Tyr Trp Arg Phe 160 165 170 Asp Trp Phe Lys Asn Ala Asp Asn Pro Ser Phe Ser Phe Arg Gin Val 175 180 185 31n Cys Pro Ala Glu Leu Val Ala Arg Thr Gly Cys Arg Arg Asn Asp 190 195 200 -so Glv Asn Phe Pro Ala Val G'n He Pro Ser Ser Ser Thr Ser Ser 205 2:0 215 23 Pro Val Asn Gin Pro Thr Ser Thr Ser Thr Thr Ser Thr Ser Thr Thr 220 225 230 235 Ser Ser Pro Pro Val Gin Pro Thr Thr Pro Ser Gly Cys Thr Ala Glu 240 245 250 Arg Trp Ala Gin Cys Gly Gly Asn Gly Trp Ser Gly Cys Thr Thr Cys 255 260 265 Val Ala Gly Ser Thr Cys Thr Lys He Asn Asp Trp Tyr His Gin Cys 270 275 280 Leu SEQUENCE DESCRIPTION: SEQ ID NO:3: GAATTCGCGG CCGCTCATTC ACTTCATTCA TTCTTTAGAA TTACATACAC TCTCTTTCAA 60 AACAGTCACT CTTTAAACAA AACAACTTTT GCAACA ATG CGA TCT TAC ACT CTT 114 Met Arg Ser Tyr Thr Leu 1 5 CTC GCC CTG GCC GGC CCT CTC GCC GTG AGT GCT GCT TCT GGA AGC GGT 162 Leu Ala Leu Ala Gly Pro Leu Ala Val Ser Ala Ala Ser Gly Ser Gly 10 15 20 CAC TCT ACT CGA TAC TGG GAT TGC TGC AAG CCT TCT TGC TCT TGG AGC 210 His Ser Thr Arg Tyr Trp Asp Cys Cys Lys Pro Ser Cys Ser Trp Ser 25 20 35 GGA AAG GCT GCT GTC AAC GCC CCT GCT TTA ACT TGT GAT AAG AAC GAC 258 Gly Lys Ala Ala Val Asn Ala Pro Ala Leu Thr Cys Asp Lys Asn Asp 40 45 50 AAC CCC ATT TCC AAC ACC AAT GCT GTC AAC GGT TGT GAG GGT GGT GGT 306 Asn Pro lie Ser Asn Thr Asn Ala Val Asn Gly Cys Glu Gly Gly Gly 55 60 65 70 TCT GCT TAT GCT TGC ACC AAC TAC TCT CCC TGG GCT GTC AAC GAT GAG 354 Ser Ala Tyr Ala Cys Thr Asn Tyr Ser Pro Trp Ala Val Asn Asp Glu 75 80 85 CTT GCC TAC GGT TTC GCT GCT ACC AAG ATC TCC GGT GGC TCC GAG GCC 402 Leu Ala Tvr Gly Phe Ala Ala Thr Lys lie Ser Gly Gly Ser Glu Ala 90 95 100 AGC TGG TGC TGT GCT TGC TAT GCT TTG ACC TTC ACC ACT GGC CCC GTC 450 Ser Trp Cys Cys Ala Cys Tyr Ala Leu Thr Phe Thr Thr Gly Pro Val 105 110 115 AAG GGC AAG AAG ATG ATC GTC CAG TCC ACC AAC ACT GGA GGT GAT CTC 498 Lys Gly Lys Lys Met He Val Gin Ser Thr Asn Thr Gly Gly Asp Leu 120 125 130 GGC GAC AAC CAC TTC GAT CTC ATG ATG CCC GGC GGT GGT GTC GGT ATC 546 Gly Asp Asn His Phe Asp Leu Met Met Pro Gly Gly Gly Val Gly lie 135 140 145 150 TTC GAC GGC TGC ACC TCT GAG TTC GGC AAG GCT CTC GGC GGT GCC CAG 594 Phe Asp Gly Cys Thr Ser Glu Phe Gly Lys Ala Leu Gly Gly Ala Gin 155 160 165 TAC GGC GGT ATC TCC TCC CGA AGC GAA TGT GAT AGC TAC CCC GAG CTT 642 Tyr Gly Gly lie Ser Ser Arg Ser Glu Cys Asp Ser Tyr Pro Glu Leu 170 175 180 CTC AAG GAC GGT TGC CAC TGG CGA TTC GAC TGG TTC GAG AAC GCC GAC 690 Leu Lys Asp Gly Cys His Trp Arg Phe Asp Trp Phe Glu Asn Ala Asp 185 190 195 AAC CCT GAC TTC ACC TTT GAG CAG GTT CAG TGC CCC AAG GCT CTC CTC 738 Asn Pro Asp Phe Thr Phe Glu Gin Val Gin Cys Pro Lys Ala Leu Leu 200 205 210 GAC ATC AGT GGA TGC AAG CGT GAT GAC GAC TCC AGC TTC CCT GCC TTC 786 Asp lie Ser Gly Cys Lys Arg Asp Asp Asp Ser Ser Phe Pro Ala Phe 215 220 225 230 AAG GTT GAT ACC TCG GCC AGC AAG CCC CAG CCC TCC AGC TCC GCT AAG 834 Lys Val Asp Thr Ser Ala Ser Lys Pro Gin Pro Ser Ser Ser Ala Lys 235 240 245 AAG ACC ACC TCC GCT GCT GCT GCC GCT CAG CCC CAG AAG ACC AAG GAT 882 Lys Thr Thr Ser Ala Ala Ala Ala Ala Gin Pro Gin Lys Thr Lys Asp 250 255 260 TCC GCT CCT GTT GTC CAG AAG TCC TCC ACC AAG CCT GCC GCT CAG CCC 930 Ser Ala Pro Val Val Gin Lys Ser Ser Thr Lys Pro Ala Ala Gin Pro 265 270 275 GAG CCT ACT AAG CCC GCC GAC AAG CCC CAG ACC GAC AAG CCT GTC GCC 978 Glu Pro Thr Lys Pro Ala Asp Lys Pro Gin Thr Asp Lys Pro Val Ala 280 285 290 ACC AAG CCT GCT GCT ACC AAG CCC GTC CAA CCT GTC AAC AAG CCC AAG 1026 Thr Lys Pro Ala Ala Thr Lys Pro Val Gin Pro Val Asn Lys Pro Lys -95 300 305 310 ACA ACC CAG AAG GTC CGT GGA ACC AAA ACC CGA GGA AGC TGC CCG GCC 1074 "hr Thr Gin Lys Val Arg Gly Thr Lys Thr Arg Gly Ser Cys Pro Ala 315 320 325 '»... 1 7 0 AAG ACT GAC GCT ACC GCC AAG GCC TCC GTT GTC CCT GCT TAT TAC CAG 1122 Lys Thr Asp Ala Thr Ala Lys Ala Ser Val Val Pro Ala Tyr Tyr Gin 330 335 340 TGT GGT GGT TCC AAG TCC GCT TAT CCC AAC GGC AAC CTC GCT TGC GCT 1170 Cys Gly Gly Ser Lys Ser Ala Tyr Pro Asn Gly Asn Leu Ala Cys Ala 345 350 355 ACT GGA AGC AAG TGT GTC AAG CAG AAC GAG TAC TAC TCC CAG TGT GTC 1218 Thr Gly Ser Lys Cys Val Lys Gin Asn Glu Tyr Tyr Ser Gin Cys Val 360 365 370 CCC AAC TAAATGGTAG ATCCATCGGT TGTGGAAGAG ACTATGCGTC TCAGAAGGGA 1274 Pro Asn 375 TCCTCTCATG AGCAGGCTTG TCATTGTATA GCATGGCATC CTGGACCAAG TGTTCGACCC 1334 TTGTTGTACA TAGTATATCT TCATTGTATA TATTTAGACA CATAGATAGC CTCTTGTCAG 1394 CGACAACTGG CTACAAAAGA CTTGGCAGGC TTGTTCAATA TTGACACAGT TTCCTCCATA 1454 AAAAAAAAAA AAAAAAAAA 1473 32 241700 SEQUENCE DESCRIPTION: SEQ ID N0:4: Met Arg Ser Tyr Thr Leu Leu Ala Leu Ala Gly Pro Leu Ala Val Ser 15 10 15 Ala Ala Ser Gly Ser Gly His Ser Thr Arg Tyr Trp Asp Cys Cys Lys 20 25 30 Pro Ser Cys Ser Trp Ser Gly Lys Ala Ala Val Asn Ala Pro Ala Leu 35 40 45 Thr Cys Asp Lys Asn Asp Asn Pro He Ser Asn Thr Asn Ala Val Asn 50 55 60 Gly Cys Glu Gly Gly Gly Ser Ala Tyr Ala Cys Thr Asn Tyr Ser Pro 65 70 75 80 Trp Ala Val Asn Asp Glu Leu Ala Tyr Gly Phe Ala Ala Thr Lys He 85 90 95 Ser Gly Gly Ser Glu Ala Ser Trp Cys Cys Ala Cys Tyr Ala Leu Thr 100 105 110 Phe Thr Thr Gly Pro Val Lys Gly Lys Lys Met lie Val Gin Ser Thr 115 120 125 Asn Thr Gly Gly Asp Leu Gly Asp Asn His Phe Asp Leu Met Met Pro 130 135 140 Gly Gly Gly Val Gly lie Phe Asp Gly Cys Thr Ser Glu Phe Gly Lys 145 150 155 160 Ala Leu Gly Gly Ala Gin Tyr Gly Gly He Ser Ser Arg Ser Glu Cys 165 170 175 Asp Ser Tyr Pro Glu Leu Leu Lys Asp Gly Cys His Trp Arg Phe Asp 180 185 190 Trp Phe Glu Asn Ala Asp Asn Pro Asp Phe Thr Phe Glu Gin Val Gin 195 200 205 Cys Pro Lys Ala Leu Leu Asp He Ser Gly Cys Lys Arg Asp Asp Asp 210 215 220 S*r Ser Pre Pro Ala Phe Lvs Val Asp Thr Ser Ala Ser Lys Pro Gin 225 230 235 240

Claims (27)

33 ? 4 Pro Ser Ser Ser Ala Lys Lys Thr Thr Ser Ala Ala Ala Ala Ala Gin 245 250 255 Pro Gin Lys Thr Lys Asp Ser Ala Pro Val Val Gin Lys Ser Ser Thr 260 265 270 Lys Pro Ala Ala Gin Pro Glu Pro Thr Lys Pro Ala Asp Lys Pro Gin 275 280 285 ihr Asp Lys Pro Val Ala Thr Lys Pro Ala Ala Thr Lys Pro Val Gin 290 295 300 Pro Val Asn Lys Pro Lys Thr Thr Gin Lys Val Arg Gly Thr Lys Thr 305 310 315 320 Arg Gly Ser Cys Pro Ala Lys Thr Asp Ala Thr Ala Lys Ala Ser Val 325 330 335 Val Pro Ala Tyr Tyr Gin Cys Gly Gly Ser Lys Ser Ala Tyr Pro Asn 340 345 350 Gly Asn Leu Ala Cys Ala Thr Gly Ser Lys Cys Val Lys Gin Asn Glu 355 360 365 fyr Tyr Ser Gin Cys Val Pro Asn 370 375 241 34 WHAT^WE CLAIM IS:

1. A detergent composition comprising a water-soluble ammonium compound of the formula wherein R]_ is Cg-C16 alkyl, each of R2, R3 and R4 is independently C1-C4 alkyl or hydroxyl alkyl, benzyl, or -(C2H4O)XH where x has a value from 2 to 5, not more than one of R2, R3 or R4 being benzyl and X~ is an anion; and a cellulase, characterized in that the cellulase provides at least 10% removal of immobilized radioactive labelled carboxymethyl cellulose according to the C14CMC method at 25 x 10"6% by weight of the cellulase protein in the laundry test solution.

2. A detergent composition according to claim 1 wherein the cellulase consists essentially of a homogeneous endoglucanase component which is immunoreactive with an antibody raised against a highly purified about 43 kD cellulase derived from Humicola insolens. DSM 1800, or which is homologous to said 43kD cellulase.

3. A detergent composition according to claim 2 wherein the endoglucanase component of said cellulase has an isoelectric point of about 5.1.

4. A detergent composition according to claim 2 or 3 wherein said endoglucanase component is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector carrying a DNA sequence encoding said endoglucanase component or a precursor of said endoglucanase component, as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the endoglucanase component, or a precursor thereof, in a culture medium under conditions permitting the expression of the endoglucanase component or precursor thereof and recovering the endoglucanase component from the culture. fc.fk.lt I 35

5. A letergent composition according to claim 1 wherein the ceLlulase has the amino acid sequence shown in the appended sequence listing ID#2, or is a homologue thereof exhibiting endoglucanase activity.

6. A detergent composition according to claim 3 wherein said cellulase is producible by a species of Humicola

7. A detergent composition according to claim 6 wherein the species of Humicola is Humicola insolens.

8. A detergent composition according to claim 1 characterized in that the cellulase is an endoglucanase enzyme having the amino acid sequence shown in the appended sequence listing ID # 4, or is a homologue thereof exhibiting endoglucanase activity.

9. A detergent composition according to claim 8 wherein said endoglucanase enzyme is producible by a species of Fusarium.

10. A detergent composition according to claim 9 wherein the species of Fusarium is Fusarium oxvsporum.

11. A detergent composition according to any one of claims 5 to 10 wherein the enzyme is produced by a DNA construct comprising a DNA sequence encoding the enzyme.

12. A detergent composition according to claim 11 wherein the DNA sequence is as shown in the appended sequence listings ID # 1 or ID # 3. 24 170 36

!3 A detergent composition according to any one of claims 5 to 12 wherein said endoglucanase component is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector carrying a DNA sequence encoding said endoglucanase component or a precursor of said endoglucanase component, as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the endoglucanase component, or a precursor thereof, in a culture medium under conditions permitting the expression of the endoglucanase component or precursor thereof and recovering the endoglucanase component from the culture.

14. A detergent composition according to claim 13 wherein said host cell is a strain of a fungus or a yeast cell belonging to a strain of Hansenula or Saccharomvces.

15. A detergent composition according to claim 14 wherein the fungus is Tricloderuca or Aspergillus.

16. A detergent composition according to claim 14 or 15 wherein the fungus is Aspergillus orvzae or Aspergillus niger.

17. A detergent composition according to claim 14, 15 or 16 wherein the yeast cell is a strain of Saccachomvces cerevisae.

IS. A detergent composition according to claim 13 wherein said host cell is a strain of a bacterium.

19. A detergent composition according to claim 18 wherein the bacterium is Bacillus, Streptomvces or B.coli. o!j v 19Q4 1 v !•: ;:r' 37 24 1, 7 00

20. A detergent composition according to any one of claims 1 to 19, wherein the water-soluble cationic compound is selected from quaternary ammonium salts in which Rj is Cl2"Ci4 alkyl and R2, R3 and R4 are selected from methyl and hydroxyethyl groups.

21. A detergent composition according to any one of claims 1 to 20, wherein the level of said water-soluble cationic compound is from 0.2 to 10%.

22. A detergent composition according to any one of claims 1 to 21, further comprising anionic surfactants, wherein the molar ratio of the anionic surfactant to the water-soluble quaternary ammonium compound is greater than 1:1.

23. A detergent composition according to any one of the preceding claims, which is a detergent additive.

24. A detergent composition according to claim 23 in the form of a non-dusting granulate or liquid.

25. A detergent composition according to claim 23 which is in granular form, compact granular form or liquid form.

26. A detergent composition according to any one of claims 1 to 25, substantially as herein described.

27. A laundry process comprising contacting fabrics with a detergent composition according to any one of claims 1 to 26, wherein the cellulase is added at levels of from 0.005 to 40 mg enzyme protein/liter of wash solution. :.;s?2v0n,\Y