WO1993016158A1

WO1993016158A1 - Detergent compositions with high activity cellulase and quaternary ammonium compounds

Info

Publication number: WO1993016158A1
Application number: PCT/US1992/001179
Authority: WO
Inventors: Andre Christian Convents; Alfred Busch; Andred Cesar Baeck
Original assignee: The Procter & Gamble Company
Priority date: 1992-02-18
Filing date: 1992-02-18
Publication date: 1993-08-19
Also published as: AU2244992A; JPH07504448A; JP2974780B2

Abstract

The present invention provides a detergent composition comprising a quaternary ammonium compound of formula: R1R2R3R4N+ X-, wherein R¿1? is C8-C16 alkyl, each of R2, R3 and R4 is independently C1-C4 alkyl or hydroxy alkyl, benzyl, or -(C2H40)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 10 % 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.

Description

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 fabricsoftening performance, and other fabric care benefits, is well-established in the art.

EP 0 026 529 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- 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 amme and cellulase.

In WO 89109259 have been disclosed cellulase

preparations useful for reducing the harshness of cottoncontaining fabrics, comprising an endoglucanase component with a nigh 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; ana large quantities of sucn 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 m detergents. Defining a cellulase 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 × 10^-6% by weight of cellulase protein in the laundry test solution has been found to provide high activity cellulase. A preferred group of cellulase falling under the high activity definition according to the present invention has been disclosed in copending

Danish Patent Application No. : 1159/90 filed May 5,

1990. 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 technigues, 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 × 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. Summary of the Invention

The present invention provides a detergent composition comprising a quaternary ammonium compound of formula

R₁R₂R₃R₄N⁺ X- wherein R₁ is C₈-C₁₆ alkyl, each of R₂, R₃ and R₄ is

independently C₁-C₄ alkyl or hydroxy alkyl, benzyl, or -(C₂H₄₀)_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 10% removal of immobilized radio-active labelled carboxymethylcellulose according to the C14 CMC-method at 25 × 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 C14CMC-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 × 5 cm. They are inocculated with 0.35 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 × 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 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 × 100

XO

Wherein XO is the radioactivity scintillation count of a

swatch treated with the laundry test solution without cellulase 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 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.

The water-soluble quaternary ammonium compound

The water-soluble soluble quaternary ammonium compound has the formula :

R₁R₂R₃R₄N⁺X- wherein R₁ is C₈-C₁₆ alkyl, each of R₂ , R₃ and R₄ is independently C₁-C₄ alkyl, C₁-C₄ hydroxy alkyl, benzyl, and -(C₂H₄₀)_xH where x has a value from 2 to 5, and X is an anion. Not more than one of R₂, R₃ or R₄ should be benzyl.

The preferred alkyl chain length for R₁ is C₁₂-C₁₅ 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, methosulphate, acetate and phosphate ions.

Examples of suitable quaternary ammonium compounds are coconut trimethyl ammonium bromide

coconut methyl dihydroxyethyl ammonium bromide decyl triethyl ammonium chloride

decyl dimethyl hydroxyethyl ammonium bromide myristyl 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, alphasulfocarboxylates and their esters, alkyl glyceryl ether sulfonates, fatty acid monoglyceride sulfates and

sulfonates, alkyl phenol polyethoxy ether sulfates, 2-acdylozy-alkane-1-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. 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 -CH2CH2O- groups per molecule. Suitable 2-acyloxy-alkane-1-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 Oxo 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 8 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 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-C₂₀ primary

and secondary alcohol ethoxy ethoxylates and C₆-C₁₀ alkylphenol ethoxylates. C₁₄-C₁₈ linear primary alcohols condensed with from seven to thirty moles of ethylene oxide per mole of alcohol are preferred, examples being C₁₄-C₁₅ (EO)7, C₁₆-C₁₈ (EO)25 and especially C₁₆-C₁₈

(EO) 11.

Suitaole zwitterionic surfactants include the C₁₂-C₁₆ 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 watersoluble, 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 SiO₂:Na₂O 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(AlO₂)_z(SiO₂)_yxH₂O

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 (SiO₂AlO₂) ₁₂27H₂O. 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 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 anyway, as appropriate to their physical form, as by mixing the components, co-agglomerating them or dispersing them in a liquid carrier. In granular form a detergent saltbuilder 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 disperion 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. 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) Celluzyme^R supplied by Novo Nordisk

= reference

2) 43kD endoglucanase

= cellulase according to the invention

Test Results :

% C14-CMC Removal by Cellulase Detergent without cellulase (= reference) 0

Detergent + Celluzyme^R

1.5 mg protein/L (150 × 10^-6%) 12.7

3.0 mg protein/L (300 × 10^-6%) 17.7

4.5 mg protein/L (450 × 10^-6%) 21.5

Detergent + 43kD endoglucanase

0.3 mg protein/L (30 × 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

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 :

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 guaternary 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 :

Percentage by weight

Ingredients III IV V VI Surfactant

Linear alkylbenzene sulfonate 8 8 8 8

Tallow alkyl sulphate 2 2 2 2

C ₁₂-C ₁₄ dimeth. hydroxyeth ammonium chlo 5 - 5 -

Fatty alcohol (C ₁₂-C ₁₅) ethoxylate 1.5 1.5 1.5 1.5

Builder/chelants

Zeolite A 18.5 18.5 18.5 18.5

Copolymer of maleic and

acrylic acid, sodium salt

Bleach

Sodium perborate 1 1 1 1 11 11

N,N,N,T-Tetraacetyl ethyiene

diamine 4 4 4 4

Perfume 0.5 0.5 0.5 0.5

Enzymes - - - -

Protease 1.6 1.6 1.6 1.6

Cellulase 43 kD 0.5 0.5 - -

Softness system

Smectite/montmorillonite clays 12.5 12.5 12.5 12.5

Polyethylene oxide 0.3 0.3 0.3 0.3

Buffer

Carbonate 10.6 10.6 10.6 10.6

Silicate (2.0) 4 4 4 4

CMC, chelants

Admix and spray-on (suds suppression,

miscellaneous,...) balance to 100 Results :

Detergent composition III 0.5% (= 40 × 10^-6% mg proteine wash liguor) 43 kD cellulase + 5% quaternary ammonium component versus detergent composition IV 0.5% (= 40 × 10^-6% mg proteine wash liquor) 43 kD cellulase no

quaternary ammonium component

Detergent composition V + 5% quaternary ammonium

composition versus detergent composition VI no quaternary ammonium component

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 Ingredients Composition (% by weight)

Regular products

I II III IV

C_{11- 12}alkyl benzene sulfonate 7 5 4 -

Tallow alcohol sulfate (Na) - 2 - - C_14-15 alkyl sulfate (Na) - - 3 4 A-Olefin (C_12-18) sulfonate (Na) - - - 0.5 Tallow alcohol ethoxylate (EO₁₁) 0.5 - - - Fatty alcohol (C p.15) ethoxylate (EO₇) - - - 0.5

Hydrogenated tallow fatty acid - 0.5 - -

C_12-14 Dimethyl(hydroeihyl)ammomum chloride - - 5 3

Sodium tπpolyphosphate 24 - - 25 Zeolite A - 20 20 - Sodium citrate - 5 5 - Oleic fatty acid - - - -

Citric acid - - - -

C_14-16alkylsuccmate - - - -

1,2-Propanediol - - - -

Ethanol - - - -

Na Metaborate Octahydrate - - - -

Polyethylene oxide 5MM molecular weight 0.05 - - 0.05

Polyethylene oxide 0.3MM molecular weight - 0.3 - -

Sodium sulfate 12 10 15 5

Sodium carbonate 5 7 - 15

Sodium silicate 4 4 4 4

Sodium perborate (1 aq.) 15 15 18 15

N,N,N,N-Tetraacetylethylene diamine 3 3 - 3

CMC 0.3 0.3 0.3 0.3

Pol yacry late (MW 1000-20000) _ 1.5 - -

Polyacrylate (MW 4000-5000) - - 3 -

Maleic-acrylic copolymer - - 3

Cellulase 0.5 0.5 0.5 1

Smectite/montmonllomte clay 10.5 10.5 10.5 10.5

- - - 0.3

Phosphate

Admix and spray-on (perfumes, protease, amylase,

balance to 100

lipolase. buffer, sud suppression, miscelaneous,

moisture and minors) Ingredients Composition ( % by weight)

Compact product Liquid product I II I

C_11-12 alkyl benzene sulfonate 8 - 10

Tallow alcohol sultate (Na) 2 2 - C_14-15 alkyl sulfate (Na) - 6 1

A-Olefin (C_12-18) sulfonate (Na) - - - Tallow alcohol ethoxylate (EO ₁₁) - - - Fatty alcohol (C_12-15) ethoxylate (EO₇) - - -

Hydrogenated tallow fatty acid - - -

C _{12- 14} Dimethyl(hydroethyl)ammonium chloride 5 5 -

Sodium tripolyphosphate - - -

Zeolite A 15 19 -

Sodium citrate - 6 -

Oleic fatty acid - - 1

Citric acid - - 2

C_14-16 alkyl succinate - - 10

1,2-Propanediol - - 3

Ethanol - - 7

Na Metaborate Octahydrate - - 1

Polyethylene oxide 5MM molecular weight - - -

Polyethylene oxide 0.3MM molecular weight 0.3 0.3 - Sultonate - 2 -

Sodium carbonate 11 11 -

Sodium silicate 4 3 -

Sodium perborate (1 aq.) 11 12 -

N,N,N,N-Tetraacetylethylene diamine 4 3 -

CMC 0.4 0.3 -

Polyacrylate (MW 1000-20000) - - -

Polyacrylate (MW 4000-5000) - - -

Maleic-acrylic copolymer 5 4 -

Cellulase 1 0.5 1

Smectite/ montmorillonite clay 12 12 10.5

Layered silicate 7 - -

Admix and spray-on (perfumes, protease, amylase,

lipolase, buffer, sud suppression, miscelaneous , balance to 100 moisture and minors) SEQUENCE DESCRIPTION: SEQ ID 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 Val 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 144 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 Gln Pro Val Phe Ser Cys Asn Ala Asn Phe Gln Arg Ile 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 Gln 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 Ile 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 Gln 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 Ile Pro Gly Gly Gly Val Gly Ile Phe Asp Gly Cys Thr

125 130 135 CCC CAG TTC GGC GGT CTG CCC GGC CAG CGC TAC GGC GGC ATC TCG TCC 528 Pro Gln Phe Gly Gly Leu Pro Gly Gln Arg Tyr Gly Gly Ile 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 Gln Val Gln 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 Gln Ile 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 Gln 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 Gln 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 Gln 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 Ile Asn Asp Trp Tyr

265 270 275 280

CAT CAG TGC CTG TAGACGCAGG GCAGCTTGAG GGCCTTACTG GTGGCCGCAA 964 His Gln Cys Leu

285

CGAAATGACA CTCCCAATCA CTGTATTAGT TCTTGTACAT AATTTCGTCA TCCCTCCAGG 1024

GATTGTCACA TAAATGCAAT GAGGAACAAT GAGTAC 1060

SEQUENCE DESCRIPTION: SEQ ID NO: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 Gln Pro

15 20 25

Val Phe Ser Cvs Asn Ala Asn Phe Gln Arg Ile Thr Asp Phe Asp Ala

30 35 40

Lys Ser Gly Cys Glu Pro Gly Gly Val Ala Tyr Ser Cys Ala Asp Gln 45 50 55

Thr Pro Trp Ala Val Asn Asp Asp Phe Ala Leu Gly Phe Ala Ala Thr 60 65 70 75

Ser Ile 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 Gln

95 100 105

Ser Thr Ser Thr Gly Gly Asp Leu Gly Ser Asn His Phe Asp Leu Asn

110 115 120

Ile Pro Gly Gly Gly Val Gly Ile Phe Asp Gly Cys Thr Pro Gln Phe 125 130 135

Gly Gly Leu Pro Gly Gln Arg Tyr Gly Gly Ile 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 ASD Asn Pro Ser Phe Ser Phe Arg Gln Val

175 180 185

Gln Cys Pro Ala Glu Leu Val Ala Arg Thr Gly Cys Arg Arg Asn Asp

190 195 200 Asp Gly A sp Pre Pro Ala Va l Gl n I le Pro Ser Ser Ser Thr Ser Ser 205 210 2 1 5 Pro Val Asn Gln Pro Thr Ser Thr Ser Thr Thr Ser Thr Ser Thr Thr 220 225 230 235

Ser Ser Pro Pro Val Gln Pro Thr Thr Pro Ser Gly Cys Thr Ala Glu

240 245 250

Arg Trp Ala Gln Cys Gly Gly Asn Gly Trp Ser Gly Cys Thr Thr Cys

255 260 265

Val Ala Gly Ser Thr Cys Thr Lys Ile Asn Asp Trp Tyr His Gln 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 30 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 Ile 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 Tyr Gly Phe Ala Ala Thr Lys Ile 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 HO 115

AAG GGC AAG AAG ATG ATC GTC CAG TCC ACC AAC ACT GGA GGT GAT CTC 498 Lys Gly Lys Lys Met Ile Val Gln 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 Ile

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 Gln

155 160 165

TAC GGC GGT ATC TCC TCC CGA AGC GAA TGT GAT AGC TAC CCC GAG CTT 642 Tyr Gly Gly Ile 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 Gln Val Gln 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 Ile 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 Gln 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 Gln Pro Gln 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 Gln Lys Ser Ser Thr Lys Pro Ala Ala Gln 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 Gln 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 Gln Pro Val Asn Lys Pro Lys

295 300 305 310

ACA ACC CAG AAG GTC CGT GGA ACC AAA ACC CGA GGA AGC TGC CCG GCC 1074 Thr Thr Gln Lys Val Arc Gly Thr Lys Thr Arα Gly Ser Cys Pro Ala

315 320 225 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 Gln

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 Gln Asn Glu Tyr Tyr Ser Gln 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

SEQUENCE DESCRIPTION: SEQ ID NO:4:

Met Arg Ser Tyr Thr Leu Leu Ala Leu Ala Gly Pro Leu Ala Val Ser 1 5 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 Ile 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 Ile

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 Ile Val Gln 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 Ile Phe Asp Gly Cys Thr Ser Glu Phe Gly Lys 145 150 155 160

Ala Leu Gly Gly Ala Gln Tyr Gly Gly Ile 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 ASD Phe Thr Phe Glu Gln Val Gln

195 200 205

Cys Pro Lys Ala Leu Leu Asp Ile Ser Gly Cys Lys Arg Asp Asp Asp 210 215 220

Ser Ser Phe Pro Ala Phe Lvs Val Asp Thr Ser Ala Ser Lys Pro Gln 225 230 235 240 Pro Ser Ser Ser Ala Lys Lys Thr Thr Ser Ala Ala Ala Ala Ala Gln 245 250 255

Pro Gln Lys Thr Lys Asp Ser Ala Pro VaTVal Gln Lys Ser Ser Thr

260 265 270

Lys Pro Ala Ala Gln Pro Glu Pro Thr Lys Pro Ala Asp Lys Pro Gln

275 280 285

Thr Asp Lys Pro Val Ala Thr Lys Pro Ala Ala Thr Lys Pro Val Gln 290 295 300

Pro Val Asn Lys Pro Lys Thr Thr Gln 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 Gln 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 Gln Asn Glu

355 360 365

Fyr Tyr Ser Gln Cys Val Pro Asn

370 375

Claims

1. A detergent composition comprising a quaternary ammonium compound of the formula

R₁R₂R₃R₄NT X- wherein R₁ is C₈-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 × 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 endoglucanase.

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 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 form the culture.

5. A detergenr 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 exmciting enαoglucanase activity.

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

7. A detergent composition according to claim 1

characterized in that the cellulase compound is and endoglucanase enzyme having the amino acid sequence shown in the appended sequence using ID#4, or is a homologue thereof exhibiting endoglucanase activity.

8. A detergent composition according to claim 7 wherein said endoglucanase enzyme is producible by a species of Fusarium. e.g. Fusarium oxysporum.

9. A detergent composition according to claim 5, 6,

7 or 8 wherein said enzyme is produced by a DNA construct comprising a DNA sequence encoding the enzyme.

10. A detergent composition according to claim 9 wherein the DNA sequence is as shown in the appended sequence listings ID#1 or ID#3.

11. A detergent composition according to claim 5, 6,

7 or 8 wherein said host cell is a strain of a fungus such as Tricloderuca or Aspergillus, preferably Aspergillus oryzae or Aspergillus niqer, or a yeqst cell belonging to a strain of Hansenula or Saccharomyces, e.g. a srrain of Saccachomyces cerevisae.

12. A detergent composition according to claim 5, 6,

7 or 8 wherein said host cell is a strain of a bacterium, e.g. Bacillus, Streptomyces or E. coli.

13. A detergent composition according to claim 1, 2, 3, 4, 5, 6, 7 or 8 wherein the water soluble cationic compound is selected from quaternary ammonium salts in which R₁ is C₁₂-C₁₄ alkyl and R₂, R₃ and R₄ are selected from methyl and hydroxyethyl groups.

14. A detergent composition according to claim 1, 2, 3, 4, 5, 6, 7 or 8 wherein the level of said watersoluble cationic compound is from 0.2 to 10%.

15. A detergent composition according to claim 1, 2, 3, 4, 5, 6, 7 or 8 further comprising anionic surfactants, wherein the molar ratio of the anionic surfactant to the water soluble quaternary ammonium compound is greater than 1:1.

16. A detergent composition according to claim 1, 2, 3, 4, 5, 6, 7 or 8 which is a detergent additive, in the form of a non-dusting granulate or liquid.

17. A detergent composition which comprises a detergent additive according to claim 1, 2, 3, 4, 5, 6, 7 or 8.

18. A detergent composition according to claim 17 which is in granular form, compact granular form or liquid form.

19. A laundry process comprising contacting fabrics with a detergent composition according to claim 1, 2, 3, 4, 5, 6, 7 or 8, wherein the cellulase being added at levels of from 0.005 to 40 mg enzyme protein/liter of wash solution.