CA2263430A1 - Detergent compositions comprising antibody controlled cellulolytic activity - Google Patents

Abstract

The present invention relates to detergent compositions comprising a cellulase-directed antibody and cellulase in order to prevent potential tensile strength loss related to the hydrolytic activity of cellulase on cellulose substrates while maintaining the desired benefits from the use of cellulase.

Description

DETERGENT COMPOSITIONS COMPRISING ANTIBODY
CONTROLLED CELLULOLYTIC ACTIVITY

FIELD of the INVENTION

The present invention relates to laundry detergent compositions comprising a cellulase-directed antibody and a cellulase in order to prevent potential tensile strength loss related to the hydrolytic activity of cellulase on cell~llose s~ sl,ates while maintaining the desired benefits from the use of cell~ se.

BACKGROUND of the INVENTION

An important part of the system which protects ve, lebrales against infections by bacteria and viruses is the humoral immune system. Specialised cells present in bone marrow, Iymphoid tissues and blood, produce immunoglobulins (antibody) which appear in response to the introduction of a micro- or macromolecu'c foreign to that body and bind the body-foreign structureinitialin~ its destruction. Such a body-foreign molec~lle is called an antigen. The antibody is c~i(ected against the antigenic determinant or hapten of the anligene.g. an amino acid sequence, parts of oligos~ccharides, polysaccharides, lipopolysaccharides, glycoproteins, lipoproteins, lipoteichoinic acids.

The specific antibodies generated in this manner can combine with the a-)ligen which elicited their fo""dtion to form an antigen-antibody complex.
Antibody molecules have binding sites that are very specific for and complementary to the structural features of the antigen that induced their formation.

... ..

This highly specific antigen-antibody recognition and binding has found several applications such as recognition agent, binding agent or carrier agent in various domains such as analytical chemistry, therapeutic treatment, health and beauty care.

EP 479 600, EP 453 097 and EP 450 800 relate to the use of antibodies or fragments thereof for the delivery of active ingredients to a target site. EP 481 701 discloses l~alment compositions for topical application containing micro~ps~ ~les which enclose a beneficial agent at a target location, the microcapsules having an antibody or antibody fragment specific to the target location or a lectin.

W092/04380 describes reshaped human antibody or reshaped human antibody f~a~~.nents having specificity for human polymorphic epithelial mucin to be used in the treatment or diagnosis of cancer. The use of Epstein-Barr virus specific polypeptides for the prod~ction of antibodies and the diagnostic and treatment of said dise~se is disclosed in W094/06470.

Oral compositions comprising a~ Itibodies as anti-caries or periodontal ~lise~ses treatment have been extensively described in WO95/01155, WO95/00110, WO95/10612, EP 140 498, GB 2 151 923, GB 2 176 400, GB 2 167 299, DE 4324859, US 5 401 723 and EP 280 576.
EP 673 683 and EP 542 309 rlisclose hair cosmetic compositions containing an a.,libody to hair or hair extract, obtained from egg yolk or poultry immunised with the hair or hair extract and a polymer emulsion to provide redlJc~d hair damage, softness, moistened feel and smoothness, said co",position being adsorbed only onto a specified part of the hair.

Comrosi(ions containing antagonists (tyrphostins or al,liho~iqs) against epidermal and transforming growth factors, suitable for use in treatment of acneare described in WO9~/24896.

The use of antibodies in the overall detergency context has been sugyested in Unilever Researchprijs "Molecule zoekt partner" 1992 wherein modified antibodies directed to specific stains are proposed to be used in bleaching process.

The production of antibodies by hyperimmunisation of mammals such as a cow with a vaccine derived from E. coli bacteria is described in EP 102 831. EP
400 569 discloses a method for ~reparing vaccine composition for dental caries in nasal drops comprising an antigen produced by integraling a protein antigen-expressing gene into the chromosomal gene of a streptococcus mutants GS-5 strain. W094/25591 discloses the prod~lr,tion of antibodies or functionalised fragments thereof derived from heavy chain immunoglobulins of camelidae.

Detergent compositions include nowadays a complex combination of active ingredients which fulfill certain specific needs: a su~raclant system, enzymes providing cleaning and fabric care benefits, bleaching agents, a buildersystem, suds su,upressors, soil-suspending agents, soil-release agents, optical brighteners, softening agents, dispersants, dye transfer inhibition col"pounds, abrasives, bactericides, perfumes, and their overall ,I)e~ro~ ance has indeed improved over the years.

In particular, current detergent formulations generally include dete,genl enzymes and more specifically cell~ ses The activity of cellulase is one in which cellulosic fibres or suL,slrales are ~tl~cked by the eellul~se and depending on the particular function of the cellulase, which can be endo-or exo cellulase and the respective hemicell~l~ ses.
The cellulose structures are depolymerized or cleaved into smaller and thereby more soluble or dispersible fractions. This activity in particular on fabrics provides a cleaning, rejuvenalion, softening and generally improved handfeel chara.,t~ri~lics to the fabric structure.

In the detergenl field cellul~ses ,~e,ro~",i.~g in a typical deterge"l wash environ",ent are available with an activity at which the desired cellul~se pelror",al1ce is reached prior to the end of a wash-cycle. However, since the cellulase continues to react, even after having provided the desired performance, cleavage of the cellulose will continue. Therefore, there is a potential risk oftensile slre"glh loss.
It should be noted however, that tensile strength loss of fabric is also an unavoidable result of mechanical action due to use/wearing and may further W O 98/07823 PCTrUS97/llS44 result from damage by a bleaching component in the laundry process especially if the fabric is contaminated with metal compounds.

It has now been surprisingly found that the application of antibodies raised against the cellulolytic enzyme prevents the occurrence of undesirable residual cellulolytic activity. The cellulolytic activity can be fully controlled during the cleaning process so that the negative effects due to overexposure to the cellulolytic enzyme can now be avoided.

It is therefore an object of the present invention to provide a cellulase-containing laundry detergent composition preventing potential tensile s(lellyltlloss related to the hydrolytic activity of cellulase on cellulose substrates while maintaining the desired benefits from the use of cellulase.

The above need has been met by specific laundry detergent co"~positions comprising a cellulase and an antibody directed against said cellulolytic enzyme.

Cellulase exhibiting exceptionally high activity have been discloseJ in the context of compact detergents in W0-92-13057 in the context of quaternary an""onium softening compounds in EP-A~95 554 and in the context of softening clay in a deterge,-t composition in EP-A495 258 and EP-A-177 165. Cellulase as such with exceptionally high activity has been disclosed in WO 91/17243.
Recognition of the potential tensile strength loss of cellulase has been repG,ted in several p! IhliC~t;l:~ils. For example Japanese application J~2-310754 discloses particular cellul~ses having a specific so-called non-de~rading index.Japanese arpli.~~tion J~3-134830 discloses deterge"~ compositions for clothing containing a cellulase which has a non-destructive index and US 4 978470 discloses a detergeot composition for closing containing cellul-lse enzyme with a "non-degrading index" of less than 500.

SUMMARY of the INVENTION

The present invention relates to the use of laundry deterge. ,t compositions in household fabric treatment machines and handwash treatments.
The laundry detergent composition comprises a cell~ se enzyme and an antibody raised against the cellulolytic enzyme in order to prevent potential W O g~ 3 PCTrUS97/11544 tensile strength loss related to the hydrolytic activity of cellulase on cellulose substrates while maintaining the desired benefits from the use of cellulase.

DETAILED DESCRIPTION of the INVENTION

ANTIBODY

An essential element of the detergel)l coi),positions of the presenl invention is an antibody.

The immunoglobulins are classified into 5 cl~sses, respectively: IgM, IgG, IgA, IgD and IgE. Preferred cl~sses of immunoglobulins are the IgG and IgA.
Secretory slgA which are found into human excreted body fluids such as milk, saliva, respiratory and intestinal fluids are especi?'ly designed to survive in said secretions, they have enhanced binding characteristics and are resistant to proteolytic hydrolysis.

The antibody which may be monoclonal or polyclonal or an antib~Jy fragment, may be generated by techniques conventional in the art, for example by using reco",binant DNA techniques allowing to produce antibodies vciriants with new prope, lies: reduced immunogenecity, enhanced affinity, altered size, ...
Specific binding may also be used. Prefer.ed for the purpose of the present invention is a ,.,Gnoclonal alltibody, more prefe"ed is a fragment thereof. These r, ag,n~n~s may be similarly generated by conventional techniques such as enzymatic digestion by papain or pepsin, or using recoi"l~inant DNA techniques.
Antibody r,ag,nenls may also be ~yerlerated by conventional recombinant DNA
techniques. Antibodies and antibodies' r,ay,ne,)ls may be humanised, such as described in Meded. - Fac. Landbouwkd. Toegepast Biol. Wet. (Univ. Gent) (1995), 60(4a, ForumforApplied Bioteel.nology, 1995, Part 1), 2057-63.

Heavy and light chains are indeed composed of constant and variable domains. In the organis.ns producing immunoglobulins in their natural state the co,)stant doi"ains are very important for a number of functions, but for many ~ppli~tions in industrial processes and products their variable domains are W O 98/078~3 PCTrUS97111544 sufficient. Consequently many methods have been described to produce antibody fragments.

Antibody fragments which are used may be a Fab, a Fv, a scFv or any other fragment having similar binding properties. Preferred routes to antibodiesfragments are through recombinant DNA technology, so that the fragment is expressed by a genetically transformed organism.

Antibodies and antibody frayments produced by recombinant DNA
technology do not need to be identical to fragment of antibodies produced in vertebrates, having nevertheless the same binding properties evaluated by their Krn, Ki and Kcat. For instance they may include sequences of amino acids andlor glycosylations which differ from those found in antibodies produced in other ways, especi?'ly sequences at the end of fragments. Somewhat ana'Qgo~ ~sly, antibody fragments produced through recombinant DNA tecl " lologymay include extra amino acid sequences at their termini which have no counterpart in antibodies produced in other ways.

A related possibility is that a binding agent for use in this invention is a natural or synthetic polymer which mimics the specific binding activity of a natural antibody's complementary region(s). Such a polymer is for example a polypeptide or a polymer i",p,i-,ling (Angew. Chem. Int. Ed. Engl. 1995, 34, 1812-1832).

The usual method for the production of antibodies may be adopted in immunising ",a,n,)~als or poultry with the corresponding antigens. As "~ammals to be immunised, mice, rabbits, goats, sheep, horses, cows, etc. may be used. The antibody (imm~,noglobulin r,action) may be separated from the antiserum, the milk or the eggs according to the ordinary antibody purification method including salting-out method, polson extraction, gel-filtration chromatography, ion-e~.cl,a"ge chromatog~apl,y, affinity chromatography and the like, the salting-out method using a,nmonium sulfate to produce the precipitates, followed by dialysing the ~,recipilates againsl physiological saline to obtain the purified precipitates as the antibody.

Plants are also capable of synthesising and assembling every kind of antibody molecule and allow a large scale of production of antibodies as ~ described in Tibtech. Dec 19g5, Vol 13, pp 522-527; Plant Mol. Biol., 26, pp 1701-1710, 1994 and Biotechnol. proj. 1991, 7, pp 455461 and in US patent 5, - 202,422. Antibodies can also be produced into microorganisms such as E. coli or S. cerevisiae via biofermentation process as illustrated in the EP patent 667394.

Techniques for the production of anlibGdy fragments are well known in the literature: Saiki et al. Science 230 1350-54 (1985); Orlandi et al. PNAS USA 86 3833-7 (1989); W089/09825; EP 368 684; WO 91/08482 and W094125591.

The drawbacks due to prolonged activity of the enzyme can be avoided by an effective control of the enzymatic activity through the introduction of the specirically conesponding antibody. Such antibodies can be either polyclonal -directed to the whole enzyme structure - or ",onoclonal - directed to specific epitopes of the enzyme activity controling regions of the enzyme structure of the enzyme core or s-6sl,ate binding domain. Antibodies raised against specific enzyme can effectively deactivate the enzyme by the antibody-antigen binding in or very near the active site. The formation of such complex leads to the enzyme deactivation and could be explained by the distortion of the 3-dimensional structure and/or steric hindla,)ce at the substrate clefl. The deactivation of the enzyme can also be achieved by the precipitation of the complex anlibody-antigen from the wasl,ing solution. Due to very high specificity and efficiency of the ~nti~GJy-antigen interaction, no other cJetergent active is thereby affected.

The cell~ se~i, ected antibodies are preferably co,)~prised in the detergent composition of the present invention at a level of from 10E~% to 10E+1% by weight of total co",position. In some instances, antibodies raised against a specific cellulase have the capability of binding other cellulases of high structural similarily, providing cross-reactivity. Typically, a molecular ratio of cellulase-directed antibody to cellulase will be of 100:1 or lower, pr~rerably of 50:1 or lower. For ",o"oclor,al antibodies or r,aS~",e-)ts thereof, the molecular ratio of cellulase-directed antibody to cellulase will be generally of 50:1 or lower, preferal~ly of 20:1 or lower.

W O 9X/'~23 PCT~US97/11544 The antibodies raised against the cellulase are released in the wash solution after a lag-period aliowing to deliver excellent performance benefits to be achieved by the end of the wash process.

Therefore, the antibodies are preferably incorporated into a release agent in order to control their release timing and rate in the wash solution. The physical form of the antibody-containing release agent is adapted to the physical form ofths corresponding detergent or additive.

For granular and powder detergent and cleaning products, the antibodies and release agents can be contained in a granulate. Said antibody granulate can suitably contain various granulation aids, binders, fillers, plasticizers, lubricants, cores and the like. Examples thereof include cellulose (e.g. cellulosic fibers or in microcrystalline form), cellulose derivatives (CMC, MC, HPC, HPMC), gelatin, starch, dextrins, sugars, polyvinylpyrrolidone, PVA, PEG, salts (e.g. sodium sulfate, calcium sulfate), titanium dioxide, talc, clays (kaolin or bentonite)and nonionic surfactants. Other materials of relevance for incor,l~oraliol, in the granulate are described in EP 304 331.
The release agent may be, for example, a cGaliog. Said coali"g protects said granulates in the wash environment for a certain period of time. The coaling will normally be arplied to said granulates in an amount in the range of 1% to 50% by weight (c~'c~ ted on the basis of the weight of the unco~led, dry granulate), preferably in the range of 5 % to 40 % by weight. The amount of coating to be applied to said granulates will depend to a considerable extent onthe nature and co,n~osilion of the desired coatil-g, and to the kind of protection said coati-,y should offer to said granul~tes. For example, the thickness of said coati. ~y or a multi-layered coating applied onto any of the above granulates may determine the period in which the content of said granulates is released. A
possible multi-layered coating may be a coating in which, for example, a fast release coating is applied over a slow release coating.
Also co-granulates can be constructed containing in the outer layer the detergent enzyme and a fast releasing agent and in the~inner core, the antibody and a slow releasing agent.

Suitable release coatings are coatings which give rise to release of the contents of antibody-containing granulates under the conditions prevailing during W O 98/07823 PCT~US97/11544 the use thereof. Thus, for e~ample, when a preparation of the invention is to beintroduced into a washing liquor containing a washing detergent (normally comprising, e.g., one or more types of surfactants~, the coating should be one which ensures the release of the contents of said granulates from the release agent when it is introduced into the washing medium.

Preferred release coating are coatings which are subst~rltially insoluble in water. Release coatings which are appropriate in washing media may suitably comprise 5!lhSPrlCeS selected from the following: cellulose and cellulase derivatives, PVA, PVP, tallow; hydrogenated tallow; partially hydrolyzed tallow;fatty acids and fatty alcohols of natural and synthetic origin; long-chain fatty acid mono-, di- and triesters of glycerol (e.g. glycerol monostearate); ethoxylated fatty alcohols; latexes; hydrocarbons of melting point in the range of 50~0~C; and waxes. Melt-coating agents are a p~efer.ed class of fast or slow release coatingagents which can be used without dilution with water. Reference may be made to Controlled Release Systems: Fabrication Technology, Vol. I, CRC Press, 1988, for further information on slow release coating.

- Coatings may suitably further comprise s~ ~hsl~nces such as clays (e.g. kaolin), titanium dioxide, pign,enls, salts (such as calcium carbonate) and the like. Theperson skilled in the art will be aware of further coating constituents of relevance in the present invention.

In liquid ~etergent coi"rssilions, the antibody can be incor,uoraled as a dispersio., of pallicl~s containing in A.tditioll to the antibo.ly, a release agent.
The a~tiboJy can be present in a liquid or solid form. Suitable particles co"sisl of a porous hyJ~upl,obic material (e.g., silica with an average pore diameter of 500 A.)g~lroi" or higher) containing into the pores a solution of antibodies and a su,raclant as described in EP 583 512 of Surutzidis A. et al.
The release agent might be a coatiny which prolects said particles in the wash cycle for a certain period of time. The coating is preferably a hydlophobic coating material such as a hydrophibic liquid polymer. Said polymer can be an organo polysiloxane oil, aller"alively a high oleou~ weight hydroca, L,on or water insoluble but water permeable polymeric material such as carboxymethylcellulose, PVA, PVP. The polymer properties are selected to achieve a suitable release profile of the antibody in the wash solution.

W O 98/07823 PCTAUS97/115~4 THE CELLULASE ENZYME

The cellulases usable in the present invention include both bacterial or fungal cell~ se. Origin can further be mesophilic or extremophilic (psyohro~c hilic, psychrotlophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.).
Purified or non-purified forms of these enzymes may be used. Also included by definition, are mutants of native enzymes. Mutants can be obtained e.g. by protein and/or genetic engineering, chemical and/or physical modifications of native enzymes. Common practice as well is the expression of the enzyme via host organisms in which the genetic material responsible for the production of the enzyme has been cloned.

Preferably, they will have a pH optimum of between 5 and 12 and an activity above 50 CEVU (Cellulose Viscosity Unit). Suitable cellulases are ~isclosed in U.S. Patent 4,435,307, Barbesgoard et al, J61078384 and W096/02653 which discloses fungal cellulase produced respectively from Humicola insolens, Tricoderma, Thielavia and Sporotrichum. Suitable cellul~ses are also disclosed in GB-A-2.075.028; GB-A-2.095.275, GB-A-2.095.275, DE-OS-2.247.832 and W095/26398.

Examples of cell~ se components which may be usable in the present invention are:
A cello~ichydrolase component which is immu.)oreactive with an a"tiboJy raised against a highly purified 70kD cellobiohydrolase (EC 3.2.1.91) derived from Hulll.c~l~ insolens, DSM 1800, or which is a homolQgue or derivative of the 70kD cqllobiohydrolase exhibiting cellulase activity, or an endoglucanase co"~ponent which is immunoreactive with an antibody raised against a highly purified 50kD endoglu~nase derived from Humicola insolens, DSM 1800, or which is a ~,o",clo~ue or derivative of the -50kD e"doglucanase exhibiting cellulase activity; a prefened el,doglucanase cGIoponel)l has the amino acid sequence disolosed in PCT Patent Application No. W091/17244, or an endoglucanase component which is immunoreactive with an antibody raised against a highly purified -SOkD (appa,ent molecular weight, the amino acid col"posilion cor,aspol)ds to 45kD with 2n glycosylation sites) endoglucanase derived from Fusarium oxysporum, DSM 2672, or which is a homologue or CA 02263430 1999-02-ll W O 98/07823 PCT~US97/11544 derivative of the -50kD endoglucanase exhibiting cellulase activity; a preferredendoglucanase component has the amino scid sequence disclosed in PCT
Patent Application No. WO91/17244, or any of the cellulases disclosed in the published European Patent Application No. EP-A2-271 004, the cellulases having a non-degrading index (NDI) of not less than 500 and being alkalophilic cellulases having an optimum pH not less than 7 or whose relative activity at a pH of not less than 8 is 50% or over of the activity under optimum conditions when carboxy methyl cellulose (CMC) is used as a substrate, or an endoglucanase component which is immunoreactive with an antibody raised against a highly purified -43kD endoglucanase derived from Humicola insolens, DSM 1800, or which is a homologue or derivative of the -43kD endoglucanase exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. WO 91/17243, or an endoglucanase component which is immunoreactive with an antibody raised against a highly purified -60kD endoglu~-~nase derived from Bacillus lautus, NCIMB 40250, or which is a homologue or derivative of the -60kD
endoglucanase exhibiting cellulase activity; a preferred endoglucanase component has the amino acid seguence disclosed in PCT Patent Application No. WO 91110732. See also the celllJIases described in W091/21081. Other suitable cellulases for fabric care and/or cleaning ,l~r~pe~ties are desc,ibed in W096/34092, WO96117994 and WO95124471.

Other suitable celllll~ces are the EGIII cellulases from Trichoderma longibrachiatum described in WO94/21801, Genencor, published Septe"ll,er 29, 1994. Fspeci~'ly suitablQ cellul~ses are the cell~ ses having color care benefits.
Examples of such cellulases are cellulases described in European patent application No. 91202879.2, filed November6, 1991 (Novo).
According to the present invention, prerer,ed cellulases are those as described in Danish Patent Application 1159/90 or PCT patent application WO91/17243 which is also known as Carezyme(TM) available from Novo Nordisk A/S in Bagsvaerd, in Denmark. The cellulase preparation described in these p~Jhli~liG"s and the Carezyme(TM) consistent with this description, can consist essenlially of a î ,o,.,ogeneous endoglucanase component, which is immunoreactive with an anti-body raised against a highly purified 43 kD cellulase derived from Hulll ~cl~ Insulens, DSM 1800, or which is homologous to said 43 kD endoglucanase. An alternative screening for appro~riale cell~ ses for use in .

W O 9~ 3 PCT~US97/11544 the laundry detergent composition accGrding to the present invention is the method specified in EP-A495 258 or more specifically in EP-A-350 098.

For industrial production of the cellulase preparation herein, however, it is prerer,ed to employ recombinant DNA techniques or other techniques involving adjustments of fermentations or mutation of the microorganisms involved to ensure overprodllction of the desired enzymatic activities. Such methods and techniques are known in the art and may readily be carried out by persons skilled in the art. common practice as well is the expression of the enzyme in host organisms in which the genetic material responsible for the production of the enzyme has been cloned.

Deterqent components The detergent compositions of the invention may also contain additional deteryer,t components. The precise nature of these additional components, and levels of incorporation thereof will depend on the physical form of the composition, and the nature of the cleaning operation for which it is to be used.

The detergent compositions according to the invention can be liquid, paste, gels, bars, tablets, powder or granular forms. Granular compositions can also be in "compact" form, the liquid compositions can also be in a "concer,llated" form.

The con,~osilions of the invention may be formulated as hand and machine laundry detergent compositions including Jaundry additive comrositions and co""~ositions suitable for use in the soaking and/or pretreatment of stainedfabrics, rinse added fabric softener compositions. Such compositions can providefabric cleaning, stain removal, whiteness maintenance, softening, color a~,pearance and dye t~a,)sfer inhibition.

When formulated as compositions suitable for use in a laundry machine washing method, the compositions of the invention preferably contain both a surfactant and a builder compound and additionally one or more detergent cG")~,o"ents l~referably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime-soap W O 9~d23 PCT~US97/11544 dispersants soil suspension and anti-redeposition agents and corrosion inhibitors. Laundry compositions can also contain softening agents as additional detergent components.

The compositions of the invention can also be used as detergent additive products comprising a cellulase-directed antibody and will be added to a conventional detergent cellu~qse-containing composition. The detergent additives can also comprise both the cellulase and cell~ se-directed antibody.
Such additive products are intended to supplement or boost the peiror",ance of conventional detergent compositions preferably comprise up to 50% antibodies by weight of total composition.

If needed the density of the laundry detergent compositions herein ranges from 400 to 1200 g/litre preferably 600 to 950 g/litre of composition measured at 20~C.

The "compact" form of the compositions herein is best reflected by density and in terms of composition by the amount of inorganic filler salt; i"organic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions the filler salts are present in s~bst~ntial amounts typically 17-35% by weight of the total composition.
In the co",pal;t compositions the filler salt is ,t~resenl in amounts not exceeding 15% of the total composition preferably not exceeding 10% most prert:rably not exceeding 5% by weight of the composition.
The inorganic filler salts such as meant in the present co"~positions are selecte~ from the alkali and alkaline-earth-metal salts of sulphates and chlorides.
A prefer,ed filler salt is sodium sulphate.

Liquid detergent compositions according to the presenl invention can also be in a "concer,lraled form" in such case the liquid deterge"t compositions accordi.)g the present invention will contain a lower amount of water co"~pared to conventional liquid detergents.
Typically the water coi ,te"t of the concer,t~ ated liquid detergen~ is ~,rbterably less than 40% more preferal~ly less than 30% most preferably less than 20% by weight of the detersJen~ composition.

SL~rfactant system The detergent compositions according to the present invention comprise a surfactant system wherein the surfactant can be selected from nonionic and/or anionic and/or cationic andlor ampholytic and/or zwitterionic and/or semi-polar surfactants.

The surfactant is typically present at a level of from 0.1% to 60% by weight.
More preferred levels of incorporation are 1% to 35% by weight most preferably from 1% to 30% by weight of detergent compositions in accord with the invention.

The surfactant is preferably formulated to be compatible with enzyme components present in the composition. In liquid or gel compositions the surfactant is most preferably formulated such that it promotes or at least does not degrade the stability of any enzyme in these compositions.

Prefer,ed surfactant systems to be used accordi"g to the present invention comprise as a surfactant one or more of the nonionic and/or anionic sul~acta"ls described herein.

Polyethylene polypropylene and polybutylene oxide condensales of alkyl phenols are suitable for use as the nonionic s- l ~actant of the surfactant systems of the present invention with the polyethylene oxide condensates being preferred. These compounds include the condensation products of alkyl phenols having an alkyl group conlai"i,1-J from about 6 to about 14 carbon atoms preferably from about 8 to about 14 carbon atoms in either a straight-chain or ~ra"~;l,ed chain configuration with the alkylene oxide. In a preferled embodiment the ethylene oxide is present in an amount equal to from about 2 to about 25 moles more preferal,ly from about 3 to about 15 moles of ethylene oxide per mole of alkyl phenol. Co"""ercially available nonionic surfactants of this type include lgepalTM C0~30 marketed by the GAF CGr~,oralion; and TritonTM X-45 X-1 14 X-100 and X-102 all marketed by the Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g. alkyl phenol ethoxylates).

CA 02263430 1999-02-ll W O 9~ /o~3 PCTrUS97/11544 The condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention.The alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohois having an alkyl group containing from about 8 to about 20 carbon atoms, more preferably from about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide and most preferably from 2 to 5 moles of ethylene oxide per mole of slcohol are present in said condensation products. Examples of co,nr,lercially available nonionic surfactants of this type include TergitolTM 15-S-9 (the condensation product of C1 1 -C1 s linear alcohol with 9 moles ethylene oxide), TergitolTM 24-L-6 NMW (the condensation product of C12-C14 primary alcohol with 6 moles ethylene oxide with a narrow molQc~ r weight distribution), both marketed by Union Carbide Corporation; NeodolTM 45-9 (the condensation product of C14-C1~ linear alcohol with 9 moles of ethylene oxide), NeodolTM 23-3 (the condensation product of C12-C13 linear alcohol with 3.0 moles of ethylene oxide), NeodolTM 45-7 (the condensation product of C14-C1s linear alcohol with 7 moles of ethylene oxide), NeodolTM 45-5 (the condensation product of C14-C1s linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical CGIIIPanY, KYrOTM EOB (the conJensation product of C13-C1s alcohol with moles ethylene oxide), marketed by The Procter & Gamble Col-"~any, and Genapol LA 030 or 050 (the cGndensdlion product of C12-C14 alcohol with 3 or ~ moles of ethylene oxide) marketed by Hoechst. Preferred range of HLB in these products is from 8-1 1 and most preferred from 8-10.

Also useful as the nonionic su. raclant of the su. ractant systems of the present invention are the alkylpolysaccharides disclosed in l:l.S. Patent 4,565,647, Llenado, issued January 21, 1986, having a hycJ,opl,obic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units. Any reducing saccharide containing 5 or 6 carbon atoms can be used, e.g., glucose, g~-ctose and gal~ctosyl moieties can be substituted for the glucosyl moieties (optionally the .. ..... . ~ .. ~

W O 98/07823 PCT~US97/11544 hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or g~l~ctose as opposed to a glucoside or galactoside). The intersaccharide bonds can be, e.g., between the one position of the additional saccharids units and the 2-, 3-, 4-, and/or 6- positions on the preceding saccharide units.
The preferred alkylpolyglycosides have the formula R20(CnH2nO)t(9lycosyl)x wherein R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl groupscontain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attach" ,el ,t at the 1 -position). The additional glycosyl units can then be attached between their 1-position and the preceding glycosyl units 2-, 3-, 4- and/or 6-position, prefera~ly predominately the 2-position.

The condensation products of ethylene oxide with a hydrophobic base for",ecl by the condensation of propylene oxide with propylene glycol are also suitable for use as the addilio,)al nonionic surfactant systems of the present invention.The hydl-ophobic portion of these co",pounds will preferably have a molecular weight of from about 1500 to about 1800 and will exhibit water insolubility. Theaddition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water soluhility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50~/0 of the total weight of the conde"sation product, which corresponds to condensation with up to about 40 moles of ethylene oxide. Examples of co",pounds of this type include certain of the commercially-available PlurafacTMLF404 and PluronicTM surfactants, marketed by BASF.

Also suitable for use as the nonionic surfactant of the nonionic sulractant system of the present invention, are the condensation products of ethylene oxide CA 02263430 l999-02-ll W O ~ o23 PCT~US97/11544 with the product resulting from the reaction of propylene oxide and ethylenediamine. The hydrophobic moiety of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of from about 2500 to about 3000. This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11,000. Examples of this type of nonionic surfactant include certain of the commercially available TetronicTM compounds, marketed by BASF.
Prefer~ed for use as the nonionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide, alkylpolysaccharides, and mixtures thereof. Most preferred are Cg-C14 alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and Cg-C1g alcohol ethoxylates (preferably C10 avg.) having - from 2 to 10 ethoxy groups, and mixtures thereof.

Highly preferred nonionic surfactants are polyhydroxy fatty acid amide SIJI ract~nts of the formula.

R2 - C - N - Z, Il I
o R1 wherein R~ is H, or R1 is C1~ hydrocdrl~yl, 2-hydroxy ethyl, 2-hydroxy propyl ora mixture thereof, R2 is Cs 31 hyJrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linear hy~JIocdrL.yl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof. rreferably, R1 is methyl, R2 is a straight C11 15 alkyl or C16 18 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, l~ctose, in a reductive amination reaction.

Suit~hle anionic su~racta"ts to be used are linear alkyl benzene sulfonate, alkyl ester sulfonate s~l,ractai)ts including linear esters of Cg-C20 carboxylicacids (i.e., fatty acids) which are sulfonated with g~seous SO3 according to '~he Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329. Suitable . . .

CA 02263430 1999-02-ll W O 98/07823 PCT~US97/11544 starting materials would include natural fatty substances as derived from tallow, palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especially for laundry applications, comprise alkyl ester sulfonate surfactants of the structural formula R3 - CH - C - oR4 I

wherein R3 is a Cg-C20 hydloca,Lyl, preferably an alkyl, or combination thereof,R4 is a C1-C6 hydrocarbyl, preferably an alkyl, or combination thereof, and M isa cation which forms a water soluble salt with the alkyl ester sulfonate. Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethanolamine, and triethanolamine. Preferably, R3 is C10-C16 alkyl, and R4 is methyl, ethyl or isopropyl. Especially preferred are the methyl ester sulfonateswherein R3 is C10-C16 alkyl.

Other suitable anionic surfactants include the alkyl sulfate su,ra~;ta"ts which are water soluble salts or acids of the formula ROSO3M wherein R preferably is a C10-C24 hydrocarbyl, preferab~y an alkyl or hydroxyalkyl having a C10-C20 alkyl co,npo-)ent, more preferably a C12-C1g alkyl or hydroxyalkyl, and M is H or a cation, e.g., an alkali metal cation (e.g. sodium, pot~ssi~ ~m, lithium), or ammonium or substituted ar"moi-ium (e.g. methyl-, di",ett,yl-, and trimethyl ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and qua~erna,y ammonium cations derived from alkylamines such as ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like). Typically, alkyl chains of C12-C16 are preferred for lower wash temperatures (e.g. below about 50~C) and C16 18 alkyl chains are prefer, ed for higher wash temperatures (e.g. above about 50~C).
Other anionic su,racla"ts useful for detersive purposes can also be included in the detergent ccsn,l,ositions of the present invention. These can include salts (including, for example, sodium, potassium, a",monium, and substituted amrnonium salts such as mono-, di- and triethanolamine salts) of soap, Cg-C22 WO 98/07823 PCTIUS97/llS44 primary of secondary alkanesulfonates, Cg-C24 olefinsulfonates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No.
1,082,179, Cg-C24 alkylpolyglycolethersulfates (containing up to 10 moles of ethylene oxide); alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-acyltaurates, alkyl succ;namates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated C12-C18 monoesters) and diesters of sulfosuccinates (especi~lly saturated and unsaturated C6-C12 diesters), acyl sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of alkylpolyglucoside (the nonionic nonsulfated compounds being described below), branched primary alkyl sulfates, and alkyl polyethoxy carl,oxylates suchas those of the formula RO~CH2CH20)k-CH2C00-M+ wherein R is a Cg-C22 alkyl, k is an integer from 1 to 10, and M is a soluble salt-forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil.

Further exa",ples are described in "SurFace Active Agents and Delerg~nts"
(Vol. I and ll by Schwartz, Perry and Berch). A variety of such surfactants are also generally disclosed in U.S. Patent 3,929,678, issued December 30, 1975 to Laughlin, et al. at Column 23, line 58 through Column 29, line 23 (herein incor~,orated by reference).
When incl~Jde~ r~in, the laundry ~etergenl compositions of the present invention typically cu,-",rise from about 1% to about 40%, ,~)referably from about 3% to about 20% by weight of such a"ionic Sl" ractanls.

Highly ~r~fer-ed anionic surfactants include alkyl alkoxylated sulfate surfactants hereof ars water soluble salts or acids of the formula RO(A)mS03M
wherein R is an uns~Jhstihlted C10-C24 alkyl or hydroxyalkyl group having a C10-C24 alkyl co,nponent, ~re~rably a C12-C20 alkyl or hydroxyalkyl, more ~referably C12-C1g alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is grealer than zero, typicaîly between about 0.5 and about 6, more prefer~bly between about 0.5 and about 3, and M is H or a cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, CA 02263430 1999-02-ll etc.), ammonium or substituted-ammonium cation. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and those derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. Exemplary surfactants are C12-C18 alkyl polyethoxylate (1.0) sulfate (C12-C18E(1.o)M)l C12-C1g alkyl polyethoxylate (2.25) sùlfate (C12-C18E(2.25)M), C12-C1g alkyl polyethoxylate (3.0) sulfate (C12-C1gE(3.0)M), and C12-C1g alkyl polyethoxylate (4.0) sulfate (C12-C1gE(4.0)M), wherein M is conveniently selected from sodium and potassium.

The detergent compositions of the present invention may also contain cationic, ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic and/or anionic surfactants other than those already described herein.

Cationic detersive surfactants suitable for use in the detergent compositions ofthe present invention are those having one long-chain hydrocarb~l group.
Examples of such cationic s~" ra~:tants include the ammonium surfactants such asalkyltrimethylar"r"onium halogenides, and those surfactants having the formula:

[R2(oR3)y][R4(0R3)y]2R5N+X~

wherein R2 is an alkyl or alkyl benzyl group having ftom about 8 to about 18 carbon atoms in the alkyl chain, each R3 is selected from the group consisting of -CH2CH2-, -CH2CH(CH3)-, -CH2CH(CH2OH)-, -CH2CH2CH2-, and mixtures thereof; each R4 is selected from the group consisting of C1-C4 alkyl, C1-C4 hydroxyalkyl, benzyl ring structures formed by joining the two R4 groups, -CH2CHOH-CHOHCOR6CHOHCH2OH wherein R6 is any hexose or hexose polymer having a molec~ r weight less than about 1000, and hydrogen when y is not 0; R5 is the same as R4 or is an alkyl chain wherein the total number of carbon atoms of R2 plus R5 is not more than about 18; each y is from 0 to about 10 and the sum of the y values is from 0 to about 15; and X is any compatible anion.

CA 02263430 l999-02-ll W O 98/07823 PCT~US97/11544 Quaternary ammonium surfactant suitable for the present invention has the formula (I):

R~

Formula I
whereby R1 is a short chainlength alkyl (C6-C10) or alkylamidoalkyl of the formula (Il):
C6~¢N~ ~

Formula ll y is 2~, preferably 3.
whereby R2 is H or a C1-C3 alkyl, whereby x is 04, prererably 0-2, most preferably 0, whereby R3, R4 and R5 are either the same or different and can be either a short chain alkyl (C1-C3) or alkoxylated alkyl of the formula lll, whereby X~ is a counterion, preferably a halide, e.g. chloride or methylsulfate.

H
Formula lll R6 is C1-C4 and z is 1 or2.

Preferred quat a,nmonium surfactants are those as defined in formula I
whereby R1 is Cg, C10 or mixtures thereof, x=o, R3, R4 = CH3 and R5 = CH2CH2~H

Highly IJreferred cationic surfactants are the water-soluble quatemary ammonium compounds useful in the present composition having the formula:
R1 R2R3R4N+X- (i) .

CA 02263430 1999-02-ll WO ~ ID23 PCT~US97/11544 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 prefer,e~ alkyl chain length for R1 is C~2-C1s particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or OXO alcohols synthesis. Preferred groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X
may be selected from halide, methosulphate, acetate and phosphate ions.
Examples of suitable quaternary ammonium compounds of formulae (i) for use herein are:
coconut trimethyl ammonium chloride or bromide;
coconut methyl dihydroxyethyl a",monium chloride or bromide;
decyl triethyl ai"r"ol,ium chloride;
decyl dimethyl hydroxyethyl a""l,o,lium chloride or bromide;
C12 15 dimethyl hydroxyethyl ammonium chloride or bromide;
coconut dimethyl hydroxyethyl ammonium chloride or bromide;
myristyl trimethyl ammonium methyl sulphate;
lauryl dimethyl benzyl ammonium chloride or bromide;
lauryl dimethyl (ethenoxy)4 a",mGnium chloride or bromide;
choline esters (compounds of formula (i) wherein R1 is CH2-CH2-~-C-C12_14 alkyl and R2R3R4 are methyl).
1~
o di-alkyl imi~ olines [compounds of formula (i)].

Other cationic surfactants useful herein are also described in U.S. Patent 4,228,044, Cambre, issued October 14, 1980 and in European Patent Arrlic~tion EP 000,224.

When incll~ded therein, the detergent compositions of the present invention typically comprise from 0.2% to about 25%, preferably from about 1% to about 8% by weight of such cationic sL-, rdctants.

Ampholytic surfactants are also suitable for use in the detergent compositions of the present invention. These su"~clants can be broadly described as aliphaticderivatives of secondary or tertiary amines, or aliphatic derivatives of CA 02263430 1999-02-ll W O 98/07823 PCTrUS97/11544 heterocyclic secondary and tertiary amines in which the aliphatic radical can bestraight- or branched-chain. One of the aliphatic substituents contains at leastabout 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic water-solubilizing group, e.g. carboxy, sulfonate,sulfate. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, lines 18-35, for examples of alllpholytic surfactants.

When included therein, the detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such ampholytic surfactants.

Zwitterionic surfactants are also suitable for use in detergent compositions.
These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quale,~,ary a"""o"ium, quaternary phosphonium or tertiary sulfonium compounds. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, line 38 through column 22, line 48, for examples of zwitterionic surfactants.

When included therein, the detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such zwillerio,)ic surfactants.

Semi-polar nonionic su-ractan~s are a special category of nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; water-solubl~ phosphine oxides contai"ing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups contai"ing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms.
Semi-polar nonionic deters~ent surfactants include the amine oxide surfactants having the formula W O 98/07823 PCT~US97/11544 R3(oR4)XN(R5)2 wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures therof containing from about 8 to about 22 carbon atoms; R4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof; x is from 0 to about 3; and each R5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups. The R5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to forma ring structure.

These amine oxide su,ractants in particular include C10-C18 alkyl dimethyl amine oxides and Cg-C12 alkoxy ethyl dihydroxy ethyl amine oxides.

When included therein, the detergent compositions of the present invention typically comprise from 0.2% to about 1~%, ,~referably from about 1% to about 10% by weight of such semi-polar nonionic surfactants.

The detergent composition of the present invention may further comprise a cosurfactant selected from the group of primary or tertiary amines.
Suitable primary amines for use herein include amines according to the formula R1NH2 wherein R1 is a C6-C12 prere.dbly C6-C10 alkyl chain or R4X(CH2)n, X
is -O-,-C(O)NH- or -NH- R4 is a C6-C12 alkyl chain n is between 1 to ~, prereral~ly 3. R1 alkyl chains may be straight or br~nc~,ed and may be interrupted with up to 12, preferably less than 5 ethylene oxide moieties.
Preferred amines according to the formula herein above are n-alkyl amines.
Suitable amines for use herein may be selected from 1-hexylamine, 1-octylamine, 1-decylamine and laurylamine. Other preferred primary amines include C8-C10 oxypropylamine, octyloxypropylamine, 2-ethylhexyl-oxypropylamine, lauryl amido propylamine and amido propylamine.

Suitable tertiary amines for use herein include tertiary amines having the formula R1 R2R3N wherein R1 and R2 are C1 -C8 alkylchains or W O ~8~'~7b23 PCTAUS97/llS44 - (CH2-CH--~O ~ H

R3 is either a C6-C12 preferably C6-C10 alkyl chain, or R3 is R4X(CH2)n, whereby X is -O-, -C(O)NH- or -NH- R4 is a C4-C12, n is between 1 to 5, preferably 2-3. Rs is H or C1-C2 alkyl and x is between 1 to 6 R3 and R4 may be linear or branched; R3 alkyl chains may be interrupted with up to 12, preferably less than 5, ethylene oxide moieties.

Preferred tertiary amines are R1R2R3N where R1 is a C6-C12 alkyl chain, R2 and R3 are C1-C3 alkyl or - (CH2- CH--~D ~ H

where R5 is H or CH3 and x = 1-2.

Also prefer,ad are the amidoamines of the formula:
o Rl--C--NH~ CH2 ~,--N~ R2 )2 wherein R1 is C6-C12 alkyl; n is 24, prefer~bly n is 3; R2 and R3 is C1-C4 Most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1 ~ecylamine, 1 -dodecylamine,C8-1 Ooxypropylamine, N coco 1-3diaminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl bis(hydroxyethyl)amine, coco bis(hydroxyehtyl)amine, lauryl amine 2 moles propoxylated, octyl amine 2 moles propoxylated, lauryl ~"~idopropyldimethylamine, C8-10 amidopropyldimethylamine and C10 amidopropyldi",etl ,ylamine.
The most preferred amines for use in the compositions herein are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Fspeci~lly desirable are n-dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7 times ethoxylated, lauryl amido propylamine and cocoamido propylamine.

W O 98/07823 PCT~US97/11544 Conventional detergent enzymes The detergent compositions of the present invention can further comprise one or more enzymes which provide detergent performance and/or fabric care benefits.

Said enzymes include enzymes selected from peroxidases, proteases, gluco-amylases, amylases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, 13-glucanases, arabinosidases, hyaluronidase, chondroitinase, l~sc~-se or mixtures thereof.

A preferred combination is a detergent composition having cocktail of conventional applicable enzymes like protease, amylase, lipase, cutinase and/or cellulase in conjunction with one or more plant cell wall degrading enzymes.

Peroxidase enzymes are used in combination with oxygen sources, e.g.
percarbonate, perborate, persulfate, hydrogen peroxide, etc. They are used for "solution bleaching", i.e. to prevent transfer of dyes or pigments removed from substrates during wash operations to other substrates in the wash solution.
Peroxid~se enzymes arë known in the art, and include, for example, horseradish peroxidase, ligninase, and haloperoxidase such as chloro- and bromo-peroxidase. Peroxid~se-containing detergent compositions are disclosed, for example, in PCT l~,terl,alional Application WO 89/099813, WO89109813 and in European Patent application EP No. 91202882.6, filed on November 6, 1991 and EP No. 96870013.8, filed February 20, 1996.
Other suitable oxidases are l~c~se enzyme using oxygen, hydrogen peroxide as primary substrate.

rl efer, ed enhancers are 1 0-Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 1 0-plle,~oxa~inepropionic acid (POP) and 1 0-methylphenoxazine (described in WO 94/1 2621). Sodium percarbonate or perborate are preferred sources of hy-llogen peroxide.

W O 9~ D23 PCTrUS97/11544 Said peroxidases are normally incorporated in the detergent composition at levels hom 0.0001% to 2% of active enzyme by weight of the detergent composition.

Other preferred enzymes that can be included in the detergent compositions of the present invention include lipases. Suitable lipase enzymes for detergent usage include those produced by microorganisms of the Pseudomonas group, such as PseudG"~o,1as stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034. Suitable lipases include those which show a positive immunological cross-reaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P
"Amano," hereinafter referred to as "Amano-P". Other suitable commercial lir~ses include Amano-CES, lipases ex Ch~omobacter viscosum, e.g.
Chromobacter vjscosum var. Iipolyticum NRRLB 3673 from Toyo Jozo Co., - Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. Especially suitable lipases are lipases such as M1 LipaseR and LipomaxR (Gist-Brocades) and LipolaseR and Lipolase UltraR(Novo) which have found to be very effective when used in combination with the compositions of thepresent invention.
Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special kind of lipase, namely lipases which do not require interfacial activation. Addition of culinases to detergent cG,npositions have been described in e.g. WO-A-88/09367 (Genencor).
The lir~ses andlor cutinases are normally incol~oraled in the detergent coi,~position at levels from 0.0001% to 2% of active enzyme by weight of the detergent composition.

Suitable prote~ses are the sl~btilisins which are obtained from particular strains of B. subtilis and B. Iicheniformis (subtilisin BPN and BPN'). One suitahle prolease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, developed and sold as ESPERASE~) by Novo Industries A/S of Denmark, hereinafter "Novo". The preparation of this enzyme and an~'ogo!~s enzymes is described in GB 1,243,784 to Novo. Other suitable proteases include ALCALASE~9, DURAZYM~ and SAVIN~SE~) from Novo and W O 98/07823 PCT~US97/11544 MAXATASE~. MAXACAL~, PROPERASE~) and MAXAPEM~ (protein engineered M~Y~C~I) from Gist-Brocades. Proteolytic enzymes also encompass modified bacterial serine proteases, such as those described in European Patent Application Serial Number 87 303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98), and which is called herein "Protease B", and in European Patent Application 199,404, Venegas, published October 29, 1986, which refers to a modified bacterial serine protealytic enzyme which is called "Protease A" herein.
More preferred is what is called herein "Protease C", which is a variant of an alkaline serine protease from Bacillus in which Iysine replaced arginine at position 27, tyrosine replaced valine at position 104, serine replaced asparagine at position 123, and alanine replaced threonine at position 274. Protease C is described in EP 90915958:4, corresponding to WO 91/06637, Published May 16, 1991. Genetically modified variants, particularly of Protease C, are also included herein. See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO 93/18140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are described in WO
92103529 A to Novo. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 95/07791 to Procter &
Gamble. A recol"binant trypsin-like protease for detergents suitable herein is described in WO 94/25583 to Novo.
- In more detail, protease referred to as "Protease D" is a carbonyl hydrolase variant having an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for a plurality of amino acid residues at a pssition in said carbonyl hydrolase equivalent to position +76, preferably also in combination with one or more amino acid residue positions equivalent to those selected from the group consisting of +99, +t01, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, ~195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274 according to the numbering of Bacillus amyloliquefaciens subtilisin, as described in WO95/10591 and in the patent application of C. Ghosh, et al, "Bleaching Compositions Comprising Protease Enzymes" having US Serial No. 08/322,677, filed October 13, 1994. Also suitable for the present invention are proteases described in patent applications EP 251 446 and WO91/06637 and protease BLAP~19 Jesc~ibed in WO91/02792.
Protease enzyme may be incorporated into the co~,positions in accordarlce with WO 98/07823 PCTrUS97/11544 the invention at a level of from 0.0001% to 2% active enzyme by weight of the composition.

Amylases (a and/or 13) can be included for removal of carbohydrate-based stains. W094/02597, Novo Nordisk A/S published February 03, 1994, describes detergent compositions which incorporate mutant amylases. See also WO94/18314, Genencor, published August 18, 1994 and W095/10603, Novo Nordisk A/S, published April 20, 1995. Other amylases known for use in detergent compositions include both a- and ,B-amylases. a-Amylases are known in the art and include those disclosed in US Pat. no. 5,003,257; EP 252,666;
WOI91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and British Patent specification no. 1,296,839 (Novo). Other suitable amylase are stability-enhanced amylases including Purafact Ox AmR described in WO 94/18314, published August 18l 1994; W096/05295, Genencor, published February 22, 1995 and amylase variants having additional modification in the immediate parent available from Novo Nordisk A/S, disclosed in WO 95/10603, published April 95. Examples of commercial a-amylases products are Termamyl~), Ban (~) ,Fungamyl(~) and Duramyl~), all available from Novo Nordisk AIS Denmark.
W095/26397 describes other suitable amylases: a-amylases characterised by having a specific activity at least 25% higher than the specific activity of Ter,ndmyl(~) at a temperature range of 25~C to 55~C and at a pH value in the range of 8 to 10, measured by the Ph~deb~s(~) a-amylase activity assay. Other amylolytic enzymes with improved properties with respect to the activity level and the combination of ll,er,nostability and a higher activity level are described in W095/35382.

The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal andyeastorigin. Origin can further be mesophilic or exl~mopl,ilic (ps~ct)r~plliiic, psycl~rolrophic, ther",opl,ilic, barophilic, alkalophilic, acidophilic, halophilic, etc. ). Purified or non-purified forms of these enzymes may be used. Also included by definition, are mutants of native enzymes. Mutants can be obtained e.g. by protein and/or genetic engineering, chemical and/or physical modifications of native enzymes. Cor",non practice as well is the expression of the enzyme via host organism in which the genetic material responsible for the production of the enzyme has been cloned.
Said enzymes are normally incorporated in the detergent coi"position at levels CA 02263430 l999-02-ll W O 98/07823 PCT~US97/11544 from 0.0001% to 2% of active enzyme by weight of the detergent composition.
The enzymes can be added as separate single ingredients (prills, granulates, stabiiized liquids, etc., containing one enzyme) or as mixtures of two or more enzymes (e.g., cogranulates) Other suitable detergent ingredients that can be added are enzyme oxidation scavengers which are described in Co-pending European Patent application 92870018.6 filed on January 31, 1992. Examples of such enzyme oxidation scavengers are ethoxylated tetraethylene polyamines.

A range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 A and WO
9307260 A to Genencor International, WO 8908694 A to Novo, and U.S.
3,553,139, January 5, 1971 to McCarty et al. Enzymes are further disrlssed in U.S. 4,101,457, Place et al, July 18, 1978, and in U.S. 4,507,219, Hughes, March 26, 1985. Enzyme ma~erials useful for liquid detergent formulations, and their incorporation into such formulations, are clisclosed in U.S. 4,261,868, Hora et al, April 14, 1981. Enzymes for use in detergents can be stabilised by various techniques. Enzyme stabilisation techniques are disclosed and exemplified in U.S. 3,600,319, August 17, 1971, Gedge et al, EP 199,405 and EP 200,586, October 29, 1986, Venegas. Enzyme stabilisation systems are also described, for example, in U.S. 3,519,570. A useful Bacillus, sp. AC13 giving proteases, xylanases and cellulases, is described in WO 9401532 A to Novo.

Co/or care benefits Technologies which provide a type of color care benefit can also be includqd Examples of these technologies are metallo catalysts for color maintenance. Such metallo catalysts are described in co-pending European Patent Application No. 92870181.2.

The Bleaching agen~

The detergent comrositions of the present invention can further include bleaching agents such as hydrogen peroxide, PB1, PB4 and percar~G~ ~ate with a particle size of 400-800 microns. These bleaching agent components can W O 98/07823 PCTrUS97/11544 include one or more oxygen bleaching agents and, depending upon the bleaching agent chosen, one or more bleach activators. When present oxygen bleaching compounds will typically be present at levels of from about 1% to about 25%.

The bleaching agent component for use herein can be any of the bleaching agents useful for detergent compositions including oxygen bleaches as well as others known in the art. The bleaching agent suitable for the presentinvention can be an activated or non-activated bleaching agent.

One category of oxygen bleaching agent that can be used encori,passes percarboxylic acid bleaching agents and salts thereof. Suitable examples of thisclass of agents include magnesium monoperoxyphthalate hexahydrate, the magnesium salt of meta-chloro perbenzoic acid, 4-nonylamino~-oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaching agents are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740,446, European Patent Application 0,133,354 and U.S. Patent 4,412,934. Highly prefer,ed bleaching agents also include 6-nonylamino~-oxoperoxycaproic acid as described in U.S. Patent 4,634,551.
Another category of bleaching agents that can be used enco",passes the halogen bleaching agents. Examples of hypohalite bleaching agents, for example, include trichloro isocyanuric acid and the sodium and pot~ssi~
dichloroisocyanurates and N-chloro and N-bromo alkane sulphonamides. Such materials are normally added at 0.5-10% by weight of the finished product, preferably 1-5% by weight.

The hyd~oge" peroxide releasing agents can be used in combination with bleach activatnrs such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene-sulfonate (NOBS, described in US 4,412,934), 3,5,-trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,~91) or pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6-aminocaproic acid (NACA-OBS, described in W094128106), which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect. Also suitable activators are acylated citrate esters such as disclosed in Co-pending European Patent Application No. 91870207.7.

CA 02263430 l999-02-ll W O 98/07823 PCTrUS97/11544 Useful bleaching agents, including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleaching compounds for use in detergent compositions according to the invention are described in our co-pending applications USSN 08/136,626, PCT/US95/07823, W095/27772, W095127773, W095/27774 and W095127775.

The hydrogen peroxide may also be present by adding an enzymatic system (i.e. an enzyme and a substrate therefore) which is capable of generatinghydrogen peroxide at the beginning or during the washing and/or rinsing process. Such enzymatic systems are disclosed in EP Patent Application 91202655.6 filed October 9, 1991.

Metal-containing catalysts for use in bleach compositions, include cobalt-containing catalysts such as Pentaamine acetate cobalt(lll) salts and manganese-containing catalysts such as those described in EPA 549 271; EPA
549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US
5,114,611. Bleaching composition comprising a peroxy compound, a manganese-containing bleach catalyst and a chelating agent is described in the patent application No 94870206.3.

Bleaching agents other than oxygen bleaching agents are also known in the art and can be utili~ed herein. One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as the sulfonated zinc and/or aluminum phthalocyanines. These materials can be deposited upon the substrate during the washing process. Upon irradiation with light, in the prese"ce of oxygen, such as by hanging clothes out to dry in the daylight, the sulfonated zinc phthalocyanine is activated and, cor,se.~uently, the suLs~,dle is bleached. P,e~r,ecl zinc phthalocyanine and a photoactivated bleaching ~rocess are described in U.S. Patent 4,033,718. Typically, detergent co",positions will contain about 0.025% to about 1.25%, by weight, of sulfonatedzinc phthalocyanine.

Builder system The con~posilions accorJir,y to the present invention may further comprise a builder system. Any conventional builder system is suitable for use herein W O 98/07823 PCTrUS97/11544 including aluminosilicate materials, silicates, polycarboxylates7 alkyl- or alkenyl-succinic acid and fatty acids, materials such as ethylenediamine tetraacetate, diethylene triamine pentamethyleneacetate, metal ion sequestrants such as aminopolyphosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
Phosphate builders can also be used herein.

Suitable builders can be an inorganic ion exchange material, commonly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
Another suitable inorganic builder material is layered silicate, e.g. SKS~
(Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na2Si2~5) Suitable polycarboxylates co"laining one carboxy group include lactic acid, glycolic acid and ether derivatives thereof as disclQserl in Belgian Patent Nos. 831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy groups include the water-soluble salts of succinic acid, malonic acid, (ethylenedioxy) diacetic acid, maleic acid, diglycollic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates described in German Offenlegenschrift 2,446,686, and 2,446,687 and U.S. Patent No. 3,935,257 and the sulfinyl c~, l oxylates described in Belgian Patent No. 840,623.
Polyc~r6Oxylates containing three carboxy groups include, in particular, water-soluble cilra~es, aconitrates and citracGnates as well as succinale derivatives such as the ~. bo~(ymethyloxysuccinates described in British Patent No.
1,379,241, lactoxysuccinates desc,ibed in Netherlands Application 7205873, and the oxypolycarboxylate materials such as 2-oxa-1,1,3-propane tricarboxylates desc~ibeJ in British Patent No. 1,387,447.

Polycarboxylates containing four carboxy groups include oxydisll~,;nates disclosed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates, 1,1,3,3-propane tetracarboxylates and 1,1,2,3-propane tetracarboxylates.
Polycarboxylates containing sulfo substituents include the sulfosuccina~e derivatives disclosed in British Patent Nos. 1,398,421 and 1,398,422 and in U.S.Patent No. 3,936,448, and the sulfonated pyrolysed citrates described in BritishPatent No. 1,082,179, while polycarboxylates containing phosphone substituents are disclosed in British Patent No. 1,439,000.

.

CA 02263430 1999-02-ll W O 98/07823 PCT~US97/11544 Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis,cis,cis-tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydro-furan - cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan -cis -dicarboxylates, 2,2,5,5-tetrahydrofuran - tet~acarboxylates, 1,2,3,4,5,6-hexane -hexacar-boxylates and and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic poly-carboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent No. 1,425,343.
Of the above, the preferred polycarboxylates are hydroxyca,boxylates containing up to three carboxy groups per molecule, more particularly citrates.
Pre~r,ed builder systems for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS~), and a water-soluble carboxylate chelating agent such as citric acid. Preferred builder systems for use in liquid detergent compositions of the present invention are soaps and polycarboxylates.

A suitable chelant for inclusion in the detergent compositions in accordance with the invention is ethylenediamine-N,N'-clisuccinic acid (EDDS) orthe alkali metal, alkaline earth metal, ammonium, or substituted a"""onium saltsthereof, or mixtures thereof. rrefelled EDDS compounds are the free acid form and the sodium or magnesium salt thereof. Examples of such preferreJ sodium salts of EDDS include Na2EDDS and Na4EDDS. Examples of such preferred magnesium salts of EDDS include MgEDDS and Mg2EDDS. The magnesium salts are the most ,,,rel~r,~d for inclusion in compositions in accordance with the invention.

r~fer, ecJ builder systems include a mixture of a water-insoluble aluminosilicate builder such as zeolite A, and a watersoluble carboxylate chelating agent such as citric acid.

Other builder materials that can form part of the builder system for use in granular compositions include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as the organic phospl,onates, amino polyalkylene phosphonates and amino polycarboxylates.

W O 98/07823 PCTnUS97/11544 Other suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 20,000 to 70,000, especially about 40,000.

Detergency builder salts are normally included in amounts of from 5% to 80% by weight of the composition preferably from 10% to 70% and most usually from 30% to 60% by weight.

Suds suppressor Another optional ingredient is a suds suppressor, exemplified by silicones, and silica-silicone mixtures. Silicones can be generally represented by alkylated polysiloxane materials while silica is normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. These materials can be incorporated as particulates in which the suds suppressor is advantageously releasably incorporated in a water-soluble or water-dispersible, stlhst~nlially non-surface-active detergent impermeable carrier. Alternatively the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to one or more of the other components.
A preferred silicone suds co-,~tolling agent is djSCIQSed in Bartollota et al.
U.S. Patent 3 933 672. Other particularly useful suds suppressors are the self-emulsifying silicone suds suppressors, described in German Patent Application DTOS 2 646 126 published April 28, 1977. An example of such a compound is DC-544, commercially available from Dow Corning, which is a siloxane~lycol copolymer. Fspeci~lly pre~r,ed suds controlling agent are the suds suppressor system c~,n~)lising a mixture of silicone oils and 2-alkyl-alcanols. Suitable 2-alkyl-alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R.
Such suds suppressor system is described in Co-pending European Patent application N 92870174.7 filed 10 November, 1992.
Especially preferred silicone suds controlling agents are described in Co-pending European Patent application N~92201649.8. Said compositions can . , CA 02263430 l999-02-ll W O 98/07823 PCT~US97/11544 preferably from 0.75% to 8%, most preferably from 1% to 6% by weight of the compositiorl.

Preferred optical brighteners are anionic in character, examples of which are disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-ylamino)stilbene-2:2' disulphonate, disodium 4, - 4'-bis-(2-morpholino-4-anilino-s-triazin~-ylamino-stilbene-2:2' - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-triazin~-ylamino)stilbene-2:2' - disulphonate, monosodium 4',4" -bis-(2,4-dianilino-s-tri-azin~ ylamino)stilbene-2-sulphonate, disodi~lrn 4,4' -bis-(2-anilino4-(N-methyl-N-2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2,2' - disulphonate, di-sodium 4,4' -bis-(4-phenyl-2, 1 ,3-triazol-2-yl)-stilbene-2,2' disulphonate, di-so-dium 4,4'bis(2-anilino~-(1-methyl-2-hydroxyethylamino)-s-triazin~- ylami-no)stilbene-2,2'disulphonate, sodium 2(stilbyl~"-(naphtho-1',2':4,5)-1,2,3 -triazole-2"-sulphonate and 4,4'-bis(2-sulphostyryl)biphenyl. Highly preferred brighteners are the specific brighteners of copending European Patent - application No. 95201943.8.

Other useful polymeric materials are the polyethylene glycols, particularly those of molecular weight 1000-10000, more particularly 2000 to 8000 and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5~h by weight. These polymers and the previously mentioned homo- or co-polymeric polycarboxylate salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proteinaceous and oxidizable soils in the presence of transition metal impurities.

Soil release agents useful in compositions of the present invention are conve,ltiGnally copolymers or terpolymers of terepl,tl)alic acid with ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are ~lisclQsed in the co,)"),o"ly assigned US Patent Nos. 4116885 and 4711730 and European Published Patent Application No. 0 272 033. A
particular prefer,ad polymer in accordance with EP-A-0 272 033 has the formula (cH3(pEG)43)o~7s(poH)o 25~T-Po)2.8(T-pEG)o 4]T( ~t)0.25((PEG)43CH3)0.7~

W O 98/07823 PCTrUS97/11544 where PEG is -(OC2H4)O-,PO is (0C3H60) and T is (pcOC6H4C0).

Also very useful are modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2 propane diol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or propane-diol. The target isto obtain a polymer capped at both end by sulphobenzoate groups, "primarily", inthe present context most of said copolymers herein will be end-capped by sulphobenzoate groups. However, some copolymers will be less than fully capped, and therefore their end groups may consist of monoester o~ ethylene glycol and/or propane 1-2 diol, thereof consist "secondarily" of such species.

The selected polyesters herein contain about 46% by weight of cJi",eli,yl terepl,Ll,alic acid, about 16% by weight of propane -1.2 diol, about 10% by weight ethylene glycol about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3.000. The polyesters and their method of preparalion are described in detail in EPA 311 342.

Is is well known in the art that free chlorine in tap water rapidly deactivates the enzymes comprised in detergent compositions. Therefore, using chlorine scavenger such as perborate, ammonium sulfate, sodium sulphite or polyethyleneimine at a levet above 0.1% by weight of total co"")osition, in the formulas will provide improved through the wash stability of the detergent enzymes. Compositions con~prising chlorine scavenger are described in the European patent application 92870018.6 filed January 31, 1 992.

Alkoxylated polycarboxylates such as those prepared from polyacrylates are useful herein to provide additional grease removal performance. Such materials are described in WO 91/08281 and PCT 90101815 at p. 4 et seq., incorporated herein by reference. Chemically, these materials co",p, ise polyacrylates having one ethoxy side~hain per every 7-8 acrylate units. The side-chains are of the formula -(CH2CH20)m(CH2)nCH3 wherein m is 2-3 and n is 6-12. The side-chains are ester-linked to the polyacrylate "backbone" to provide a "comb" polymer type structure. The molecnl~- weight can vary, but is typically in the range of about 2000 to about 50,000. Such alkoxylated comprise a silicone/silica mixture in combination with fumed nonporous silica such as AerosilR.

The suds suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1%
by weight.

Others Other components used in detergent compositions may be employed, such as soil-suspending agents, soil-release agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, andlor encapsulated or non-enc~psul~ted perfumes.

Especially suitable encapsulating materials are water soluble c~psules which consist of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1,464,616.

Other suitable water soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid-esters of substituted dicarboxylic acids such as described in US 3,455,838. These acid-ester dextrins are, preferably, prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of said enc~psul~ting materials include N-Lok manufactured by National Starch. The N-Lok enc~psul~ting material consists of a ",odiried maize starch and ~IUCOSe. The starch is modified by adding monofunctional s~ Ihstih~ted groups such as octenyl succinic acid anhydride.

Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydtoxyethylcellulose, and homo- or co-polymeric polycarl,oxylic acids or their salts. Polymers of this type include the polyacrylates and maleic anhydride-acrylic acid copolymers previously mentioned as builders, as well as copolymers of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the maleic anhydride constituting at least 20 mole percent of the copolymer. These materials are normally used at levels of from 0.5% to 10% by weight, more WO 98/07823 PC'r/US97/11544 poiycarboxylates can comprise from about 0.05% to about 10%, by weight, of the compositions herein.

Soffenjng agents Fabric softening agents can also be inco"~orated into laundry detergent compositions in accordance with the present invention. These agents may be inorganic or organic in type. Inorganic softening agents are exemplified by the smectite clays disclosed in GB-A-1 400 898 and in USP 5,019,292. Organic fabric softening agents include the water insoluble tertiary amines as disclosedin GB-A1 514 276 and EP-B0 011 340 and their combination with mono C12-C14 quaternary ammonium salts are disclosed in EP-B-0 026 527 and EP-B-0 026 528 and di-long-chain amides as disclosed in EP-B-0 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0 313 146.

Levels of smectite clay are normally in the range from 2% to 20%, more preferably from 5% to 15% by weight, with the material being added as a dry mixed component to the remainder of the formulation. Organic fabric s~lei,i"g agents such as the water-inscluhle tertiary amines or dilong chain amide materials are incorporated at levels of from 0.5% to 5% by weight, normally from1% to 3% by weight whilst the high mol~cul~r weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1% to 2%, normally from 0.15% to 1.5% by weight. These materials are normally added to the spray dried po,lion of the composition, although in some instances it may be more convenient to add them as a dry mixed particu'~te, or spray them as molten liquid on to other solid components of the composition.

Dispersants The detergent composition of the present invention can also contain dispersants: Suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.

CA 02263430 1999-02-ll W O 98/07823 PCT~US97/11544 Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 1,000 to 100,000.

Especially, copolymer of acrylate and methylacrylate such as the 480N
having a molecular weight of 4000, at a level from 0.5-20% by weight of composition can be added in the detergent compositions of the present invention.

The compositions of the invention may contain a lime soap peptiser compound, which has a lime soap dispersing power (LSDP), as defined hereinafter of no more than 8, pre~erably no more than 7, most preferably no more than 6. The lime soap peptiser compound is preferably present at a level from 0% to 20% by weight.

A numerical measure of the effectiveness of a lime soap peptiser is given by the lime soap dispersant power (LSDP) which is determined using the lime soap dispersant test as described in an article by H.C. Bor!yl,elly and C.A.
Bergman, J. Am. Oil. Chem. Soc., volume 27, pages 88-90, (1950). This lime soap dispersion test method is widely used by practitioners in this art field being referred to, for example, in the following review articles; W.N. Linfield, Surfactant science Series, Volume 7, page 3; W.N. Linfield, Tenside surf. det., volume 27, pages 159-163, (1990); and M.K. Nagarajan, W.F. Masler, Cosmetics and Toiletries, volume 104, pages 71-73, (1989). The LSDP is the % weight ratio of dispersing agent to sodium oleate required to disperse the lime soap cleposils formed by 0.025g of sodium oleate in 30ml of water of 333ppm CaCo3 (Ca:Mg=3:2) equivalent ha,dl,ess.
S~"ractar,ts having good lime soap peptiser cap~l~ility will include certain amine oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated alcohols.

Exemplary surfactants having a LSDP of no more than 8 for use in accord with the present invention include C16-C1g ~i,nelhyl amine oxide, C12-C1g alkyl ethoxysulfates with an average degree of ethoxylation of from 1-5, particularly C12-C1s alkyl ethoxysulfate surfactant with a degree of ethoxylation of amount 3(LSDP=4), and the C14-C1s ethoxylated alcohols with an average degree of W O 98/07823 PCT~US97/11544 ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol A012 and Lutensol A030 respectively, by BASF GmbH.

Polymeric lime soap peptisers suitable for use herein are described in the article by M.K. Nagarajan, W.F. Masler, to be found in Cosmetics and Toiletries,volume 104, pages 71-73, (1989).

Hydrophobic bleaches such as 4-[N-octanoyl~-aminohexanoyl]ben~ene sulfonate, 4-[N-nonanoyl~-aminohexanoyl]benzene sulfonate, 4-[N-decanoyl~-aminohexanoyl]benzene sulfonate and mixtures thereof; and nonanoyloxy benzene sulfonate together with hydrophilic / hydrophobic bleach formulations can also be used as lime soap peptisers compounds.

Dye transfer inhibition The detergent compositions of the present invention can also include compounds for inhibiting dye transfer from one fabric to another of solubilized and suspended dyes encountered during fabric laundering operations involving colored fabrics.

Polymeric dye transfer inhibiting agents The detergent compositions according to the present invention also comprise from 0.001% to 10 %, preferably from 0.01% to 2%, more preferably from 0.0~% to 1% by weight of polymeric dye transfer inhibiting agents. Said polymeric dye transrer inhibiting agents are normally incorporated into detergent co",l-ositions in order to inhibit the transfer of dyes from colored fabrics onto fabrics washed therewith. These polymers have the ability to complex or adsorb the fugitive dyes washed out of dyed fabrics before the dyes have the opportunity to become attached to other articles in the wash.
Especially suitable polymeric dye transfer inhibiting agents are polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
Addition of such polymers also enhances the performance of the enzymes acco,di"g the invention.

W O 9~ 23 PCT~US97/11544 a) Polyamine N-oxide polymers The polyamine N-oxide polymers suitable for use contain units having the following structure formula:
p I

(I) Ax I
R

wherein P is a polymerisable unit, whereto the R-N-O group can be attached to or wherein the R-N-O group forms part of the polymerisable unit or a combination of both.

Il 11 11 - AisNC, CO,C,-O-,-S-,-N-;xisOor1;
R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclic or alicyclic groups or any combination thereof whereto the nitrogen of the - N-O group can be attached or wherein the nitrogen of the N-O group is part of these groups.

The N-O group can be represented by the following general structures:

O O

(R1 )x -N- (R2)y =N- (R1 )x I

(R3)z wherein R1, R2, and R3 are aliphatic groups, aro,natic, heterocyclic or alicyclic groups or combinations thereof, x or/and y or/and z is 0 or 1 and wherein the nil,oyel- of the N-O group can be attached or wherein the ni~o~en of the N-O group forms part of these groups.

The N-O group can be part of the polymerisable unit (P) or can be attached to the polymeric backbone or a combination of both.

W O 98/07823 PCT~US97/11544 Suitable polyamine N-oxides wherein the N-O group forms part of the polymerisable unit comprise polyamine N-oxides wherein R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups.
One class of said polyamine N-oxides comprises the group of polyamine N-oxides wherein the nitrogen of the N-O group forms part of the R-group.
Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof.
Another class of said polyamine N-oxides comprises the group of polyamine N-oxides wherein the nitrogen of the N-O group is attached to the R-group.

Other suitable polyamine N-oxides are the polyamine oxides whereto the N-O group is attached to the polymerisable unit.
Praferled class of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic groups wherein the nitrogen of the N-0 functional group is part of said R group.
Examples of these classes are polyamine oxides wherein R is a heterocyclic compound such as pyrridine, pyrrole, imidazole and derivatives thereof.
Another preferred class of polyamine N-oxides are the polyamine oxides having the general formula (I) wherein R are aromatic, heterocyclic or alicyclic groupswherein the nitrogen of the N-0 functional group is attached to said R groups.
Examples of these r~sses are polyamine oxides wherein R groups can be aromatic such as phenyl.

Any polymer bachLone can be used as long as the amine oxide polymer formed is water-soluble and has dye transfer inhibiling properties. Examples of suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamide, polyimides, polyacrylates and mixtures thereof.

The amine N-oxide polymers of the present invention typically have a ratio of amine to the amine N-oxide of 10:1 to 1:1000000. However the amount of amine oxide groups present in the polyamine oxide polymer can be varied by ap~.rop, iale copolymerization or by appropriate degree of N-oxidation.
Preferably, the ratio of amine to amine N-oxide is from 2:3 to 1:1000000. More preferably from 1:4 to 1:1000000, most preferably from 1:7 to 1:1000000. The polymers of the present invention actually e~ ,cG.,.pass random or block W O 98/07823 PCTrUSg7/11544 copolymers where one monomer type is an amine N-oxide and the other monomer type is either an amine N-oxide or not. The amine oxide unit of the polyamine N-oxides has a PKa < 10 preferably PKa < 7 more preferred PKa <
6.
The polyamine oxides can be obtained in almost any degree of polymerisation.
The degree of polymerisation is not critical provided the material has the desired water-solubility and dye-suspending power.
Typically the average molecular weight is within the range of 500 to 1000000; preferably from 1 000 to 50000 more prererably from 2 000 to 30 000 most pre~erably from 3 000 to 20 000.

b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole The N-vinyli~"ida~ole N-vinylpyrrolidone polymers used in the present invention have an average molecular weight range from 5000-1 000000 preferably from 5 000-200 000.
Highly preferred polymers for use in detergent compositions accordi"g to the present invention comprise a polymer selected from N-vinylimidazole N-vinylpyrrolidone copolymers wherein said polymer has an average molecular weight range from 5 000 to 50 000 more preferably from 8 000 to 30 000 most preferably from 10 000 to 20 000.
The average molec~ r weight range was deter~ined by light scattering as described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113"Modern M~thods of Polymer Characterization".
Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an average moleclJIar weight range from 5 000 to S0 000; more preferably from 8 000 to 30 000; most preferably from 10 000 to 20 000.

The N-vinylimidazole N-vinylpyrrolidone copolymers characterized by having said average molecu~a weight range provide excellent dye lranster inhibiting pr~,pe,lies while not adversely affecting the cleaning pe,rorl"ance of detergent compositions formulated therewith.
The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2 more ~referdbly from 0.8 to 0.3 most preferably from 0.6 to 0.4 .

W O 98/07823 PCTrUS97/11~44 c) Polyvinylpyrrolidone The detergent compositions of the present invention may also utilize polyvinylpyrrolidone ("PVP") having an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 51~~~ to about 15,000. Suitable polyvinylpyrrolidones are coi"ll,ercially vailable from ISP Corporation, New York, NY and ~lor,l~eal, Canada under the product names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average molecular weight of 40,000), PVP K~0 (average molecular weight of 160,000), and PVP K-90 (average molecular weight of 360,000). Other suitable polyvinylpyrrolidones which are commercially available from BASF CooperaliGn include Sokalan HP 165 and Sokalan HP 12; polyvinylpyrrolidones known to persons skilled in the detergent field (see for example EP-A-262,897 and EP-A-256,696).

d) Polyvinylox~olidone:

The detergent compositions of the present invention may also utilize polyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Said polyvinyloxazolidones have an average molecular weight of from about 2,500 to about 400,000, prefsr~bly from about 5,000 to about 200,000, more pre~erably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 1 5,000.

e) Polyvinylimidazole:

The ~Jeter~e~)t co",positions of the present invention may also utilize polyvinylimidazole as polymeric dye transfer inhibiting agent. Said polyvinylimidazoles have an average from about 2,500 to about 400,000, l~referably from about 5~000 to about 200,000, more preferal)ly from about 5,000to about 50,000, and most preferably from about 5,000 to about 15,000.

.

CA 02263430 1999-02-ll f) Cross-linked polymers:

Cross-linked polymers are polymers whose backbone are interconnected to a certain degree; these links can be of chemical or physical nature, possibly withactive groups n the backbone or on branches; cross-linked polymers have been described in the Journal of Polymer Science, volume 22, pages 1035-1039.

In one embodiment, the cross-linked polymers are made in such a way that they form a three-dimensional rigid structure, which can entrap dyes in the pores formed by the three-dimensional structure. In another embodiment, the cross-linked polymers entrap the dyes by swelling.

Such cross-linked polymers are described in the co-pending patent application 94870213.9 Method of washinq The compositions of the invention may be used in essentially any washing or cleaning methods, including soaking methods, pretreatment methods and methods with rinsing steps for which a separate rinse aid composition may be added.
The process described herein comprises contacting fabrics with a laundering solution in the usual manner and exemplified hereunder.

The process of the invention is conveniently carried out in the course of the cleaning process. The method of cleaning is preferably carried out at 5~C to95~C, espesi~"y between 10~C and 60~C. The pH of the treatment solution is preferably from 7 to 11.

The following examples are meant to exemplify compositions of the present invention, but are not necess~rily meant to limit or otherwise define the scope of the invention.

In the detergent compositions, the enzymes levels are expressed by pure enzyme by weight of the total composition and unless otherwise specified, the W O 98/07823 PCT~US97/11544 detergent ingredients are expressed by weight of the total compositions. The abbreviated component identifications therein have the following meanings:

LAS : Sodium linear C12 alkyl benzene sulphonate TAS : Sodium tallow alkyl sulphate CXYAS : Sodium C1X - C1y alkyl sulfate 25EY : A C12 C1s predominantly linear primary alcohol condensed with an average of Y moles of ethylene oxide CXYEZ : A c1x - C1y predominantly linear primary alcohol condensed with an average of Z moles of ethylene oxide XYEZS : C1X - C1y sodium alkyl sulfate condensed with an average of Z moles of ethylene oxide per mole QAS : R2.N+(CH3)2(C2H4OH) with R2 = C12-C14 Soap : Sodium linear alkyl carboxylate derived from a 80/20 mixture of tallow and coconut oils.

TFM : C16-C1g alkyl N-methyl glucamide.

TPKFA : C12-C14 topped whole cut fatty acids.
DEQA . Di-(tallow-oxy-ethyl) dimethyl ammonium chloride.

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

Neodol 45-13 : C14-C15 linear primary alcohol ethoxylate, sold by Shell Chemical CO.

PCT~US97/11544 Silicate : Amorphous Sodium Silicate (SiO2:Na2O ratio = 2.0) NaSKS-6 : Crystalline layered silicate of formula ~-Na2Si2Os Carbonate : Anhydrous sodium carbonate with a particle size between 200 ~m and 900~1m.

Bicarbo"ate : Anhydrous sodium bicarbonate with a particle size between 400 ~m and 1 200~m.

STPP : Anhydrous sodium tripolyphosphate MA/M : Copolymer of 1:4 maleic/acrylic acid average molecular weight about 80 000 Polyacrylate : Polyacrylate homopolymer with an average molecular weight of 8 000 sold under the tradename PA30 by BASF GmbH

Zeolite A : Hydrated Sodium Aluminosili~te of formula Na12(A1~2Si~2)12. 27H20 having a primary particle size in the range from 0.1 to 10 micrometers Citrate : Tri-sodium citrate dihydrate of activity 86 4% with a particle size distribution between 425 ~m and 850 llm.

Citric : Anhydrous citric acid PB1 : Anhydrous sodium perborate monohydrate bleach e,llpi,ical formula NaBO2.H2O2 PB4 : Anhydrous sodium perborate tetrahydrate PercarL,o"ate : Anhydrous sodium percarbonate bleach of empirical formula 2Na2CO3.3H2O2 W 098/07823 PCTrUS97111544 TAED : Tetraacetyl ethylene diamine.

NOBS : Nonanoyloxybenzene sulfonate in the form of the sodium salt.

Photoactivated : Sulfonated zinc phtlocyanine encapsulated in dextrin Bleach soluble polymer.

Protease : Proteolytic enzyme sold under the tradename Savinase, Alc~l~se, Durazym by Novo Nordisk AIS, Maxacal, Maxapem sold by Gist-Brocades and proteases described in patents WO91/06637 andlor WO95/10591 and/or EP 251 446.

Amylase : Amylolytic enzyme sold under the tradename Purafact Ox AmR ~Jesc, iL,ed in WO 94/18314, W096/05295 sold by Genencor; Termamyl~, Fungamyl~) and Duramyl~), all available from Novo Nordisk A/S and those described in WO95126397.

Lipase : Lipolytic enzyme sold under the tradename Lipolase, Lipolase Ultra by Novo Nordisk A/S

Cellulase : Cellulytic enzyme sold under the tradename Carezyme, Celluzyme and/or Endol~se by Novo Nordisk A/S.

Antibody : Rabbit anti-Carezyme antibody available from Novo Nordisk A/S at a dilution 1: 1000 Batch #: Ra17-11195 (anti-Carezyme PPC 3404).

CMC : Sodiumcarboxymethyl cellulose.

HEDP : 1,1 -hydroxyetharie diphosphonic acid.

W O 9XJ'~.7~23 ~iO

DETPMP Diethylene triamine penta (methylene phosphonic acid), marketed by Monsanto under the Trade name Dequest 2060.

PVNO : Poly(4-vinylpyridine)-N-Oxide.
PVPVI : Poly (4-vinylpyridine)-N-oxide/copolymer of vinyl-imidazole and vinyl-pyrrolidone.

Brightener 1 : Disodium4,4'-bis(2-sulphostyryl)biphenyl.
Brightener 2 : Disodium 4,4'-bis(4-anilino~-morpholino-1.3.5-triazin-2-yl) stilbene-2:2'-disulfonate.

Silicone antifoam : Polydimethylsiloxane foam controller with siloxane-oxyalkylene copolymer as dispersing agent with a ratio of said foam controller to said dispersing agent of 10:1 to 100:1.

Granular Suds : 12% Silicone/silica, 18% stearyl alcohol,70% starch in Suppressor granular form SRP 1 : Sulfobenzoyl end ~pped esters with oxyethylene oxy and terephtaloyl backbone.

SRP 2 : Diethoxylated poly (1,2 propylene terephtalate) short block polymer.

Sulphate : Anhydrous sodium sulphate.

HMWPEO : High molecular weight polyethy~ene oxide PEG : Polyethyleneglycol.

Encapsulated : Insoluble fragrance delivery technology utilising perfume particles zeolite 1 3x, perfume and a dextrose/glycerin agglomerating binder.

CA 02263430 l999-02-ll W O ~8~'~7~23 PCTrUS97/11544 Example 1:

Antibodies' production Chickens were injected in the breast muscle with 1 ml of a 1 mg/ml Carezyme~) emulsion. The Carezyme emulsion was prepared with a Freunds completed adjuvants (Freund and McDermott, 1942; Freund 1956) by intensively mixing an equal amount of the Carezyme solution (2 mg/ml) Freunds complete adjuvant.
The immunisation scheme was completed with injections using a Freunds uncomplete adjuvant and after a 4 weeks period, the eggs were collected during one week. The e)~lracRol~ of the antibodies from the eg~s yolks was done accor~Jing to the Polson extraction method as described in Immunological Investi~tion 19, 1990, pp 253-258.

Carezyme enzymatic inactivation A Carezyme stock solution was prepared in a Tris Buffer (5x10-2M Tris, 25 mM
NaCI, pH=8) and three Tris buffers (O.OSM KH2P04) were prepared at a pH of resr~ctively to 7, 8 and 9.5. The Carezyme solution was diluted in the Tris buffer to a final concel,l(ation of 0.6 CEVU/ml.
The carezyme preparalio,l was ina~ ted with the antibody solution (0.18 mg/ml) during 60 minutes at 30~C, 40~C and 50~C.
The resict~ Carezyme activity was measured according to the Illethod desaibed by Novo Nordisk publication AF253. Within 5 minutes, the enzymatic activity of Carezymo was completely blocked as shown in the table below.

Residual Carezyme(E9 activity (in % after 5 minutes) pH (Tris buffer) T=30~C T=40~C T=50~C

9.5 3 6 4 .. . . . .. . _ . . .

CA 02263430 l999-02-ll W O 98/07823 PCT~US97/11544 Example 2 The Carezyme(~)-directed antibodies were prepared according to the method described in example 1. The Carezyme enzymatic deactivation was measured into commercially available detergent soMtions comprising Ariel liquid (0.8% in city water, pH 8.5) and Ariel Color Futur (0.8% in city water, pH 9.5).

In example A, the same procedure as illustrated in example 1 was followed wherein the ina Ih~tion solution was added to the detergent solution.

In example B, the detergent sohltion already contained Carezyme at an initial level of 0.6 CEVUlml and the antibody was subsequently thereto added.

As shown in the table below, the Carezyme enzymatic activity in a detergenl sol~tion has been completely blocked by the additio-, of a Carezyme-directed - antibody in both instances.

Residual Car~ ."eactivity (in % after 5 minutes) Mix;nq sequence Ariel liquid solution Ariel Color Solution W O 98107823 PCT~US97/11544 Example 3 The following laundry detergent compositions were prepared in accord with the invention:

11 111 lV V Vl LAS 8.0 8.0 8.0 8.0 8.0 8.0 C25E3 3.4 3.4 3.4 3.4 3.4 3.4 QAS - 0.8 0.8 - 0.8 0.8 Zeolite A 18.1 18.1 18.1 18.1 18.1 18.1 Carbonate 13.0 13.0 13.0 27.0 27.0 27.0 Silicate 1.4 1.4 1.4 3.0 3.0 3.0 Sulfate 26.1 26.1 26.1 26.1 26.1 26.1 PB4 9.0 9.0 9.0 9.0 9.0 9.0 TAED 1.5 1.5. 1.5 1.5 1.5 1.5 DETPMP 0.25 0.25 0.25 0.25 0.25 0.25 H E D P 0.3 0.3 0.3 0.3 0.3 0.3 Protease 0.0026 0.0026 0.0026 0.0026 0.0026 0.0026 Amylase 0.0009 0.0009 0.0009 0.0009 0.0009 0.0009 Cellulase 0.0006 0.0006 0.008 0.03 0.005 0.05 Antibody 0.25 5 10E-1 1 10E-2 0.5 MA/M 0.3 0.3 0.3 0.3 0.3 0.3 CMC 0.2 0.2 0.2 0.2 0.2 0.2 Photoa~;~i./ated 15 15 15 15 15 15 bleach (ppm) Brightener 1 0.09 0.09 0.09 0.09 0.09 0.09 Perfume 0.3 0.3 0.3 0.3 0.3 0.3 Silicone anlir~din 0.5 0.5 0.5 0.5 0.5 0.5 Misc/minors to 100%
Densityin g/litre 850 850 850 850 850 850 . .

CA 02263430 l999-02-ll Example 4 The following granular laundry detergent compositions of bulk density 750 g/litre were prepared in accord with the invention:

ll lll LAS 5.25 5.61 4.76 TAS 1.25 1.86 1.57 C45AS - 2.24 3.89 C25AE3S - 0.76 1.18 C45E7 3.25 - 5.0 QAS 0.8 2.0 2.0 STPP 19.7 Zeolite A - 19.5 19.5 NaSKS-6/citricacid (79:21) - 10.6 10.6 Carbonate 6.1 21.4 21.4 Bicarbonate - 2.0 2.0 Silicate 6.8 Sodium sulfate 39.8 - 14.3 PB4 5.0 12.7 TAED 0.5 3.1 DETPMP 0.25 0.2 0.2 HEDP - 0.3 0.3 Antibody 0.02 0.1 Protease 0.0026 0.0005 0.045 Lipase 0.003 0.003 0.003 Cellulase 0.0006 0.0006 0.0006 Amylase 0.0009 0.0009 0.0009 MA/M 0.8 1.6 1.6 CMC 0.2 0.4 0.4 Photoactivated bleach 15 ppm 27 ppm 27 ppm (ppm) Brightener 1 0.08 0.19 0.19 Brightener 2 - 0.04 0.04 Encapsulated perfume 0.3 0.3 0.3 particles Silicone antifoam 0.5 2.4 2.4 Minors/misc to 100%

ExamPie S

The following detergent formulations, according to the present invention were prepared, where I is a phosphorus-containing detergent composition, ll is a zeolite-containing detergent composition and lll is a compact detergent composition:

Blown Powder STPP 24.0 - 24.0 Zeolite A - 24.0 C45AS 9.0 6.0 13.0 MA/M 2.0 4.0 2.0 LAS 6.0 8.0 11.0 TAS 2.0 Silicate 7.0 3.0 3.0 CMC 1.0 1.0 0.5 Brightener 2 0.2 0.2 0.2 Soap 1.0 1.0 1.0 DETPMP 0.4 0.4 0.2 Spray On C45E7 2.5 2.5 2.0 C25E3 2.5 2.5 2.0 Silicone ar,lirod.,~ 0.3 0.3 0.3 Perfume 0.3 0.3 0.3 Dry additives Carbonate 6.0 13.0 15.0 PB4 18.0 18.0 10.0 PB1 4.0 4.0 0 TAED 3.0 3.0 1.0 CA 02263430 1999-02-ll W 09~ 23 PCT~US97/11544 Photoactivated bleach 0.02 0.02 0.02 Protease 0.01 0.01 0.01 Lipase 0.009 0.009 0.009 Amylase 0.002 0.003 0.001 Cellulase 0.05 0.005 0 0005 Antibody 1 1 OE-1 1 OE-1 Dry mixed sodiumsulfate 3.0 3.0 5.0 Balance (Moisture & 100.0 100.0 100.0 Miscellaneous) Density (g/litre) 630 670 670 Example 6 The following nil bleach-containing detergent formulations of particular use in the washing of colored clothing, according to the present invention were prepared:

Blown Powder Zeolite A 15.0 15.0 Sodium sulfate 0.0 5.0 LAS 3.0 3.0 DETPMP 0.4 0.5 CMC 0.4 0.4 MA/AA 4.0 4.0 ~gglomerates C45AS - - 11.0 LAS 6.0 5.0 TAS 3.0 2.0 Silicate 4.0 4.0 Zeolite A 10.0 15.0 13.0 CMC - - 0.5 MAIAA - - 2.0 Carbonate 9.0 7.0 7.0 Spray On Perfume 0.3 0.3 0.5 C45E7 4.0 4.0 4.0 C25E3 2.0 2.0 2.0 W O 98/07823 PCT~US97/11544 Dry additives MA/AA - - 3 ~
NaSKS-6 - - 12.0 Citrate 10.0 - 8.0 Bicarbonate 7.0 3.0 5.0 Carbonate 8.0 5.0 7.0 PVPVI/PVNO 0.5 0.5 0.5 Protease 0.026 0.016 0.047 Lipase 0.009 0.009 0.009 Amylase 0.005 0.005 0.005 Cellulase 0.006 0.006 0.006 Antibody 1 0.05 0.01 Silicone anliroar" 5.0 5.0 5.0 Dry additives Sodium sulfate 0.0 9.0 0.0 Balance (Moisture and 100.0 100.0 100.0 Misce"-neous) Density (g/litre) 700 700 700 W O ~ 3 PCTrUS97/11544 Example 7 The following detergent formulations, according to the present invention were prepared:
11 111 lV

LAS 20.0 14.0 24.0 22.0 QAS 0.7 1.0 - 0.7 TFM - 1.0 C25E5/C45E7 - 2.0 - 0.5 C45E3S - 2.5 STPP 30.0 18.0 30.0 22.0 Silicate 9.0 5.0 10.0 8.0 Carbonate 13.0 7.5 - 5.0 Bicarbonate - 7.5 - -DETPMP 0.7 1.0 SRP 1 0.3 0.2 - 0.1 MA/M 2.0 1.5 2.0 1.0 CMC 0.8 0.4 0.4 0.2 Protease 0.008 0.01 0.026 0.026 Amylase 0.007 0.004 - 0.002 Lipase 0.004 0.002 0.004 0.002 Cellulase 0.0015 0.0005 0.05 0.005 Antibody 0.003 0.001 1 0.01 Photoactivated 70ppm 45ppm - 1 Oppm bleach (ppm) Brightener 1 0.2 0.2 0.08 0.2 PB1 6.0 2.0 NOBS 2.0 1.0 Balance (Moisture 100 100 100 100 and Miscell~neous) W O 9~ /o23 PCTrUS97/11544 59 Example 8 The following detergent formulations, according to the present invention were prepared:

11 111 lV

Blown Powder Zeolite A 30.0 22.0 6.0 6.7 Na SkS-6 - - 3.3 Polycarboxylate - - - 7.1 Sodium sulfate 19.0 5.0 7.0 MA/M 3.0 3.0 6.0 LAS 14.0 12.0 22.0 21.5 C45AS 8.0 7.0 7.0 5.5 Cationic - - - 1.0 Silicate - 1.0 5.0 11.4 Soap - - 2.0 Brightener 1 0.2 0.2 0.2 Carbonate 8.0 16.0 20.0 10.0 DETPMP - 0.4 0.4 Spray On C45E7 1.0 1.0 1.0 3.2 Dry additives PVPVIIPVNO 0.5 0.5 0.5 Antibody 0.005 0.005 0.005 0.005 Protease 0.052 0.01 0.01 0.01 Lipase 0.009 0.009 0.009 0.009 Amylase 0.001 0.001 0.001 0.001 Cellulase 0.0002 0.001 0.0002 0.001 NOBS - 6.1 4.5 3.2 PB1 1.0 5.0 6.0 3.9 Sodium sulfate - 6.0 - to balance Balance (Moisture and 100 100 100 Miscellaneous) CA 02263430 1999-02-ll PCTrUS97/11544 Example 9 The following high density and bleach-containing detergent formulations, according to the present invention were prepared:

Blown Powder Zeolite A 15.0 15.0 15.0 Sodium sulfate 0.0 5.0 0.0 LAS 3.0 3.0 3.0 QAS - 1.5 1.5 DETPMP 0.4 0.4 0.4 CMC 0.4 0.4 0.4 MA/M 4.0 2.0 2.0 Agglomerates LAS 5.0 5.0 5.0 TAS 2.0 2.0 1.0 Silicate 3.0 3.0 4.0 Zeolite A 8.0 8.0 8.0 Carbonate 8.0 8.0 4.0 Spray On Perfume 0.3 0.3 0.3 C45E7 2.0 2.0 2.0 C25E3 2.0 - -Dry additives Citrate 5.0 - 2.0 Bicarbonate - 3.0 Carbonate 8.0 15.0 10.0 TAED 6.0 2.0 5.0 PB1 14.0 7.0 10.0 Polyethylene oxide of MW - - 0.2 5,000,000 Bentonite clay - - 10.0 Antibody 0.1 0.1 0.1 Protease 0.01 0.01 0.01 CA 02263430 1999-02-ll PCT~US97/11544 Lipase 0.009 0.009 0.009 Amylase 0.005 0.005 0.005 Cellulase 0.002 0.0006 0.002 Silicone antifoam 5.0 5.0 5.0 Dry additives Sodium sulfate 0.0 3.0 0.0 Balance (Moisture and 100.0 100.0 100.0 Miscellaneous) Density (g/litre) 850 850 850 . ~ . .....

CA 02263430 1999-02-ll W O 98t07823 PCT~US97/11544 Example 10 The following high density detergent formulations, according to the present invention were prepared:

ll Ag~lomerate C45AS 11.0 14.0 Zeolite A 15.0 6.0 Carbonate 4.0 8.0 MA/M 4.0 2.0 CMC 0.5 0 5 DETPMP 0.4 0.4 Spray On Perfume 0.5 0.5 Dry Adds HEDP 0.5 0.3 SKS 6 13.0 10.0 Citrate 3.0 1.0 TAED 5.0 7.0 P~r~r~onate 20.0 20.0 SRP 1 0.3 0.3 Antibody 0. 1 Protease 0.014 0.014 Lipase 0.009 0.009 Cell~ se 0.001 0.0006 Arnylase 0.005 0.005 Silicone ~ Itiroa~ 5.0 5.0 Bri$~h~e"er 1 0.2 0.2 Brightener 2 0.2 Balance (Moisture and 100 100 Miscellaneous) Density (g/litre) 850 850 CA 02263430 1999-02-ll W O 98/07823 PCT~US97/11544 Example 1 1 The following granular detergent formulations, according to the present invention were prepared:
11 111 lV V

LAS 21.0 25.0 18.0 18.0 Coco C12-14 AS - - - - 21.9 AE3S - - 1.5 1.5 2.3 Decyl di,netl,yl hydroxyethyl - 0.4 0.7 0.7 0.8 NH4+CI
Nonionic 1.2 - 0.9 0.5 Coco C12-14 Fatty Alcohol - - - - 1.0 STPP 44.0 25.0 22.5 22.5 22.5 Zeolite A 7.0 10.0 - - 8.0 SRP1 0.3 0.15 0.2 0.1 0.2 CMC 0.3 2.0 0.75 0.4 1.0 Carbonate 17.5 29.3 5.0 13.0 15.0 Silicate 2.0 - 7.6 7.9 Antibody 1 0.01 0.005 0.01 0.0001 Protease 0.007 0.007 0.007 0.007 0.007 Amylase - 0.004 0.004 0.004 0.004 Lipase 0.003 0.003 0.003 Cellulase 0.001 0.001 0.001 0.001 0.001 NOBS - - - 1.2 1.0 PB1 - - - 2.4 1.2 Diethylene triamine penta - - - 0.7 1.0 acetic acid Diethylene triamine penta - - 0.6 methyl phosphonic acid Mg Sulfate - - 0.8 Pl~otoacti~rated bleach 45 50 ppm 15 45 ppm 42 ppm ppm ppm Bri~htener 1 0.05 - 0.04 0.04 0.0 Briyhle. .er 2 0.1 0.3 0.05 0.13 0.13 Water and Minors up to 100%

CA 02263430 l999-02-ll W O 3~ 7~23 PCT~US97/11544 Example 12 The following liquid detergent formulations, according to the present invention were prepared:

11 111 lV V Vl Vll Vlll LAS 10.0 13.0 9.0 - 25.0 C25AS 4.0 1.0 2.0 10.0 - 13.0 18.0 15.0 C25E3S 1.0 - - 3.0 - 2.0 2.0 4.0 C25E7 6.0 8.0 13.0 2.5 - - 4.0 4.0 TFM - - - 4.5 - 6.0 8.0 8.0 QAS - - - - 3.0 1.0 TPKFA 2.0 - 13.0 2.0 - 15.0 7.0 7.0 Rapeseed fatty - - - 5.0 - - 4.0 4.0 acids Citric 2.0 3.0 1.0 1.~ 1.0 1.0 1.0 1.0 Dodecenyl/ 12.0 10.0 - - 15.0 tetradecenyl succinic acid Oleic acid 4.0 2.0 1.0 - 1.0 - - -Ethanol 4.0 4.0 7.0 2.0 7.0 2.0 3.0 2.0 1,2 Propanediol 4.0 4.0 2.0 7.0 6.0 8.0 10.0 13.-Mono Ethanol - - - 5.0 - - 9.0 9.0 Amine Tri Ethanol - - 8 Amine NaOH (pH) 8.0 8.0 7.6 7.7 8.0 7.5 8.0 8.2 Ethoxylated 0.5 - 0.5 0.2 - - 0.4 0.3 tetraethylene pentamine DETPMP 1.0 1.0 0.5 1.0 2.0 1.2 1.0 SRP 2 0.3 - 0.3 0.1 - - 0.2 0.1 PVNO - - - - - - - 0.10 Antibody 0.01 0.005 0.1 0.02 1 0.05 0.01 0.000 W O 98/07823 PCTrUS97111544 Protease. 005 . 005 . 004 . 003 0. 08 . 005 . 003 . 006 Lipase - .002 - .001 - - 003 003 Amylase .002 .002 .005 .004 .002 .008 .005 .005 Cellulase .005 .002 .005 0.000 .002 .005 0.000 0.000 Boric acid 0.1 0.2 - 2.0 1.0 1.5 Z.5 2.5 Na formate - - 1.0 Ca chloride - 0.015 - 0.01 Bentonite clay - - - - 4.0 4.0 Suspending clay - - - - 0.6 0.3 Balance Moisture and Miscellaneous: Up to 100%

CA 02263430 1999-02-ll PCTrUS97/11544 W O 9~ 23 Example 13 Granular fabric cleaning compositions which provide "softening through the wash" capability were prepared in accord with the present invention:

ll 45AS - 10.0 LAS 7.6 68AS 1.3 45E7 4.0 25E3 - 5.0 Coco-alkyl-dimethyl hydroxy- 1.4 1.0 ethyl ammonium chloride Citrate 5.0 3.0 Na-SKS~ - 11.0 Zeolite A 15.0 15.0 MA/M 4.0 4.0 PB1 1 5.0 Percarbonate - 15.0 TAED 5.0 5.0 Smectite clay 10.0 10.0 HMWPEO - 0.1 Antibody 0.01 0.5 Protease 0.02 0.01 Lipase 0.02 0.01 Amylase 0 03 0.005 Cellul~se 0.001 0.05 Silicate 3.0 5.0 Carbonate 10.0 10.0 Granular suds suppressor 1.0 4.0 CMC 0.2 0.1 Water/minors Up to 100%

W O 98/07823 PCT~US97111544 ExamPIe 14 The following rinse added fabric softener composition was prepared in accord with the present invention:
Softener active 20.0 Antibody 0.003 Amylase o.oo1 Cellulase 0.001 HCL ~~
A"liroa,n agent 0.01 Blue dye 25ppm CaCI2 0.20 Perfume o.go Water / minors Up to 100%

ExamPle 15 The following fabric softener composition was prepared in accord with the present invention:

DEQA 2.6 19.0 SDASA - - 70.0 Stearic acid of IV=0 0.3 Neodol 45-13 - - 13.0 Hydrochloride acid 0.02 0.02 Ethanol - - 1.0 PEG - 0.6 Antibody 0.1 1 0.0003 Cellul~se 0.05 0.003 0.001 Perfume 1.0 1.0 0.75 Di~erai!yl Succinate - - 0.38 Silicone anliro~,n 0.01 0.01 Electrolyte - 600ppm Dye 1 OOppm 50ppm 0.01 Water and minors 100% 100%
-CA 02263430 1999-02-ll WO 9~J'~7023 PCT~US97/11544 Example 16 Syndet bar fabric cleaning compositions were prepared in accord with the present invention:

11 111 lV
C26 AS 20.0 20.0 20.0 20.0 CFAA 5.0 5.0 5.0 50 LAS (C1 1-13) 10.0 10.0 10.0 10 0 Sodium carbonate 25.0 25.0 25.0 25.0 Sodium pyrophosphate 7.0 7.0 7.0 7.0 STPP 7.0 7.0 7.0 7.0 Zeolite A 5.0 5.0 5.0 5 0 CMC 0.2 0.2 0.2 0.2 Polyacrylate (MW 1400) 0.2 0.2 0.2 0.2 Coconutmonethanolamide 5.0 5.0 5.0 5.0 Antibody 0.01 0.05 0.07 0.1 Cellulase 0.001 0.02 0.03 0.05 Amylase 0.01 0.02 0.01 0.01 Protease 0.3 0.5 0.05 Brightener, perfume 0.2 0.2 0.2 0.2 CaS04 1.0 1.0 1.0 1.0 MsSO4 1.0 1.0 1.0 1.0 Water 4.0 4.0 4.0 4.0 Filler~: balance to 100%

~Can be selected from convenient materials such as CaC03, talc, clay (Kaolinite,Sroectile), silicates, and the like.

Example 17 Detergent additives were prepared in accord with the present invention:
ll lll Zeolite A 35 Prutease - - 0.3 ce~ se o. 1 - o~ 1 Antibody 1 OE I 1 1 OE~1 1 OEO

Claims (13)

WHAT IS CLAIMED IS:

1. A detergent composition comprising a cellulase and a cellulase-directed antibody.

2. A detergent composition according to claim 1 wherein said cellulase-directed antibody is comprised at a level of from 10E-6% to 10E+1% by weight of total composition.

3. A detergent composition according to claims 1-2 wherein the cellulase is selected from "50kD endoglucanase derived from Humicola Insulens, DSM
1800 and/or 43kD endoglucanase derived from Humicola Insulens, DSM
1800.

4. A detergent composition according to claims 1-3 wherein the cellulase is comprised at a level of from 0.0001% to 2%, preferably from 0.0001% to 0.5%, more preferably from 0.001% to 0.1% of pure enzyme by weight of total composition.

5. A detergent composition according to claims 14 wherein the molecular ratio of cellulose-directed antibody to cellulase is equal or less than 100:1, preferably equal or less than 50:1.

6. A detergent composition according to claims 1-5 wherein said antibody is a monoclonal antibody, preferably a fragment thereof.

7. A detergent composition according to claim 6 wherein the molecular ratio of said cellulase-directed antibody to cellulase is equal or less than 50:1, preferably equal or less than 20:1.

8. A detergent composition according to claims 1-7, wherein said cellulase-directed antibody is incorporated into a release agent.

9. A detergent composition according to any of the preceding claims further comprising one or more components selected from anionic, nonionic, cationic, amphoteric and zwitterionic surfactants, builder, bleach system, suds suppressors, soil release polymer, lime soap dispersant, soil suspension and anti-redeposition agents, smectite clays and/or mixtures thereof.

10. A detergent composition according to any of the preceding claims which is in the form of a liquid, granular, powder, gel, paste or bar.

11. A detergent additive comprising a cellulase-directed antibody.

12. A detergent additive according to claim 11 further comprising a cellulase.

13. Use of a cellulase-directed antibody in a detergent composition for controlling the cellulolytic enzymatic activity.