WO2009019076A1

WO2009019076A1 - Enzyme delivery device

Info

Publication number: WO2009019076A1
Application number: PCT/EP2008/058295
Authority: WO
Inventors: Panos Kotsakis; Neil James Parry
Original assignee: Unilever Plc; Unilever N.V.; Hindustan Unilever Limited
Priority date: 2007-08-03
Filing date: 2008-06-27
Publication date: 2009-02-12
Also published as: EP2171027A1

Abstract

A low surfactant or surfactant-free process for washing fabrics in a washing machine comprising the steps of treating the fabrics with one or more enzymes and agitating the fabrics with a secondary agitation device in the washing machine; and a secondary agitation device for use in a primary agitation device said primary agitation device comprising a washing machine, and the secondary agitation device containing one or more enzymes for use in the low surfactant or surfactant-free fabric washing process.

Description

Enzyme delivery Device

The present invention concerns the delivery of enzymes in a washing process.

Laundry compositions which are aimed at effective stain removal are generally multi-component compositions containing, at the very least a surfactant.

An objective is to provide an improved washing process with improved stain removal by enzymes. Reducing the chemical loading and replacement by sustainable or more environmentally friendly technologies or processes are needed without compromising the cleaning performance.

Accordingly, in a first aspect, the present invention provides a low surfactant or surfactant-free process for washing fabrics in a washing machine comprising the steps of

1. treating the fabrics with one or more enzymes 2. agitating the fabrics with a secondary agitation device in the washing machine; the secondary agitation device according to any of claims 11-15.

The steps of the above process are preferably carried out during overlapping time periods and are further preferably carried out substantially simultaneously.

In another aspect the invention provides a secondary agitation device for use in a primary agitation device such as a washing machine, the secondary agitation device containing one or more enzymes for use in the low surfactant or surfactant-free fabric washing process.

Preferably delivery of the one or more enzymes is via the agitation device.

Even further preferably the one or more enzymes are contained in or on the agitation device at the start of the washing process. Accordingly the agitation device may contain one or more filling/dispensing apertures.

The agitation device may be hollow or contain one or more hollow portions for containing the enzymes

The agitation device may be any shape, such as spherical. The device may be rigid or flexible.

Preferably the device contains one or more projections for increasing mechanical agitation. Preferably said projections may be rigid or semi rigid.

The term "low surfactant or surfactant free" as used herein means: For washing liquid compositions 0 - 40% of the compositions, more preferably 0 - 20% of the compositions and even more preferably 0 - 10% of the composition. For particulates 0 - 20 % of the composition, more preferably 0 - 10% of the, and even more preferably 0 - 5% of the composition .

By "particulates" it is meant herein to include powders, agglomerates, granules, Surprisingly, this particular sequence improves stain removal despite the low levels or even the absence of surfactant .

The enzymes may be in any suitable form such as granular.

The enzymes may be contained in water soluble packaging such as water soluble capsules. Said water soluble packaging may be rigid or flexible. Said water soluble packaging may comprise PVA or other water soluble polymeric film packaging.

It is to be understood that enzyme variants (produced, for example, by recombinant techniques) are included within the meaning of the term "enzyme". Examples of such enzyme variants are disclosed, e.g., in EP 251,446 (Genencor) , WO 91/00345 (Novo Nordisk) , EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV) .

The types of enzymes which may appropriately be incorporated in granules of the invention include oxidoreductases, transferases hydrolases, lyases, isomerases and ligases, that is, respectively (EC 1. -.-.-), (EC 2.-.-.-), (EC 3.-.- .-), (EC 4.-.-.-), (EC 5.-.-.-), (EC 6.-.-.-), wherein such enzyme classification is in accordance with Recommendations (1992) of the Nomenclature Committee of the International

Union of Biochemistry and Molecular Biology, Academic Press, Inc., 1992. Especially contemplated enzymes include proteases, alpha- amylases, cellulases, lipases, peroxidases/oxidases, pectate lyases, and mannanases, or mixtures thereof.

Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. The protease may be a serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279) . Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270 and WO 94/25583.

Examples of useful proteases are the variants described in WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274. Preferred commercially available protease enzymes include Alcalase™, Savinase™, Primase™, Duralase™, Dyrazym™, Esperase™, Everlase™, Polarzyme™, and Kannase™, (Novozymes A/S) , Maxatase™, Maxacal™, Maxapem™, Properase™, Purafect™, Purafect OxP™, FN2™, and FN3™ (Genencor International Inc.) .

Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces) , e.g. from H. lanuginosa (T. lanuginosus) as described in EP 258 068 and EP 305 216 or from H. insolens as described in WO 96/13580, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P. stutzeri (GB 1,372,034), P. fluorescens, Pseudomonas sp . strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), a Bacillus lipase, e.g. from B. subtilis (Dartois et al . (1993), Biochemica et Biophysica Acta, 1131, 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422) .

Other examples are lipase variants such as those described in WO 92/05249, WO 94/01541, EP 407 225, EP 260 105, WO 95/35381, WO 96/00292, WO 95/30744, WO 94/25578,

WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202.

Preferred commercially available lipase enzymes include Lipolase™ and Lipolase Ultra™, Lipex™ (Novozymes A/S) .

The method of the invention may be carried out in the presence of cutinase. classified in EC 3.1.1.74. The cutinase used according to the invention may be of any origin. Preferably cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.

Cutinases are enzymes which are able to degrade cutin. In a preferred embodiment, the cutinase is derived from a strain of Aspergillus, in particular Aspergillus oryzae, a strain of Alternaria, in particular Alternaria brassiciola , a strain of Fusarium, in particular Fusarium solani, Fusarium solani pisi, Fusarium roseum culmorum, or Fusarium roseum sambucium, a strain of Helminthosporum, in particular Helminthosporum sativum, a strain of Humicola, in particular Humicola insolens, a strain of Pseudomonas, in particular Pseudomonas mendocina, or Pseudomonas putida, a strain of Rhizoctonia, in particular Rhizoctonia solani, a strain of Streptomyces, in particular Streptomyces scabies, or a strain of Ulocladium, in particular Ulocladium consortiale. In a most preferred embodiment the cutinase is derived from a strain of Humicola insolens, in particular the strain

Humicola insolens DSM 1800. Humicola insolens cutinase is described in WO 96/13580 which is herby incorporated by reference. The cutinase may be a variant, such as one of the variants disclosed in WO 00/34450 and WO 01/92502, which are hereby incorporated by reference. Preferred cutinase variants include variants listed in Example 2 of WO 01/92502, which is hereby specifically incorporated by reference .

Preferred commercial cutinases include NOVOZYM™ 51032 (available from Novozymes A/S, Denmark) .

The method of the invention may be carried out in the presence of phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32. As used herein, the term phospholipase is an enzyme which has activity towards phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol . Phospholipases are enzymes which participate in the hydrolysis of phospholipids. Several types of phospholipase activity can be distinguished, including phospholipases Ai and A₂ which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B) which can hydrolyze the remaining fatty acyl group in lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterases) release diacyl glycerol or phosphatidic acid respectively.

The term phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (Ai or A₂), phospholipase B activity, phospholipase C activity or phospholipase D activity. The term "phospholipase A" used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase Ai and/or Phospholipase A₂ activity. The phospholipase activity may be provided by enzymes having other activities as well, such as, e.g., a lipase with phospholipase activity. The phospholipase activity may, e.g., be from a lipase with phospholipase side activity. In other embodiments of the invention the phospholipase enzyme activity is provided by an enzyme having essentially only phospholipase activity and wherein the phospholipase enzyme activity is not a side activity.

The phospholipase may be of any origin, e.g., of animal origin (such as, e.g., mammalian), e.g. from pancreas (e.g., bovine or porcine pancreas), or snake venom or bee venom. Preferably the phospholipase may be of microbial origin, e.g., from filamentous fungi, yeast or bacteria, such as the genus or species Aspergillus , e.g., A. niger; Dictyostelium, e.g., D. discoideum; Mucor, e.g. M. javanicus , M. mucedo, M. subtilissimus; Neurospora, e.g. N. crassa; Rhizomucor, e.g.,

R. pusillus; Rhizopus , e.g. R. arrhizus , R. japonicus , R. stolonifer; Sclerotinia , e.g., 5. libertiana; Trichophyton, e.g. T. rubrum; Whetzelinia, e.g., W. sclerotiorum;

Bacillus , e.g., B. megaterium, B. subtilis; Citrobacter, e.g., C. freundii; Enterobacter, e.g., E. aerogenes , E. cloacae Edwardsiella , E. tarda; Erwinia , e.g., E. herbicola;

Escherichia, e.g., E. coll; Klebsiella, e.g., K. pneumoniae; Proteus, e.g., P. vulgaris; Providencia , e.g., P. stuartii;

Salmonella, e.g. 5. typhimurium; Serratia, e.g., 5. liquefasciens , S. marcescens; Shigella , e.g., 5. flexneri;

Streptomyces , e.g., 5. violeceoruber; Yersinia, e.g., Y. enterocolitica . Thus, the phospholipase may be fungal, e.g., from the class Pyrenomycetes, such as the genus

Fusarium, such as a strain of F. culmorum, F. heterosporum,

F. solani, or a strain of F. oxysporum. The phospholipase may also be from a filamentous fungus strain within the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger or Aspergillus oryzae.

Preferred phospholipases are derived from a strain of Humicola, especially Humicola lanuginosa . The phospholipase may be a variant, such as one of the variants disclosed in WO 00/32758, which are hereby incorporated by reference. Preferred phospholipase variants include variants listed in Example 5 of WO 00/32758, which is hereby specifically incorporated by reference. In another preferred embodiment the phospholipase is one described in WO 04/111216, especially the variants listed in the table in Example 1. In another preferred embodiment the phospholipase is derived from a strain of Fusarium, especially Fusarium oxysporum. The phospholipase may be the one concerned in WO 98/026057 derived from Fusarium oxysporum DSM 2672, or variants thereof.

In a preferred embodiment of the invention the phospholipase is a phospholipase Ai (EC. 3.1.1.32) . In another preferred embodiment of the invention the phospholipase is a phospholipase A₂ (EC .3.1.1.4. ) .

Examples of commercial phospholipases include LECITASE™ and LECITASE™ ULTRA, YIELSMAX, or LIPOPAN F (available from Novozymes A/S, Denmark) .

Suitable amylases (alpha and/or beta) include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g. a special strain of B. lichen!formis, described in more detail in GB 1,296,839, or the Bacillus sp . strains disclosed in WO 95/026397 or WO 00/060060.

Examples of useful amylases are the variants described in WO 94/02597, WO 94/18314, WO 96/23873, WO 97/43424, WO

01/066712, WO 02/010355, WO 02/031124 and PCT/DK2005/000469 (which references all incorporated by reference.

Commercially available amylases are Duramyl™, Termamyl™, Termamyl Ultra™, Natalase™, Stainzyme™, Fungamyl™ and BAN™ (Novozymes A/S) , Rapidase™ and Purastar™ (from Genencor International Inc.) .

Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila , and Fusarium oxysporum disclosed in US

4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, WO 89/09259, WO 96/029397, and WO 98/012307.

Especially suitable cellulases are the alkaline or neutral cellulases having color care benefits. Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940. Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471, WO 98/12307 and PCT/DK98/00299.

Commercially available cellulases include Celluzyme™, Carezyme™, Endolase™, Renozyme™ (Novozymes A/S) , Clazinase™ and Puradax HA™ (Genencor International Inc.), and KAC- 500 (B)™ (Kao Corporation) .

Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include Guardzyme™ and Novozym™ 51004 (Novozymes A/S) .

Examples of pectate lyases include pectate lyases that have been cloned from different bacterial genera such as Erwinia , Pseudomonas , Klebsiella and Xanthomonas, as well as from Bacillus subtilis (Nasser et al . (1993) FEBS Letts. 335:319- 326) and Bacillus sp . YA- 14 (Kim et al . (1994) Biosci. Biotech. Biochem. 58:947-949) . Purification of pectate lyases with maximum activity in the pH range of 8-10 produced by Bacillus pumilus (Dave and Vaughn (1971) J. Bacterid. 108:166-174), B. polymyxa (Nagel and Vaughn (1961) Arch. Biochem. Biophys. 93:344-352), B. stearothermophilus (Karbassi and Vaughn (1980) Can. J.

Microbiol. 26:377-384), Bacillus sp . (Hasegawa and Nagel (1966) J. Food Sci. 31:838-845) and Bacillus sp . RK9 (Kelly and Fogarty (1978) Can. J. Microbiol. 24:1164-1172) have also been described. Any of the above, as well as divalent cation-independent and/or thermostable pectate lyases, may be used in practicing the invention. In preferred embodiments, the pectate lyase comprises the amino acid sequence of a pectate lyase disclosed in Heffron et al . , (1995) MoI. Plant-Microbe Interact. 8: 331-334 and Henrissat et al., (1995) Plant Physiol. 107: 963-976. Specifically contemplated pectatel lyases are disclosed in WO 99/27083 and WO 99/27084. Other specifically contemplates pectate lyases derived from Bacillus lichen!formis is disclosed in US patent no. 6,284,524 (which document is hereby incorporated by reference) . Specifically contemplated pectate lyase variants are disclosed in WO 02/006442, especially the variants disclosed in the Examples in WO 02/006442 (which document is hereby incorporated by reference) .

Examples of commercially available alkaline pectate lyases include BIOPREP™ and SCOURZYME™ L from Novozymes A/S, Denmark .

Examples of mannanases (EC 3.2.1.78) include mannanases of bacterial and fungal origin. In a specific embodiment the mannanase is derived from a strain of the filamentous fungus genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus (WO 94/25576) . WO 93/24622 discloses a mannanase isolated from Trichoderma reseei. Mannanases have also been isolated from several bacteria, including Bacillus organisms. For example, Talbot et al . , Appl . Environ. Microbiol., Vol.56, No. 11, pp. 3505-3510 (1990) describes a beta-mannanase derived from Bacillus stearothermophilus . Mendoza et al . , World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a beta-mannanase derived from Bacillus subtilis . JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp . JP-A- 63056289 describes the production of an alkaline, thermostable beta-mannanase. JP-A-63036775 relates to the Bacillus microorganism FERM P-8856 which produces beta- mannanase and beta-mannosidase . JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp . AM- 001. A purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active. Contemplated are the alkaline family 5 and 26 mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp . , and Humicola insolens disclosed in WO 99/64619. Especially contemplated are the Bacillus sp . mannanases concerned in the Examples in WO 99/64619 which document is hereby incorporated by reference.

Examples of commercially available mannanases include Mannaway™ available from Novozymes A/S Denmark.

Any enzyme present in the composition may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708.

The process of the invention does not require surfactants however it may utilise other components such as perfume etc.

The present invention is suitable for use in industrial or domestic fabric wash compositions, fabric conditioning compositions and compositions for both washing and conditioning fabrics (so-called through the wash conditioner compositions) . The present invention can also be applied to industrial or domestic non-detergent based fabric care compositions, for example spray-on compositions. Fabric wash compositions according to the present invention may be in any suitable form, for example powdered, tableted powders, liquid or solid detergent bars.

Other contemplated ingredients including surfactants, hydrotropes, preservatives, fillers, builders, complexing agents, polymers, stabilizers, perfumes per se, other conventional detergent ingredients, or combinations of one or more thereof are discussed below.

The composition may comprise one or more polymers. Examples are carboxymethylcellulose, poly (vinylpyrrolidone) , poly (ethylene glycol), poly (vinyl alcohol), poly (vinylpyridine- N-oxide) , poly (vinylimidazole) , polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.

Modern detergent compositions typically employ polymers as so-called ^λdye-transfer inhibitors' . These prevent migration of dyes, especially during long soak times. Any suitable dye-transfer inhibition agents may be used in accordance with the present invention. Generally, such dye- transfer inhibiting agents include polyvinyl pyrrolidone polymers, polyamine N-oxide polymers, copolymers of N- vinylpyrrolidone and N-vinylimidazole, manganese pthalocyanine, peroxidases, and mixtures thereof.

Nitrogen-containing, dye binding, DTI polymers are preferred. Of these polymers and co-polymers of cyclic amines such as vinyl pyrrolidone, and/or vinyl imidazole are preferred. Polyamine N-oxide polymers suitable for use herein contain units having the following structural formula: R-A_x-P; wherein P is a polymerizable unit to which an N-O group can be attached or the N-O group can form part of the polymerizable unit; A is one of the following structures: - NC(O)-, -C(O)O-, -S-, -0-, -N=; x is 0 or 1; and R is an aliphatic, ethoxylated aliphatic, aromatic, heterocyclic or alicyclic group or combination thereof to which the nitrogen of the N-O group can be attached or the N-O group is part of these groups, or the N-O group can be attached to both units. Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine and derivatives thereof. The N-O group can be represented by the following general structures: N(O) (R') 0-3 , or =N(0) (R') 0-1 , wherein each R' independently represents an aliphatic, aromatic, heterocyclic or alicylic group or combination thereof; and the nitrogen of the N-O group can be attached or form part of any of the aforementioned groups. The amine oxide unit of the polyamine N-oxides has a pKa<10, preferably pKa<7, more preferably pKa<6.

Any polymer backbone can be used provided the amine oxide polymer formed is water-soluble and has dye transfer inhibiting properties. Examples of suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamides, polyimides, polyacrylates and mixtures thereof. These polymers include random or block copolymers where one monomer type is an amine N-oxide and the other monomer type is an N-oxide. The amine N-oxide polymers typically have a ratio of amine to the amine N- oxide of 10:1 to 1:1,000,000. However, the number of amine oxide groups present in the polyamine oxide polymer can be varied by appropriate copolymerization or by an appropriate degree of N-oxidation. The polyamine oxides can be obtained in almost any degree of polymerization. Typically, the average molecular weight is within the range of 500 to 1,000,000; more preferably 1,000 to 500,000; most preferably 5,000 to 100,000. This preferred class of materials is referred to herein as "PVNO". A preferred polyamine N-oxide is poly (4-vinylpyridine-N-oxide) which as an average molecular weight of about 50,000 and an amine to amine N- oxide ratio of about 1:4.

Copolymers of N-vinylpyrrolidone and N-vinylimidazole polymers (as a class, referred to as "PVPVI") are also preferred. Preferably the PVPVI has an average molecular weight range from 5,000 to 1,000,000, more preferably from 5,000 to 200,000, and most preferably from 10,000 to 20,000, as determined by light scattering as described in Barth, et al . , Chemical Analysis, Vol. 113. "Modern Methods of Polymer Characterization". The preferred PVPVI copolymers typically have a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1:1 to 0.2:1, more preferably from 0.8:1 to 0.3:1, most preferably from 0.6:1 to 0.4:1. These copolymers can be either linear or branched. Suitable PVPVI polymers include Sokalan^(TM) HP56, available commercially from BASF, Ludwigshafen, Germany.

Also preferred as dye transfer inhibition agents are polyvinylpyrrolidone polymers ("PVP") having an average molecular weight of from about 5,000 to about 400,000, preferably from about 5,000 to about 2000,000, and more preferably from about 5,000 to about 50,000. PVP ' s are disclosed for example in EP-A-262,897 and EP-A-256, 696. Suitable PVP polymers include Sokalan^(TM) HP50, available commercially from BASF. Compositions containing PVP can also contain polyethylene glycol ("PEG") having an average molecular weight from about 500 to about 100,000, preferably from about 1,000 to about 10,000. Preferably, the ratio of PEG to PVP on a ppm basis delivered in wash solutions is from about 2:1 to about 50:1, and more preferably from about 3:1 to about 10:1.

Also suitable as dye transfer inhibiting agents are those from the class of modified polyethyleneimine polymers, as disclosed for example in WO-A-0005334. These modified polyethyleneimine polymers are water-soluble or dispersible, modified polyamines. Modified polyamines are further disclosed in US-A-4, 548, 744 ; US-A-4, 597, 898 ; US-A- 4,877,896; US-A- 4,891, 160; US-A- 4,976,879; US-A- 5,415,807; GB-A-1 , 537 , 288 ; GB-A-1 , 498 , 520 ; DE-A-28 29022; and JP-A-O 6313271.

Preferably the composition according to the present invention comprises a dye transfer inhibition agent selected from polyvinylpyrridine N-oxide (PVNO) , polyvinyl pyrrolidone (PVP), polyvinyl imidazole, N-vinylpyrrolidone and N-vinylimidazole copolymers (PVPVI), copolymers thereof, and mixtures thereof.

The amount of dye transfer inhibition agent in the composition according to the present invention will be from - I i

0.01 to 10 %, preferably from 0.02 to 5 %, more preferably from 0.03 to 2 %, by weight of the composition.

Other Detergent ingredients : The composition may also contain other conventional detergent ingredients such as e.g. fabric conditioners including clays, foam boosters, suds suppressors (anti- foams) , anti-corrosion agents, soil-suspending agents, anti- soil redeposition agents, further dyes, anti-microbials, optical brighteners, tarnish inhibitors, or perfumes.

Examples

Example 1

Wash Evaluation of protease and a lipase in grass stain removal (washing machine)

Wash performance was evaluated by washing multi-stains under 4 conditions (1) No actives (2) in the presence of enzymes (protease, lipase) (3) an agitation tool (4) enzymes together with an agitation tool as in Fig 1.

Wash: VLD 00 multistains were washed together with 2kg cotton/ polycotton ballast in a Miele washing machine, under European conditions at 40⁰C for 30 min , with 2 x 10 min rinse cycles. The wash balls containing PVA capsule blanks, or PVA capsules loaded with lipex 10OT, savinase 24GTTwere placed in the proximity of the stain. The final concentration of each enzyme was lOmg/ 1 of liquor. Evaluation: Colour remission of the swatches was measured at

410 nm using a Hunterlab UltraScan

VIS remission spectrophotometer. The results are expressed as delta remission= (.Rafter wash-Λbefore wash) enzyme- (.Rafter wash-.Rbefore wash) control, where R is the remission at 410 nm using the CIE L*a*b* (CIELAB) values generated (figure 1) .

Table 1 : Wash performance in the presence and absence of a wash ball/ surfactant - values are Mean values

Large stains were washed with either a wash ball or with surfactant (LAS Neodol-25EO, 80:20) dosed in the machine drawer unit at 0.25, 0.5, 1, and 5g/l together with Q2-3302 antifoam (Dow Corning) . All washes were carried out in the presence of 3kg cotton/ polycotton ballast in a Miele washing machine, at 40⁰C for 30 min , FH=12, with 2 x 10 min rinse cycles. The wash balls containing PVA capsule blanks, or PVA capsules loaded with enzymes were secured in the proximity of the stain. The l*a*b and ΔE values of grass stains were obtained after wash using a Hunterlab calibrated against clean wfklOA (cotton) fabric. Results are expressed as stain removal index (SRI), where SRI= 100-ΔE_post-wash- Table 2 : Enzyme delivered inside agitation device vs enzymes delivered with (but not contained within) agitation device.

Various non-limiting embodiments of the invention will now be more particularly described with reference to the following figures in which:

Figure 1 shows a device according to the invention

Referring to the drawing a spherical agitation device is shown, 1 comprising a rigid plastic material and being covered in rigid projections 3 to increase agitation. The device further includes filling aperture 5 and dispensing apertures 7.

In one embodiment the device is a solid device. In a second embodiment the device is hollow and has a single opening for filling and dispensing. Granular enzyme is introduced contained in water soluble e.g. PVA capsules. The enzyme can either be loaded in the device or simply added to the wash at the same time as the agitation device is added.

It is of course to be understood that the invention is not intended to be restricted to the details of the above embodiment which are described by way of example only.

Claims

1. A low surfactant or surfactant-free process for washing fabrics in a washing machine and comprising the steps of 1. treating the fabrics with one or more enzymes

2. agitating the fabrics with a secondary agitation device in the washing machine; the secondary agitation device according to any of claims 11-15.

2. A low surfactant or surfactant-free process for washing fabrics according to claim 1 characterised in that the steps are carried out during overlapping time periods.

3. A low surfactant or surfactant-free process for washing fabrics according to any preceding claim characterised in that the steps are carried out substantially simultaneously.

4. A low surfactant or surfactant-free process for washing fabrics according to any preceding claim characterised in that the one or more enzymes is delivered via said secondary agitation device.

5. A low surfactant or surfactant-free process for washing fabrics according to any preceding claim characterised in that the one or more enzymes are contained in or on the second agitation device.

6. A low surfactant or surfactant-free process washing process according to any preceding claim characterised in that the surfactant concentration is 0-40% of a liquid composition .

7. A low surfactant or surfactant-free process washing process according to any preceding claim characterised in that the surfactant concentration is 0-20% of a liquid composition .

8. A low surfactant or surfactant-free process washing process according to any preceding claim characterised in that the surfactant concentration is 0-10% of a liquid composition .

9. A low surfactant or surfactant-free process washing process according to any preceding claim characterised in that the surfactant concentration is 0-20% of a powder composition .

10. A low surfactant or surfactant-free process washing process according to any preceding claim characterised in that the surfactant concentration is 0-10% of a powder composition .

11. A low surfactant or surfactant-free process washing process according to any preceding claim characterised in that the surfactant concentration is 0-5% of a powder composition .

12. A secondary agitation device for use in a primary agitation device said primary agitation device comprising a washing machine, and the secondary agitation device containing one or more enzymes for use in the low surfactant or surfactant-free fabric washing process according to any of the above claims.

13. A secondary agitation device according to claim 12 characterised in that said secondary agitation device is hollow or contains one or more hollow portions containing the enzymes.

14. A secondary agitation device according to claim 12 or 13 characterised in that the device comprises one or more filling/dispensing apertures

15. A secondary agitation device according to any of claims 12-14 characterised in that the agitation is generally spherical .

16. A secondary agitation device according to any of claims 12-15 characterised in that the agitation device comprising one or more projections.

17. A secondary agitation device according to any of claims 12-16 characterised in that said one or more projections are rigid or semi-rigid or a combination thereof.

18. A secondary agitation device according to any of claims 12-17 characterised in that the projections are 0.5-30 mm in length.

19. A secondary agitation device according to any of claims 12-18 characterised in that the projections are 5mm-3cm in diameter .

20. A secondary agitation device according to any of claims 12-19 characterised in that the projections are finger-like projections .

21. A secondary agitation device according to any of claims 12-20 characterised in that the projections are tapered e.g. in direction of the ends of the or each projection.