EP2171027A1 - Enzymabgabevorrichtung - Google Patents

Enzymabgabevorrichtung

Info

Publication number
EP2171027A1
EP2171027A1 EP08774457A EP08774457A EP2171027A1 EP 2171027 A1 EP2171027 A1 EP 2171027A1 EP 08774457 A EP08774457 A EP 08774457A EP 08774457 A EP08774457 A EP 08774457A EP 2171027 A1 EP2171027 A1 EP 2171027A1
Authority
EP
European Patent Office
Prior art keywords
surfactant
agitation device
washing
secondary agitation
enzymes
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP08774457A
Other languages
English (en)
French (fr)
Inventor
Panos Kotsakis
Neil James Parry
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Unilever PLC
Unilever NV
Original Assignee
Unilever PLC
Unilever NV
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Unilever PLC, Unilever NV filed Critical Unilever PLC
Priority to EP08774457A priority Critical patent/EP2171027A1/de
Publication of EP2171027A1 publication Critical patent/EP2171027A1/de
Withdrawn legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
    • C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06F—LAUNDERING, DRYING, IRONING, PRESSING OR FOLDING TEXTILE ARTICLES
    • D06F39/00—Details of washing machines not specific to a single type of machines covered by groups D06F9/00 - D06F27/00 
    • D06F39/02—Devices for adding soap or other washing agents
    • D06F39/024—Devices for adding soap or other washing agents mounted on the agitator or the rotating drum; Free body dispensers
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06F—LAUNDERING, DRYING, IRONING, PRESSING OR FOLDING TEXTILE ARTICLES
    • D06F35/00—Washing machines, apparatus, or methods not otherwise provided for
    • D06F35/005—Methods for washing, rinsing or spin-drying
    • D06F35/006—Methods for washing, rinsing or spin-drying for washing or rinsing only

Definitions

  • 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.
  • the present invention provides a low surfactant or surfactant-free process for washing fabrics in a washing machine comprising the steps of
  • the steps of the above process are preferably carried out during overlapping time periods and are further preferably carried out substantially simultaneously.
  • 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.
  • the one or more enzymes are contained in or on the agitation device at the start of the washing process.
  • 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.
  • the device contains one or more projections for increasing mechanical agitation.
  • said projections may be rigid or semi rigid.
  • low surfactant or surfactant free 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 .
  • pillates 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.
  • enzyme variants 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
  • 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.
  • 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 AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, DyrazymTM, EsperaseTM, EverlaseTM, PolarzymeTM, and KannaseTM, (Novozymes A/S) , MaxataseTM, MaxacalTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (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.
  • 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,
  • Preferred commercially available lipase enzymes include LipolaseTM and Lipolase UltraTM, LipexTM (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.
  • 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
  • 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 NOVOZYMTM 51032 (available from Novozymes A/S, Denmark) .
  • phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32.
  • 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.
  • phospholipases Ai and A 2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid
  • lysophospholipase or phospholipase B
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (Ai or A 2 ), phospholipase B activity, phospholipase C activity or phospholipase D activity.
  • phospholipase A used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase Ai and/or Phospholipase A 2 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.
  • 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.
  • animal origin such as, e.g., mammalian
  • pancreas e.g., bovine or porcine pancreas
  • snake venom or bee venom e.g., from snake venom or bee venom.
  • 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. subtiliss
  • 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;
  • 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,
  • 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.
  • the phospholipase is one described in WO 04/111216, especially the variants listed in the table in Example 1.
  • 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.
  • the phospholipase is a phospholipase Ai (EC. 3.1.1.32) . In another preferred embodiment of the invention the phospholipase is a phospholipase A 2 (EC .3.1.1.4. ) .
  • Examples of commercial phospholipases include LECITASETM and LECITASETM ULTRA, YIELSMAX, or LIPOPAN F (available from Novozymes A/S, Denmark) .
  • Suitable amylases 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.
  • amylases examples are the variants described in WO 94/02597, WO 94/18314, WO 96/23873, WO 97/43424, WO
  • amylases are DuramylTM, TermamylTM, Termamyl UltraTM, NatalaseTM, StainzymeTM, FungamylTM and BANTM (Novozymes A/S) , RapidaseTM and PurastarTM (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
  • 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.
  • cellulases include CelluzymeTM, CarezymeTM, EndolaseTM, RenozymeTM (Novozymes A/S) , ClazinaseTM and Puradax HATM (Genencor International Inc.), and KAC- 500 (B)TM (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 GuardzymeTM and NovozymTM 51004 (Novozymes A/S) .
  • pectate lyases examples 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.
  • the pectate lyase comprises the amino acid sequence of a pectate lyase disclosed in Heffron et al . , (1995) MoI. Plant-Microbe Interact.
  • 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) .
  • 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) .
  • alkaline pectate lyases examples include BIOPREPTM and SCOURZYMETM L from Novozymes A/S, Denmark .
  • mannanases examples include mannanases of bacterial and fungal origin.
  • 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.
  • 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.
  • mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp . , and Humicola insolens disclosed in WO 99/64619.
  • Bacillus sp . mannanases concerned in the Examples in WO 99/64619 which document is hereby incorporated by reference.
  • mannanases examples include MannawayTM 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.
  • 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
  • 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.
  • 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.
  • 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 ⁇ dye-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.
  • 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.
  • Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine and derivatives thereof.
  • 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.
  • 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 are also preferred.
  • 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.
  • PVP polyvinylpyrrolidone polymers
  • PVP polyvinylpyrrolidone polymers
  • TM Sokalan
  • 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.
  • PEG polyethylene glycol
  • 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.
  • 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.
  • 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.
  • PVNO polyvinylpyrridine N-oxide
  • PVP polyvinyl pyrrolidone
  • PVVI polyvinyl imidazole
  • 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.
  • 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.
  • 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.
  • VLD 00 multistains were washed together with 2kg cotton/ polycotton ballast in a Miele washing machine, under European conditions at 40 0 C 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 24GTT were placed in the proximity of the stain.
  • the final concentration of each enzyme was lOmg/ 1 of liquor.
  • Colour remission of the swatches was measured at
  • Figure 1 shows a device according to the invention
  • a spherical agitation device 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.
  • the device is a solid device.
  • 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.

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  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Textile Engineering (AREA)
  • Detergent Compositions (AREA)
EP08774457A 2007-08-03 2008-06-27 Enzymabgabevorrichtung Withdrawn EP2171027A1 (de)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP08774457A EP2171027A1 (de) 2007-08-03 2008-06-27 Enzymabgabevorrichtung

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
EP07113812 2007-08-03
EP08774457A EP2171027A1 (de) 2007-08-03 2008-06-27 Enzymabgabevorrichtung
PCT/EP2008/058295 WO2009019076A1 (en) 2007-08-03 2008-06-27 Enzyme delivery device

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EP2171027A1 true EP2171027A1 (de) 2010-04-07

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EP3088504B1 (de) 2015-04-29 2021-07-21 The Procter & Gamble Company Verfahren zur behandlung eines stoffes

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FR2627199B1 (fr) * 1988-02-11 1990-08-03 Procter & Gamble Dispositif pour le lavage du linge en machine
FR2641551B2 (fr) * 1988-05-18 1991-11-22 Procter & Gamble Procede et dispositif pour le lavage du linge en machine avec un produit particulaire
EP0641881A1 (de) * 1993-08-10 1995-03-08 The Procter & Gamble Company Ausgabevorrichtung
AU2002223020B2 (en) * 2000-11-27 2006-07-06 Novozymes A/S Automated mechanical stress assay for screening cleaning ingredients
WO2004074419A2 (en) * 2003-02-18 2004-09-02 Novozymes A/S Detergent compositions
US20050059567A1 (en) * 2003-09-11 2005-03-17 The Procter & Gamble Company Methods of formulating enzyme cocktails, enzyme cocktails for the removal of egg-based and grass-based stains and/or soils, compositions and products comprising same

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