CN104884598A

CN104884598A - Enzyme treatment composition

Info

Publication number: CN104884598A
Application number: CN201380067446.XA
Authority: CN
Inventors: R·A·冈加比森
Original assignee: Unilever NV
Current assignee: Unilever IP Holdings BV
Priority date: 2012-12-20
Filing date: 2013-12-13
Publication date: 2015-09-02
Anticipated expiration: 2033-12-13
Also published as: WO2014095618A1; EP2935550A1; BR112015013243A2; CN104884598B

Abstract

An enzymatic treatment composition comprising the combination of: - (iii) one or more enzymes; and - (iv) one or more arginine compounds.

Description

Enzyme-treated composition

Technical field

The present invention relates to the enzyme process decontamination of spot in fabric.Particularly but not exclusively, the pre-treatment that the present invention relates to by directly using or stain stains on fabrics carrys out the fabric decontaminating composition of decontamination.

Background technology

Enzyme is used in detergent formulation to help clean and decontamination.

In many weathers and in developing country, laundry is carried out at low or ambient temperatures.These temperature are challenges to the clothing decontamination product depending on enzyme, and enzyme works best between 50-70 degree.With regard to modern laundry machine, decontamination depends on to a great extent and is heated on envrionment temperature by water in washing machine, and this accounts for the significant proportion of the relevant greenhouse gases footprint of laundry---and for environment reason, these footprints need to reduce.

Summary of the invention

The object of the invention is to improve the low temperature/room temperature enzyme process decontamination of staining stains on fabrics.

In first, the invention provides a kind of fabric decontaminating composition, described composition comprises the combination of following component:

(i) one or more enzymes; With

(ii) one or more arginine compounds.

Preferably, described spot comprises biological substance, is preferably deposited in the protein-based and/or starchy material on fabric.

Preferably, described composition is environment activity.

Preferably, described composition comprises one or more tensio-active agents.

In second, the invention provides a kind of from staining the method that fabric substrate removes spot, described method comprises the step of the compositions-treated spot by the present invention first aspect.

Preferably, described method is carried out in envrionment conditions.

Preferably, the method for second aspect comprise add or with not adding water to the step of staining the direct applying said compositions of fabric.The step of applying said compositions can from the pre-step (as pre-treatment) that can be further (" mainly ") washing procedure subsequently as main washed journey or its.So further, washing step subsequently mainly comprises any washing process in any hand washing process or fabric washing machine.

Correspondingly, in the 3rd, the invention provides a kind of fabric decontaminating treatment unit, described device comprises the storage storage vault of composition of the present invention first aspect and the process component for basad direct applying said compositions, described in use the method preferably adopting second aspect.

In yet another aspect, the invention provides the purposes of arginine compounds in the enzyme process of textile stains removes.

Embodiment

Use the present invention, the enzyme process of the spot that arginine compounds reinforced fabric exists removes and effective at a lower temperature.Wash area prevailing in envrionment temperature, this provides the clothing (that is, fabric) of the improvement of staining fabric to clean.Scourability under the lesser temps improved can contribute to suppressing the employing of hot wash in these countries, and along with the raising of the standard of living and more people can afford washing machine, hot wash is in rising trend.To the invention provides in envrionment temperature cleaning process the protein of (using cold washing liquid) and/or starch-based stains and/or spot enzyme process performance and without the need to the temperature sensitivity of careful consideration enzyme in storage process.Therefore enzyme can more freely be selected based on other consideration.

Arginine compounds removing spot at environmental protect temperature and therefore can significantly reduce the energy cost of washing each time.

As used herein, term " substrate " comprises fabric, clothes etc.

As used herein, term " arginine compounds " is intended to comprise any suitable arginine compounds, comprises stereoisomerism and racemic form, derivative and is substituted derivative, their salt and their any mixture.

Preferably, arginine compounds with in the scope of 0.01mg/ml to 10mg/ml, in the scope of more preferably 0.01-0.32mg/ml, more preferably the concentration of 0.08-0.16mg/ml be present in any washings.

Preferably, arginine compounds is present in any composition of the present invention with the concentration in the scope of the every agent of 40mg to 5000mg, the preferably every agent of 320mg to 4000mg.Described composition can single dose form or provide with multiple doses, free-flowing form (powder, liquid, gel, paste etc.), uses measuring apparatus to measure by human consumer.Described dosage can in the scope of 10ml to 100ml.

For for local stain treatment/pretreated pretreatment unit, the concentration in composition can be washed in formula higher than main higher and every agent concentration, therefore can in the scope of the every agent of 300-5000mg, the preferably every agent of 500mg to 2000mg.Pretreatment unit dosage level can change in 0.1-10ml.

Term " environment activity " be intended to refer to lower than 25 degrees Celsius and preferably 22 or lower, more preferably 15 degrees centigrade or lower but height overall in 1 degree Celsius and " activity " refer to realize in decontamination effective.

As used herein, in the context of enzyme process fabric treatment composition, term " process " preferably refers to clean, more preferably refers to decontamination.

Preferably, " decontamination " with alleviate unit (Remission unit) or alleviate index (Remission index) measure.When exist be equal to or greater than 2 alleviate units, more preferably greater than or equal the alleviation of 5 units time, preferably illustrate " decontamination ".This represents effective decontamination of (human eye) visual effects.

As used herein, term " enzyme " comprises enzyme variant (such as being produced by recombinant technology).The example of this type of enzyme variant is at such as EP 251, have open in 446 (Genencor), WO 91/00345 (NovoNordisk), EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV).

Unless otherwise noted, otherwise all percentage ratios mentioned herein all by weight, calculates relative to total composition.Abbreviation " wt% " is interpreted as account for total composition % by weight.

Preferably, described pretreatment compositions is environment activity.Correspondingly, the temperature of the washings step of water washing process therefore in washing process (but not comprising drying) always lower than 40 DEG C, preferably lower than 30 DEG C, more preferably less than 25 DEG C, more preferably less than 22 DEG C, also more preferably 15 DEG C or lower.Cold washing liquid is encouraged to be that environment and economy is favourable.

Correspondingly, described enzymatic treatment composition preferably together with specification sheets packaging use described compositions-treated substrate with such as method as herein described at low temperatures, described low temperature preferably lower than 40 DEG C, more preferably less than 30 DEG C, even more preferably less than 25 DEG C, preferably at 22 DEG C or lower, most preferably at 15 DEG C.

For wherein needing enzyme process cleaning spot in the envrionment temperature cleaning process (that is, environment for use temperature washes liquid) but wherein composition is inevitably stored in the particular condition under comparatively high temps, the present invention is especially favourable.Effective at low temperatures addicted to cold enzyme, but because it is flexible to the temperature sensitive raised.Addicted to temperature (with thermophilic) enzyme stablize at elevated temperatures, but under low temperature washing conditions degradation.The invention provides and use the low temperature enzyme process addicted to the substrate of warm enzyme to clean.

Correspondingly, described enzyme system preferably comprises addicted to temperature or Zimadzhunt L 340 system.Described enzyme system can even for do not comprise addicted to cold enzyme addicted to temperature and/or Zimadzhunt L 340 system.

Enzyme can from animal, plant, bacterial origin (being derived from bacterium) or fungic origin (being derived from fungi), but preferably from the enzyme of bacterial origin.Comprise chemically modified or protein engineering mutant.The gene of this fermentoid of encoding can transfer to preferred Expression product host from a host, and the latter can or can not be identical with initial host.

One or more enzymes described preferably comprise proteolytic enzyme.

Preferred proteolytic enzyme is serine protease or metalloprotease, preferred alkaline microbial protease or trypsin like proteases.

Commercially available proteolytic enzyme comprises Alcalase ^tM, Savinase ^tM, Primase ^tM, Duralase ^tM, Dyrazym ^tM, Esperase ^tM, Everlase ^tM, Polarzyme ^tMand Kannase ^tM(Novozymes A/S), Maxatase ^tM, Maxacal ^tM, Maxapem ^tM, Properase ^tM, Purafect ^tM, Purafect OxP ^tM, FN2 ^tMand FN3 ^tM(Genencor InternationalInc.).

When proteolytic enzyme, arginine compounds is underivatized arginine and/or homoarginine, more preferably underivatized arginine.

One or more enzymes described preferably comprise amylase.

Suitable amylase (α and/or β) comprises those of bacterium or fungic origin.Comprise chemically modified or protein engineering mutant.Amylase comprises and such as derives from genus bacillus as GB1,296, the α-amylase of Bacillus strain disclosed in the special bacterial strain of the Bacillus licheniformis described in more detail in 839 or WO95/026397 or WO 00/060060.

Commercially available amylase has Duramyl ^tM, Termamyl ^tM, Termamyl Ultra ^tM, Natalase ^tM, Stainzyme ^tM, Fungamyl ^tMand BAN ^tM(Novozymes A/S), Rapidase ^tMand Purastar ^tM(from Genencor International Inc.).Commercially available amylase comprises Stainzyme ^tM(Novozymes).

One or more enzymes described can comprise proteolytic enzyme in combination with amylase and described arginine compounds is underivatized arginine.

Described enzyme preferably exists with 0.001-5 % by weight, more preferably 0.01-3%.

Described composition preferably also comprises other enzyme.

Described composition preferably comprises lipase; Preferred lipase comprises so-called " the first washing " lipase, it comprises the polypeptide that aminoacid sequence and the wild type lipase being derived from Humicola lanuginosa (Humicolalanuginosa) strain DSM 4109 have at least 90% sequence iden, and compared with described wild type lipase, it is included in electric neutrality in the 15A of E1 or Q249 or electronegative amino acid by the amino acid whose replacement of positively charged; And can also comprise:

(I) in the peptide addition of C-end;

(II) in the peptide addition of N-end;

(III) limit below:

I. in the position E210 of described wild type lipase, electronegative amino acid is comprised;

Ii. in the region corresponding to the position 90-101 of described wild type lipase, electronegative amino acid is comprised; With

Iii. the position corresponding to the N94 of described wild type lipase comprises electric neutrality or electronegative amino acid; And/or

Iv. in the region corresponding to the position 90-101 of described wild type lipase, there is negative charge or neutral charge; With

V. their mixture.

These lipase can Lipex ^tMtrade mark derives from Novozymes.Novozymes is with title Lipoclean ^tMdisclose from Novozymes but it is believed that the similar enzyme outside superincumbent definition, and this enzyme is also preferred.

Other possible lipase comprises from Humicola (Humicola, synonym Thermomyces) lipase, such as, from other Humicola lanuginosa (H.lanuginosa or T.lanuginosus) bacterial strain or from Humicola insolens (H.insolens); Pseudomonas Lipases, such as, belong to bacterial strain SD 705 (WO 95/06270 and WO 96/27002), winconsin pseudomonas (P.wisconsinensis) from Pseudomonas alcaligenes (P.alcaligenes) or pseudomonas pseudoalcaligenes (P.pseudoalcaligenes), pseudomonas cepacia (P.cepacia), Pseudomonas stutzeri (P.stutzeri), Pseudomonas fluorescens (P.fluorescens), pseudomonas (Pseudomonas); Genus bacillus lipase, such as from subtilis (the B.subtilis) (people (1993) such as Dartois, Biochemica etBiophysica Acta, 1131,253-360), bacstearothermophilus (B.stearothermophilus) (JP 64/744992) or bacillus pumilus (B.pumilus) (WO 91/16422).

Commercially available lipase comprises Lipolase ^tMwith Lipolase Ultra ^tMand bacterial enzyme (from Genecor).This is the bacterial origin lipase of the mutation M21L of the lipase of Pseudomonas alcaligenes, as authorized Gist-Brocades (M.M.M.J.Cox, H.B.M.Lenting, L.J.S.M.Mulleners and J.M.van der Laan) WO 94/25578 described in.

Described composition preferably comprises the Phospholipid hydrolase classifying as EC 3.1.1.4 and/or EC 3.1.1.32.As used herein, term Phospholipid hydrolase is to the activated enzyme of phosphatide tool.Phosphatide, as Yelkin TTS or Phosphatidycholine, is formed by the glycerine of Phosphation in the 3rd position by two fatty acid esterifications by outside (sn-1) and middle (sn-2) position; Described phosphoric acid then can esterified one-tenth amino alcohol.Phospholipid hydrolase is the enzyme of the hydrolysis participating in phosphatide.Can distinguish the phospholipase activity of some types, comprise: phospholipase A1 and A2, an aliphatic acyl groups (respectively in sn-1 and sn-2 position) hydrolysis is formed lysophospholipid by it; With lysophospholipase (or phospholipase B), the residue aliphatic acyl groups in its hydrolyzable lysophospholipid.Phospholipase C and Phospholipase D (phosphodiesterase) will discharge DG or phosphatidic acid respectively.

Described composition preferably comprises the at ranged in EC 3.1.1.74.At used according to the invention can be any source.Preferably, at is microbe-derived, particularly bacterium, fungi or yeast sources.

Described composition preferably comprises cellulase, and described cellulase comprises those of bacterium or originated from fungus.Comprise chemically modified or protein engineering mutant.Suitable cellulase comprises from bacillus, Rhodopseudomonas, Humicola, fusarium, Thielavia, the cellulase of Acremonium, such as US 4, 435, 307, US 5, 648, 263, US 5, 691, 178, US 5, 776, 757, WO 89/09259, Humicola insolens (Humicola insolens) is originated from disclosed in WO 96/029397 and WO 98/012307, autochthonal shuttle spore mould (Thielaviaterrestris), the fungal cellulase of thermophilic fungus destroyed wire (Myceliophthora thermophila) and Fusarium oxysporum (Fusarium oxysporum).Commercially available cellulase comprises Celluzyme ^tM, Carezyme ^tM, Endolase ^tM, Renozyme ^tM(Novozymes A/S), Clazinase ^tMwith Puradax HA ^tM(Genencor International Inc.) and KAC-500 (B) ^tM(Kao Corporation).

Described composition preferably comprises the peroxidase/oxydase of especially bacterial origin.Comprise chemically modified or protein engineering mutant.The example of oxidizing bacteria has but is not limited to the Aeromonas (Aeromonas sp) that oxydase can stem from.

Described composition preferably comprises pectate lyase (also claim Polygalacturonate lyase), and pectate lyase comprises and belonging to as erwinia, Rhodopseudomonas, Klebsiella and xanthomonas and the pectate lyase of cloning from subtilis people (1993) FEBS Letts.335:319-326 such as () Nasser and bacillus YA-14 people (1994) Biosci.Biotech.Biochem.58:947-949 such as () Kim from different bacterium.By bacillus pumilus (Bacillus pumilus) (Dave and Vaughn (1971) J.Bacteriol.108:166-174), poly-viscosity bacillus (B.polymyxa) (Nagel and Vaughn (1961) Arch.Biochem.Biophys.93:344-352), bacstearothermophilus (B.stearothermophilus) (Karbassi and Vaughn (1980) Can.J.Microbiol.26:377-384), the purifying within the scope of the pH of 8-10 with the pectate lyase of maximum activity that bacillus (Bacillus sp.) (Hasegawa and Nagel (1966) J.Food Sci.31:838-845) and bacillus RK9 (Bacillus sp.RK9) (Kelly and Fogarty (1978) Can.J.Microbiol.24:1164-1172) produce also is shown in description.When implementing of the present invention, any above-mentioned pectate lyase and divalent cation dependent/non-dependent and/or thermostability pectate lyase can be used.In preferred embodiments, pectate lyase comprises the people such as Heffron, (1995) people such as Mol.Plant-Microbe Interact.8:331-334 and Henrissat, pectate lyase disclosed in (1995) Plant Physiol.107:963-976.The pectate lyase clearly contained has open in WO 99/27083 and WO99/27084.Other pectate lyase clearly contained (being derived from Bacillus licheniformis), at United States Patent (USP) the 6th, has open in 284, No. 524 (this file is incorporated herein by reference).The pectate lyase mutation clearly contained has open in WO 02/006442, mutation disclosed in the embodiment especially in WO 02/006442 (this file is incorporated herein by reference).The example of commercially available alkaline pectin hydrochlorate lyase comprises the BIOPREP from Denmark Novozymes A/S ^tMand SCOURZYME ^tMl.

Described composition preferably comprises mannase: the example of mannase (EC 3.2.1.78) comprises the mannase of bacterium and originated from fungus.In a specific embodiment, mannase is derived from the bacterial strain (WO 94/25576) that filamentous fungus belongs to aspergillus tubigensis, preferably aspergillus niger or microorganism Aspergillus aculeatus.WO 93/24622 discloses a kind of mannase be separated from Trichodermareesei.Mannase also from some bacteria distribution, comprises genus bacillus organism.Such as, the people such as Talbot, Appl.Environ.Microbiol., Vol.56, No.11, pp.3505-3510 (1990) describe a kind of 'beta '-mannase being derived from bacstearothermophilus.The people such as Mendoza, World J.Microbiol.Biotech., Vol.10, No.5, pp.551-555 (1994) describe a kind of 'beta '-mannase being derived from subtilis.JP-A-03047076 discloses a kind of 'beta '-mannase being derived from bacillus.JP-A-63056289 describes the production of a kind of alkalescence, thermally-stabilised 'beta '-mannase.JP-A-63036775 relates to micro-organisms bacillus FERM P-8856, and it produces 'beta '-mannase and beta-Mannosidase.JP-A-08051975 discloses the alkaline ' beta '-mannase belonging to AM-001 from Alkaliphilic bacillus.A kind of purified mannanase from bacillus amyloliquefaciens has open in WO 97/11164.WO 91/18974 describes a kind of hemicellulase as dextranase, zytase or Mannanase Activity thing.Contain alkaline family 5 and 26 mannase being derived from glutinous agar genus bacillus (Bacillus agaradhaerens), Bacillus licheniformis (Bacillus licheniformis), salt tolerant Alkaliphilic bacillus (Bacillus halodurans), Bacillus clausii (Bacillusclausii), bacillus (Bacillus sp.) and Humicola insolens (Humicola insolens) disclosed in WO 99/64619.What especially contain is the bacillus mannase related in the embodiment of WO 99/64619.

The example of commercially available mannase comprises the Mannaway that can derive from Denmark Novozymes A/S ^tM.

The enzyme existed and any spices/fragrant substance or front perfume (or spice) may demonstrate certain interaction, therefore should be chosen as and make this interaction not be negative.Some negative interactions are by encapsulating one in product or other enzyme and front perfume (or spice) and/or avoid with other isolation method.

tensio-active agent

Described composition preferably comprises tensio-active agent.

Described tensio-active agent can be synthetic surfactant or with biological mode such as from the bio-surfactant of bacterium, fungi or other Microbe synthesis.Bio-surfactant preferably comprises the bio-surfactant being derived from microorganism.Preferably, it comprises Glycolipids Biosurfactants via, and described Glycolipids Biosurfactants via can be rhamnolipid or sophorolipid or marine alga glycolipid or mannosylerythritol lipid (MEL).Or, bio-surfactant advantageously can comprise cellobiose, bio-surfactant, lipoprotein and lipopeptid based on peptide (such as, Surfactin), lipid acid (such as, corynomucolic acid) (preferably there is hydrocarbon chain C12-C14), phosphatide (such as, by the phosphatidylethanolamine that the Rhodococcus of growth on normal paraffin produces, it causes interfacial tension lowering between water and n-Hexadecane to the CMC lower than 1mN m-1 and 30mgL-1) people such as (, 1982) Kretschner and spiculisporic acid; Polymer-type bio-surfactant, comprises Tego Care PS (emulsan), Thioctic Acid (liposan), Mannoproteins and polysaccharide-protein mixture.Preferably, bio-surfactant comprises rhamnolipid.

Composition according to the present invention comprises tensio-active agent, preferred stain release tensio-active agent.Detersive surfactant refers to that in this tensio-active agent or any surfactant mixture, the textile fabric of at least one tensio-active agent to the part process as laundry processes provides decontamination and cleaning effect.The part of other tensio-active agent as described composition that can be or can not be detersive surfactant can be used.

Detersive surfactant is present in laundry detergent composition with the weight level of 3 to 85 % by weight, preferably 3 to 60 % by weight, more preferably 3 to 40 % by weight, most preferably 3 to 35 % by weight.Also can introduce other tensio-active agent in laundry composition of the present invention; These tensio-active agents can be decontamination or non-detersive surfactant.

Preferably, detersive surfactant comprises aniorfic surfactant, nonionic surface active agent or the mixture of the two.More preferably, detersive surfactant mixture comprises anionic and nonionic surface active agent.Cationic surfactant optionally exists as a part for detersive surfactant.

If existed, based on the total weight of the tensio-active agent existed, aniorfic surfactant exists with the level of 0.1 to 95 % by weight, preferably 1 to 50 % by weight, more preferably 1.5 to 25 % by weight.Based on the total weight of the tensio-active agent existed, if existed, nonionic surface active agent is introduced with the level of 0.1 to 95 % by weight, preferably 1 to 50 % by weight, more preferably 1.5 to 25 % by weight.Introduce anionic and the detersive surfactant mixture both nonionic surface active agent if used, then the ratio of preferred anionic type tensio-active agent to nonionic surface active agent is 10:1 to 1:10.

Nonionic surface active agent

For purposes of the present invention, unless otherwise noted, otherwise " nonionic surface active agent " should be defined as molecular weight is less than about 10, the amphiphile, amphiphilic molecule of 000, and it is substantially free of any functional group under the Normal Wash pH of 6-11 with net charge.

The nonionic surface active agent of any type can be used.It is highly preferred that there is C ₈-C ₃₅, preferred C ₈-C ₃₀, more preferably C ₁₀-C ₂₄, especially C ₁₀-C ₁₈the alkyl chain of carbon atom and have preferably 3 to 25, the fatty acid alkoxylates of more preferably 5 to 15 ethylene oxide groups, especially ethoxylate, such as, from the Neodols of Shell (Hague, Detch); Can have 1,000 to 30, the ethylene oxide/propylene oxide segmented copolymer of the molecular weight of 000, such as, from the Pluronic (trade mark) of BASF (Ludwigshafen, Germany); And alkylphenol ethoxylate, such as can derive from the Triton X-100 of Dow Chemical (Michigan, USA Midland).

Other nonionic surface active agent considered within the scope of the invention comprises: the condenses of alkanolamine and lipid acid, as coconut oleoyl amine DEA; Polyvalent alcohol-fatty acid ester, as derived from the Span series of Uniqema (Dutch person of outstanding talent reaches); Ethoxylated polyalchohols-fatty acid ester, as derived from the Tween series of Uniqema (Dutch person of outstanding talent reaches); APG, as derived from the APG series of Cognis (Dusseldorf ,Germany); With n-alkyl pyrrolidone, as the Surfadone series product sold by ISP (New Jersey Wei grace).

Aniorfic surfactant

" aniorfic surfactant " is defined as the amphiphile, amphiphilic molecule comprising one or more functional group in this article, and when when being in the aqueous solution under the Normal Wash pH between 6 and 11, it has clean anionic charge.

Preferred aniorfic surfactant is an alkali metal salt of the organosulfur reaction product in its molecular structure with the alkyl radicals containing about 6 to 24 carbon atoms and the atomic group being selected from sulphonate atomic group and sulfuric ester atomic group.

Although any aniorfic surfactant hereinafter described such as sulfated alkyl ether, soap, fatty sulfonate, alkylbenzene sulfonate, sulfosuccinic ester, primary alkyl sulphates, alkene sulfonate, paraffin sulfonate and organophosphate all can use, but preferred aniorfic surfactant is alkali and alkaline earth metal ions salt, the aliphatic alcohol sulfate of fatty acid carboxylate ester, preferred primary alkyl sulphates, more preferably they are ethoxylations, such as sulfated alkyl ether; With alkylbenzene sulfonate or their mixture.

Cationic, amphoterics and/or zwitterionics

In addition, according to there is cationic, amphoterics and/or zwitterionics in composition of the present invention.

Preferred cationic surfactant is for having general formula R ₁r ₂r ₃r ₄n ⁺x ^-quaternary ammonium salt, such as wherein R ₁for C ₁₂-C ₁₄alkyl group, R ₂and R ₃for methyl group, R ₄for 2-hydroxyethyl groups, X ^-for chlorion.This material can Praepagen (trade mark) HY commercially available with the form of 40 % by weight aqueous solution from ClariantGmbH.

In a preferred embodiment, composition according to the present invention comprises both sexes or zwitterionics.Amphoterics be not only containing acidic-group but also containing basic group and by under the Normal Wash pH between 6 and 11 with the molecule that zwitter-ion exists.Preferably, both sexes or zwitterionics with 0.1 to 20 % by weight, more preferably 0.25 to 15 % by weight, even more preferably 0.5 to 10 % by weight level exist.

The example of suitable zwitterionics be can broadly be described as having have a long chain alkyl group of about 8 to about 18 carbon atoms and at least one be selected from those of the derivative of the aliphatic quaternary ammonium of the water solubilising atomic group of sulfate radical, sulfonate radical, carboxylate radical, phosphate radical or phosphonate radical, sulfonium and phosphonium compounds.The general formula of these compounds is:

R ₁(R ₂) _xY ⁺R ₃Z ^-

Wherein R ₁containing having the alkyl of 8 to 18 carbon atoms, thiazolinyl or hydroxyalkyl group, 0 to 10 ethyleneoxy group group or 0 to 2 glycerol unit; Y is nitrogen, sulphur or phosphorus atom; R ₂for having alkyl or the hydroxyalkyl group of 1 to 3 carbon atom; When Y is sulphur atom, x is 1, when Y be nitrogen or phosphorus atom time, x is 2; R ₃for there is the alkyl of 1 to 5 carbon atom or hydroxyalkyl group and Z is the atomic group being selected from sulfate radical, sulfonate radical, carboxylate radical, phosphate radical or phosphonate radical.

Preferred amphoterics is amine oxide, such as coco dimethyl amine oxide.Preferred zwitterionics is trimethyl-glycine, especially amido betaines.Preferred trimethyl-glycine is C ₈to C ₁₈alkyl amido alkyl betaine, such as cocoamido trimethyl-glycine.These can be used as cosurfactant and introduce, and based on the weighing scale of total composition, preferably exist with the amount of 0 to 10 % by weight, more preferably 1 to 5 % by weight.

Be beet alkali surface activator for introduction into the preferred both sexes in composition according to the present invention or zwitterionics.The example of these tensio-active agents is mentioned in enumerating below.

Sulfatobetaine, as 3-(dodecyl dimethyl ammonium)-1-propane vitriol; With 2-(coco dimethyl ammonium)-1-ethanesulfonate.

Sultaine, as: 3-(dodecyl dimethyl ammonium)-2-hydroxyl-1-propane sulfonate; 3-(dodecyldimethylamine base ammonium)-1-propane sulfonate; 3-(C ₁₂-C ₁₄alkylamidopropyl group Dimethyl Ammonium)-2-hydroxyl-1-propane sulfonate; With 3-(coco dimethyl ammonium)-1-propane sulfonate.

Carboxybetaine, as (dodecyl dimethyl ammonium) acetate (also claiming lauryl betaine); (dodecyldimethylamine base ammonium) acetate (also claiming myristyl betaine); (coco dimethyl ammonium) acetate (also claiming coconut trimethyl-glycine); (oleyl dimethyl ammonium) acetate (also claiming oil-based betaine); (dodecyloxy methyl dimethoxy base ammonium) acetate; (cocoamidopropyl dimethyl ammonium) acetate (also claiming cocoamido-propyl trimethyl-glycine or CAPB).

Sulfonium trimethyl-glycine, as: (dodecyl dimethyl sulfonium) acetate; With 3-(coco dimethyl-sulfonium)-1-propane sulfonate.

Phosphonium trimethyl-glycine, as: 4-(San Jia Ji Phosphonium)-1-n-Hexadecane sulfonate; 3-(Shi bis-Wan base Er Jia Ji Phosphonium)-1-propane sulfonate; With 2-(Shi bis-Wan base Er Jia Ji Phosphonium)-1-ethanesulfonate.

Preferably comprise carboxybetaine or sultaine as both sexes or zwitterionics according to composition of the present invention, or comprise their mixture.Especially preferred is lauryl betaine.

Described treatment compositions can comprise other composition common in detergent liquid.Especially polyester affinity (substantive) soil release polymer, hydrotrote, opalizer, tinting material, spices, other enzyme, other tensio-active agent, composition is as spices or the microcapsule of nursing additive, tenderizer, for the polymkeric substance of anti-redeposition of soil, SYNTHETIC OPTICAL WHITNER, bleach-activating agent and bleaching catalyst, antioxidant, pH control agent and buffer reagent, thickening material, for rheology modified, the external structure agent or do not have with embedding functional component wherein of visual cues and other composition well known by persons skilled in the art.

Present combination non-limiting example below further describes the present invention, wherein

Fig. 1 is bar graph, shows the change of average RFU reading with arginine concentrations of replicate(determination) 1-4 in the table 1 of embodiment 1.Error bar shows the standard deviation between four replicate(determination)s of each concentration;

Fig. 2 is bar graph, shows the change of average RFU reading with arginine concentrations of replicate(determination) 1-4 in the table 2 of embodiment 2.Error bar shows the standard deviation between four replicate(determination)s of each concentration.

embodiment

All values in whole part is % by weight of the total base composition A without enzyme, so as in each embodiment only enzyme be clearly be called those that add.

Detergent composition A

Wherein:

Neodol 25-7 (from Shell)=C ₁₂-C ₁₅alcohol 7-ethoxylate

LAS acid=C ₁₀-C ₁₄alkyl benzene sulphonate (ABS);

SLES=C12-C13 alcohol 3-polyethoxylate sulfates, Na salt :=sodium lauryl tri(oxyethyl) sulfate (there are average 3 ethylene oxide groups);

Embodiment 1: arginine is on the impact of Savinase (Sai Wei) activity

Embodiment 1 reagent:

-reaction buffer: 50mM Tris.HCl (TRIS hydrochloride, hydrochloride, from Sigma Aldrich) (pH 8.0)

-Savinase 16L (from Novozymes).

-preparation BODIPY TR-X dyestuff as described below is in conjunction with casein substrate solution: be thoroughly dissolved in the sodium bicarbonate buffer liquid (pH 8.5) of 200 μ l 0.1M by the casein substrate (Invitrogen, catalog number E6639) of 1mgBODIPY TR-X dye marker.Then this 200 μ l solution is added in 19.8ml 50mM Tris.HCl (pH 8.0) to prepare the working solution of 10 μ g/ml.Fresh substrate prepare soon before each test and store at room temperature dark place until needs.

-DL-arginine (number: 230-571-3) by Sigma catalog number 11020, EC

Embodiment 1 experimental program

Following reaction mixture is prepared in 300 hole, μ l hole/96 microtitre (micropore) plates:

Test mixture:

Savinase 16L(2.6μg/ml)： 100μl

Casein substrate (10 μ g/ml) the 80 μ l of BODIPY TR-X dye marker

DL-arginine (0.15 to 1M) 20 μ l

Control mixture (Arginine free):

Savinase 16L(2.6μg/ml)： 100μl

Casein substrate (10 μ g/ml) the 80 μ l of BODIPY TR-X dye marker

50mM Tris.HCl(pH 8.0) 20μl

In both cases, substrate all finally adds and reactant is descended cultivations 1 hour in 22 degree.The hydrolysis of proteases catalyze discharges high fluorescence BODIPY TR-X dye marker peptide.The adjoint increase of fluorescence is proportional with protease activity.Be set as exciting under 485nm and detecting under 530nm in the fluorescence microplate reader of transmitting measuring fluorescence intensity.

Embodiment 1 result

Table 1: the Relative fluorescence units (RFU) that the 1.3 μ g/ml Savinase and 4 μ g/mlBODIPY TR-X dye marker casein substrate with a series of arginine concentrations are recorded.Four replicate(determination)s are carried out abreast to each concentration.

DL-arginine (M)	Parallel 1	Parallel 2	Parallel 3	Parallel 4	Average RFU 1-4	Standard deviation
							0	2103.462	2189.599	2100.607	2095.228	2122.224	45.04620581
0.015	2693.568	2811.747	2828.436	2832.729	2791.62	65.99156151
							0.03	3023.701	3312.857	3350.904	3263.515	3237.74425	147.1118607
0.06	3456.281	3635.014	3661.681	3610.958	3590.9835	92.16030525
							0.12	3942.019	4046.703	3909.106	4000.389	3974.55425	61.141618
0.25	4144.113	4339.233	3943.937	4085.495	4128.1945	163.8746683
							0.5	3895.805	4176.904	3861.651	3970.51	3976.2175	141.3026302
1	3255.572	3485.625	3240.836	3506.565	3372.1495	143.5011783

Result is shown in Figure 1

Under 0.25M, arginine improves the maximum value of relative Savinase activity to 51.4%.

Embodiment 2: arginine is on the impact of Stainzyme (removing stain enzyme) activity

Embodiment 2 reagent:

-reaction buffer: 50mM MOPS (pH 6.9)

-Stainzyme 12L(Novozymes)。

-BODIPY FL dyestuff is in conjunction with DQ starch substrates solution: be thoroughly dissolved in the sodium-acetate buffer (pH 4.0) of 100 μ l 50mM in conjunction with DQ starch substrates (Invitrogen, catalog number E33651) by 1mg BODIPY FL dyestuff.Then this 100 μ l solution is added in 900 μ l 50mM MOPS (pH 6.9) to prepare the working solution of 10 μ g/ml.Fresh substrate prepare soon before each test and store at room temperature dark place until needs.

-arginine (number: 230-571-3) by Sigma catalog number 11020, EC

Embodiment 2 scheme:

Following reaction mixture is prepared in 300 μ l 96 orifice plates:

Test mixture:

Stainzyme 12L(0.34μg/ml)： 80μl

BODIPY FL dyestuff is in conjunction with DQ starch substrates (10 μ g/ml) 100 μ l

DL-arginine (0.15 to 1M) 20 μ l

Control mixture (Arginine free):

Stainzyme 12L(0.34μg/ml)： 80μl

50mM MOPS(pH 6.9) 20μl

In both contrast and test mixture, substrate all finally adds and cultivation 30 minutes under reacting on 22 degree.Substrate, by amylase degrades, discharges high fluorescence light segments.The adjoint increase of fluorescence is proportional with amylase activity.Be set as such as exciting under 485nm and detecting under 520nm in the fluorescence microplate reader of transmitting measuring fluorescence intensity.

Embodiment 2 result

Table 2: the Relative fluorescence units (RFU) that Stainzyme and the BODIPY FL dyestuff with a series of DL-arginine concentrations is recorded in conjunction with DQ starch substrates.Four replicate(determination)s are carried out abreast to each concentration.

The result of table 2 is shown in Figure 2.

Under 0.06M, arginine improves the maximum value of relative Stainzyme activity to 14.3%.Embodiment 3: end-point method detergency test

Embodiment 3 reagent:

-following dirty cloth sample is punching into and coils and transfer to 300 μ l 96 orifice plates:

Protease-sensitive spot: EMPA117: blood/milk/ink (Testfabrics Inc.)

Responsive spot: the CS27 of amylase: yam starch, coloured (Testfabrics Inc.)

-laundry enzyme (Novozymes):

(1)Savinase 16L

(2)Stainzyme 12L

-composition A

-DL-arginine (number: 230-571-3) by Sigma catalog number 11020, EC

Embodiment 3 scheme:

-pre-rinsing stains cloth to remove the free spot of any remnants:

-in each hole, add 200 μ l distilled water

-under 900rpm jolting plate 10 minutes

-remove washings

Reaction mixture:

Test mixture:

* in distilled water, the arginine of following mg/ml concentration is diluted to: 0.08,0.16,0.32,0.64,1.28,2.56 and 5.12.

Control mixture:

Enzyme (Stainzyme/Savinase) 5mg/L 20 μ l

Example composition A:5mg/L 100 μ l

Distilled water 80 μ l

-in both cases, enzyme all finally adds.Reaction is cultivated 1 hour while jolting under 900rpm under 22 degree.

-by adding 200 μ l distilled water in each hole, then under 900rpm, jolting carrys out rinsing cloth in 5 minutes.Then washings is removed.Repeat this program continuous four times.

-40 degree will be distributed under dry 3 hours

After-drying, digital scanning spot plate also measures its Δ E.This value is used to express cleaning effect and be defined as calico and the aberration stained between cloth after washing.Mathematically, Δ E is defined as:

ΔE＝[(ΔL) ²+(Δa) ²+(Δb) ²] ^1/2

Wherein Δ L is measuring through darkness difference between washing cloth and calico; Δ a and Δ b is respectively measuring of redness and yellowing difference between two cloth.From this formula clearly, the value of Δ E is lower, and cloth will be whiter.About this colour examining technology, with reference to Commission International deI'Eclairage (CIE); Recommendation on Uniform Colour Spaces, colourdifference equations, psychometric colour terms, supplement no.2to CIEPublication, no.15, Colormetry, Bureau Central de la CIE, Paris 1978.

Embodiment 3 result

Cleaning effect is have expressed with the form of decontamination index (SRI) in following table:

SRI＝100-ΔE

SRI is higher, then cloth is more clean, SRI=100 (white).

Table 3.1: use the EMPA117 through processing in composition A with Savinase and a series of arginine concentrations to stain the end-point method detergency test of cloth.Same 96 orifice plates carry out four replicate(determination)s abreast.Scanning board also calculates Δ E and SRI value.

The result of table 3.1 is shown in Fig. 3 .1.

Table 3.2: use the CS27 through processing in composition A with Stainzyme and a series of DL-arginine concentrations to stain the end-point method detergency test of cloth.Same 96 orifice plates carry out four replicate(determination)s abreast.Scanning board also calculates Δ E and SRI value.

The result of table 3.2 is shown in Fig. 3 .2.

These results illustrate, arginine compounds DL-arginine can dose dependent fashion to strengthen the decontamination of Savinase and Stainzyme active.

Claims

1. a fabric decontaminating composition, described fabric decontaminating composition comprises the combination of following component:

(i) one or more enzymes; With

(ii) one or more arginine compounds.

2. fabric decontaminating composition according to claim 1, is characterized in that it is environment activity.

3. fabric decontaminating composition according to claim 1, is characterized in that it comprises one or more tensio-active agents.

4. fabric decontaminating composition according to claim 1, is characterized in that one or more enzymes described comprise proteolytic enzyme.

5. fabric decontaminating composition according to claim 1, is characterized in that one or more enzymes described comprise amylase.

6., from staining the method that fabric removes spot, described method comprises the step by spot described in the compositions-treated according to any one of claim 1-5.

7. method according to claim 6, is characterized in that described method is carried out in envrionment conditions.

8. the method according to claim 7 or 8, is characterized in that described composition is applied directly to described spot, and described step is optionally pre-treatment step.

9. arginine compounds and one or more enzymes are in combination for from staining in fabric the purposes removing spot, and one or more enzymes described are preferably proteolytic enzyme and/or amylase.