CN103946359A - Detergent compositions comprising surfactant and enzyme - Google Patents

Detergent compositions comprising surfactant and enzyme Download PDF

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Publication number
CN103946359A
CN103946359A CN201280045017.8A CN201280045017A CN103946359A CN 103946359 A CN103946359 A CN 103946359A CN 201280045017 A CN201280045017 A CN 201280045017A CN 103946359 A CN103946359 A CN 103946359A
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China
Prior art keywords
enzyme
surfactant
detergent compositions
containing detergent
phospholipase
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CN201280045017.8A
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Chinese (zh)
Inventor
A·T·库克
N·J·帕里
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Unilever NV
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Unilever NV
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    • 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
    • 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
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/12—Sulfonic acids or sulfuric acid esters; Salts thereof
    • C11D1/30—Sulfonation products derived from lignin
    • 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
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3707—Polyethers, e.g. polyalkyleneoxides
    • 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
    • C11D3/382—Vegetable products, e.g. soya meal, wood flour, sawdust

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Organic Chemistry (AREA)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

The invention provides an enzymatic detergent composition comprising the combination of a surfactant system; one or more enzymes and one or more lignin compounds. The invention also provides a process for treating a substrate, comprising the steps of treating the substrate with an enzymatic detergent composition comprising the combination of a surfactant system; one or more enzymes and one or more lignin compounds.

Description

The detergent composition that comprises tensio-active agent and enzyme
The present invention relates to enzyme-containing detergent compositions.
Enzyme is used in detergent formulations to help clean and decontamination.
The object of the invention is to improve the performance of enzyme in detergent formulations.
In first aspect, the invention provides enzyme-containing detergent compositions, it comprises following combination:
(i) surfactant system;
(ii) one or more enzymes,
(iii) one or more lignin compounds.
In second aspect, the invention provides the method for clean matrix, it comprises the step of utilizing the enzyme-containing detergent compositions of first aspect present invention to process matrix.
By the present invention, clean-up performance is improved.
As used herein term " matrix " comprises fabric and clothes and laundry project.Therefore, preferably, described method is for laundering of textile fabrics, namely removes stain/soil from fabric.
Preferably, described cleaning method occurs in the washing container that contains washings, and described washings comprises water and enzyme-containing detergent compositions.Washings can be applied to matrix or matrix can be immersed in washings whole or in part.
Cleaning method alternatively comprises enzyme-containing detergent compositions (undissolved, not add water) is directly applied to the partly or entirely upper of fabric, thereby directly processes the one or more spots on fabric.Preferably pretreatment process of this method, thus can then utilize/in washings, process (for example,, as " master " washing method).Preferably, described master washes as described in a second aspect of the present invention.
Preferably, the time length of described method is less than 60 minutes, is more preferably less than 30 minutes.If it is pretreatment process, pre-treatment step is preferably less than 5 minutes, and is more preferably less than 2 minutes (but continuing during cleaning meeting by the enzyme so used at least a portion in any washing process subsequently).
Synergistic combination of the present invention is significantly improved the performance under low temperature---and under low temperature, the stain/soil of clean oil & fat is more a problem.
Preferably, the washings temperature of described method is less than 40 DEG C, and is preferably less than 30 DEG C, and is more preferably less than 25 DEG C.Cold washing liquid is that environment and economy is favourable.
Enzyme-containing detergent compositions, preferably low temperature formulations.Therefore, enzyme-containing detergent compositions is preferably packaging together with the specification sheets of subzero treatment, and described low temperature is preferably less than 40 DEG C, is more preferably less than 30 DEG C, is even more preferably less than 25 DEG C.
The invention provides oily soil and/or the spot enzymatic performance in Low-temperature cleaning method (utilizing cold washing liquid), and without the temperature sensitivity that thinks better of enzyme.Therefore, enzyme can more freely be selected on the basis of other Considerations.
The present invention on the one hand need to be in low temperature clean method (utilizing cold washing liquid) for the clean oily dirt of enzymatic and/or spot but the situation that wherein composition must be stored under comparatively high temps is especially favourable.Having a liking for cold enzyme (psychrophilic enzyme) is effectively at low temperature, but due to its handiness thereby to the temperature sensitive raising.Have a liking for temperature (mesophilic) (with thermophilic (thermophilic)) enzyme stable at elevated temperatures, but performance reduces.The invention provides with having a liking for warm enzyme to carry out enzymatic and clean matrix, and can bear without the design of requiring efforts rising temperature have a liking for cold enzyme.
Therefore, enzyme system preferably comprises and has a liking for temperature or Zimadzhunt L 340 system.Enzyme system can be even have a liking for temperature and/or with Zimadzhunt L 340 system, have a liking for cold enzyme and do not comprise.
Enzyme can be bacterial origin (deriving from bacterium) or originated from fungus (deriving from fungi), but, the enzyme in preferred bacterium source.
Composition preferably comprises 1 to 70wt% tensio-active agent, and most preferably 10 to 30wt%.
Preferably, tensio-active agent comprises at least bio-surfactant of 1wt% (based on cleaning compositions).
Preferably, bio-surfactant is bacterial origin.
Preferably, bio-surfactant and enzyme are bacterial origin.
Mutant chemically modified or protein engineering is also included within the present invention.
One or more enzymes can be used as system and provide.
Preferably, described one or more enzymes comprise lipase.Preferred lipase comprises from Humicola (Humicola) lipase of (also claiming thermophilic fungus to belong to (Thermomyces)), for example, from comb and parallel cotton fibers prior to spinning shape humicola lanuginosa (H.lanuginosa (T.lanuginosus)) or from Humicola insolens (H.insolens); Rhodopseudomonas (Pseudomonas) lipase, for example, from Pseudomonas alcaligenes (P.alcaligenes) or pseudomonas pseudoalcaligenes (P.pseudoalcaligenes), pseudomonas cepacia (P.cepacia), pseudomonas stanieri (P.stutzeri), Pseudomonas fluorescens (P.fluorescens), pseudomonas strain SD705 (WO95/06720 and WO96/27002), Wisconsin pseudomonas (P.wisconsinensis); Bacillus (Bacillus) lipase, for example, from subtilis (B.subtilis) (Dartois etc. (1993), Biochemica et Biophysica Acta, 1131,253-360), bacillus acidocldarius (B.stearothermophilus) (JP64/744992) or bacillus pumilus (B.pumilus) (WO91/16422).
Commercially available lipase comprises Lipolase tMwith Lipolase Mltra tM, Lipex tM(Novozymes A/S) and bacterial enzyme, (from Genecor).This is the lipase from bacterium, the variant M21L of the lipase of Pseudomonas alcaligenes, it is described in the WO94/25578 of Gist-Brocades (M.M.M.J.Cox, H.B.M.Lenting, L.J.S.M.M μ lleners and J.M.van der Laan).
Preferred Phospholipid hydrolase (EC3.1.1.4 and/or EC3.1.1.32) comprises the enzyme of hydrolytic phosphatide.They comprise that a fatty acyl group of hydrolysis (respectively in sn-1 and sn-2 position) is to form the phospholipase A of lysophospholipid 1and A 2; With the lysophospholipase (or phospholipase B) that can be hydrolyzed remaining fatty acyl group in lysophospholipid; But also comprising Phospholipase C and Phospholipase D (phosphodiesterase), it discharges respectively DG or phosphatidic acid.
The relevant term " phospholipase A " of enzyme used herein and of the present invention means to contain has phospholipase A 1and/or phospholipase A 2active enzyme.Phospholipase activity also can for example, provide by also having other active enzymes (having the lipase of phospholipase activity).
Phospholipid hydrolase can be any source, for example animal-origin (for example Mammals), and for example, for example, from pancreas (ox or pig pancreas), or snake venom or bee venom.Preferably, Phospholipid hydrolase can be microbe-derived, for example, be derived from filamentous fungus, yeast or bacterium, for example Aspergillus or kind, for example aspergillus niger (A.niger); Dictyostelium (Dictyostelium), for example dictyostelium discoideum (D.discoideum); Mucor (Mucor), for example mucor javanicus (M.javanicus), mucor mucedo (M.mucedo), thin spore Mucor (M.subtilissimus); Neurospora (Neurospora), for example Neuraspora crassa (N.crassa); Rhizomucor (Rhizomucor), for example Rhizomucor pusillus (R.pusillus); Rhizopus (Rhizopus), for example rhizopus arrhizus (R.arrhizus), routine Japanese head mold (R.japonicus), rhizopus stolonifer (R.stolonifer); Sclerotinia (Sclerotinia), for example soybean sclerotinite (S.libertiana); Hair moss Pseudomonas (Trichophyton), for example red hair moss bacterium (T.rubrum); Vickers Sclerotinia (Whetzelinia), for example W.sclerotiorum; Bacillus, for example bacillus megaterium, subtilis; Citrobacter (Citrobacter), for example citrobacter freundii (C.freundii); Enterobacter (Enterobacter), for example enteroaerogen (E.aerogenes) or enterobacter cloacae (E.cloacae); Edwardsiella (Edwardsiella), blunt tarda (E.tarda); Erwinia (Erwinia), for example raw Erwinia of grass (E.herbicola); Escherichia (Escherichia), for example intestinal bacteria; Klebsiella, for example Klebsiella pneumonia (K.pneumoniae); Proteus (Proteus), for example proteus vulgaris (P.vulgaris); Providencia (Providencia), for example providencia stuartii (P.stuartii); Salmonella, for example Salmonella typhimurium (S.typhimurium); Serratia (Serratia), for example liquefied Serratia (S.liquefasciens), serratia marcescens (s.marcescens); Shigella (Shigella), for example shigella flexneri (S.flexneri); Streptomyces, for example Streptomyces violaceoruber (S.violeceoruber); Or Yersinia, for example yersinia entero-colitica (Y.enterocolitica).Therefore Phospholipid hydrolase can come from for example Mycophyta, for example pyrenomycetes (Pyrenomycetes) class, as fusarium (genus Fusarium), the bacterial strain of for example machete sickle spore (F.c μ lmomm), different spore sickle spore (F.heterosporum), fusarium solanae (F.solani), or the bacterial strain of sharp sickle spore (F.oxysporum).Phospholipid hydrolase can also be from the filamentous fungal strains in Aspergillus, the bacterial strain of for example Aspergillus awamori (Aspergillus awamori), smelly aspergillus (Aspergillus foetidus), aspergillus japonicus (Aspergillus japonicus), aspergillus niger or aspergillus oryzae (Aspergillu oryzae).
Preferred Phospholipid hydrolase is the bacterial strain that is derived from Humicola, especially dredges cotton shape humicola lanuginosa bacterial strain or variant; And be the bacterial strain that is derived from sickle-like bacteria, the bacterial strain of especially sharp sickle spore.Phospholipid hydrolase can be derived from sharp sickle spore DSM2672.
Preferably, Phospholipid hydrolase comprises phospholipase A 1or phospholipase A (EC.3.1.1.32) 2(EC.3.1.1.4).
The example of commercially available Phospholipid hydrolase comprises LECITASE tMand LECITASE tMuLTRA, YIELSMAX or LIPOPAN F (can purchased from Novozymes A/S, Denmark).
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 International Inc.).
Other enzyme is optional from as follows: cellulase, esterase, peroxidase/oxydase, oxydo-reductase, polygalacturonase, lyase, mannase and composition thereof.
The bacterial enzyme using is in the present invention cellulase, esterase, peroxidase/oxydase, polygalacturonase, lyase, mannase or its mixture.The bacterial gene of coding this kind of enzyme can be transferred to the host of preferred generation expression body, and it is not limited to bacterium, and comprises for example other microorganism host.But term bacterial enzyme used herein comprises and derives from first bacterium the enzyme that is expressed.
Composition can comprise the at being sorted in EC3.1.1.74.The example of bacterium at is from Rhodopseudomonas, the at of the bacterial strain of particularly pseudomonas mendocina (Pseudomonas mendocina), or pseudomonas putida (Pseudomonas putida).
Enzyme can be the Phospholipid hydrolase that is classified as EC3.1.1.4 and/or EC3.1.1.32.As used herein, term Phospholipid hydrolase is to the activated enzyme of phosphatide tool.Phosphatide, as Yelkin TTS or phosphatidylcholine, it is by being formed by the glycerine of Phosphation by two fatty acid esterifications and in the 3rd position in the position of outside (SB-1) and middle (sn-2); Phosphoric acid and then can esterification become amino alcohol.Phospholipid hydrolase is the enzyme that participates in phosphatide hydrolysis.The phospholipase activity that can distinguish several types, comprises phospholipase A 1and A 2, its fatty acyl group of hydrolysis (respectively in sn-1 and sn-2 position) is to form lysophospholipid; And lysophospholipase (or phospholipase B), it can be hydrolyzed remaining fatty acyl group in lysophospholipid.Phospholipase C and Phospholipase D (phosphodiesterase) discharge respectively DG or phosphatidic acid.
Term Phospholipid hydrolase comprises the enzyme with phospholipase activity, described phospholipase activity for example, phospholipase A (A 1or A 2), phospholipase B activity, Phospholipase C activity or Phospholipase D activity.The relevant term " phospholipase A " of enzyme used herein and of the present invention means to contain has phospholipase A 1and/or phospholipase A 2active enzyme.Phospholipase activity also can for example, provide by also having other active enzymes (having the lipase of phospholipase activity).Phospholipase activity can be for example from having the secondary active lipase of Phospholipid hydrolase.In other embodiment of the present invention, Phospholipid hydrolase enzymic activity is not to be that secondary active enzyme provides by substantially only having phospholipase activity and wherein said phospholipase activity.
Preferably, Phospholipid hydrolase is bacterial origin: bacillus, for example, bacillus megaterium (B.megaterium), subtilis (B.subtilis); Citrobacter (Citrobacter), for example citrobacter freundii (C.freundii); Enterobacter (Enterobacter), for example enteroaerogen (E.aerogenes) or enterobacter cloacae (E.cloacae); Edwardsiella (Edwardsiella), blunt tarda (E.tarda); Erwinia (Erwinia), for example raw Erwinia of grass (E.herbicola); Escherichia (Escherichia), for example intestinal bacteria; Klebsiella, for example Klebsiella pneumonia (K.pneumoniae); Proteus (Proteus), for example proteus vulgaris (P.vulgaris); Providencia (Providencia), for example providencia stuartii (P.stuartii); Salmonella, for example Salmonella typhimurium (S.typhimurium); Serratia (Serratia), for example liquefied Serratia (S.liquefasciens), serratia marcescens (S.marcescens); Shigella (Shigella), for example shigella flexneri (S.flexneri);
Especially bacterial origin of suitable cellulase.Comprise the mutant of chemically modified or protein engineering.Applicable cellulase comprises the cellulase from bacillus, Rhodopseudomonas and genus clostridium.
Especially bacterial origin of applicable peroxidase/oxydase.Comprise the mutant of chemically modified or protein engineering.The example of oxidisability bacterium is but is not limited to Aeromonas (Aeromonas sp.), and oxydase can stem from this.
The example of pectate lyase comprises by following different bacterium and belongs to and clone the pectate lyase obtaining, such as erwinia, Rhodopseudomonas, Klebsiella and xanthomonas and subtilis (Nasser etc., (1993) FEBS Letts.335:319-326) and bacillus YA-14 (Kim etc., (1994) Biosci.Biotech.Biochem.58:947-949).
The example (EC3.2.1.78) of mannase comprises those that separate from several bacteriums, comprises genus bacillus organism.The people's such as such as Talbot Appl.Environ.Microbiol, the 56th volume, o. 11th, 3505-3510 page (1990) has been described the 'beta '-mannase that derives from bacstearothermophilus (Bacillus Stearothermophilius).The people's such as Mendoza World J.Microbiol.Biotech., the 10th volume, the 5th phase, 551-555 page (1994) has been described the 'beta '-mannase that derives from subtilis (Bacillus subtilis).JP-A-03047076 discloses the 'beta '-mannase that derives from bacillus.JP-A-63056289 has described the thermally-stabilised 'beta '-mannase of producing alkalescence.JP-A-63036775 relates to bacillus micro-organism FERMP-8856, and it produces 'beta '-mannase and beta-Mannosidase.JP-A-08051975 discloses the alkaline ' beta '-mannase that belongs to AM-001 from Alkaliphilic bacillus.Be described in WO97/11164 from the mannase of bacillus amyloliquefaciens (Bacillus amyloliquefaciens) purifying.WO91/18974 has described hemicellulase, for example, have those of dextranase, zytase or mannosans enzymic activity.What in the embodiment of WO99/64619, pay close attention to is the mannase of bacillus.
Composition can further comprise other enzyme of bacterial origin and/or the enzyme of non-bacterial origin.
lignin compound
Preferred lignin compound comprises lignin polymers, and more preferably it is the lignin polymers of modification.As used herein " lignin polymers of modification " is intended to represent to have carried out chemical reaction with by the covalently bound chemical part xylogen to xylogen.Normally random replacement of the chemical part connecting.
The lignin polymers of preferred modification is by anionic group, cation group or alkoxy base, or the xylogen of its mixture replacement.Preferably, replace and occur in the aliphatic part of xylogen, and be random.Preferably, the lignin polymers of modification is replaced by anionic group, and is preferably sulfonate.Preferred cation group is quaternary amine.Preferred alkoxy base is the polyalkylene oxide chain with the repeating unit of 5 to 30 alkoxyl group parts, preferred oxyethyl group.Preferably, the sulfonated lignin of modification are replaced by anionic group or alkoxy base.The lignin polymers of modification has been discussed in WO/2010/033743.Most preferably, the lignin polymers of modification is sulfonated lignin (Sulfite lignin).Sulfonated lignin can obtain by Howard method.
Exemplary sulfonated lignin can obtain from multiple source, comprise hardwood, cork and regenerant or effluent stream.Sulfonated lignin can thick or pure form utilize, for example " in statu quo " or all liquid state, or with sugar and the lignosulfonic acid salt form of purifying from wherein removing or destroy of other carbohydrate contents, or the lignosulfonic acid salt form of the purifying partly or entirely eliminated of inorganic components.Sulfonated lignin can its salt form, comprise that calcium lignin sulphonate, sodium lignosulfonate, ammonium lignosulphonate, lignosulfonic acid potassium, magnesium lignosulfonate and composition thereof or adulterant utilize.
Sulfonated lignin preferably have 2000 to 100000 weight-average molecular weight.Their basic structural unit is phenyl-propane.Sulfonation degree is preferably 0.3 to 1.0 of every phenyl-propane unit sulfonate group.
Commercially available sulfonated lignin comprise the Ultrazine from Borregaard LignoTech.Other supplier comprises Georgia-Pacific Corporation, Lenzing AG and Tembec Inc.At Lauten, R.A., Myrvold, and Gundersen B.O., S.A. in (2010) New Developments in the Commercial Utilization of Lignosulfonates, at Surfactants from Renewable Resources (M.Kjellin and I.Johansson writes), John Wiley & Sons, Ltd, Chickester, has discussed sulfonated lignin in UK.
tensio-active agent
tensio-active agent
a) bio-surfactant of bacterial origin
Preferred bio-surfactant comprises rhamnolipid, and it can derive from Rhodopseudomonas.
The bio-surfactant of other bacterial origin can derive from " Mapping of Patents in Bioemulsifiers and biosurfactants-review ", be published in Journal of Scientific and Industrial Research the 65th volume, 2006,91 pages.In the definition of bacteriogenic bio-surfactant, we comprised that bacterial gene is wherein cloned and subsequently from another organism express and manufacture those.For example, produced rhamnolipid from intestinal bacteria (E.coli) by this way.
b) from the bio-surfactant of non-bacterial origin
Bio-surfactant within the scope of the present invention also can derive from from yeast and fungi.
Bio-surfactant from non-bacterial micro-organism source comprises those that derive from fungi and yeast, for example sophorolipid, its honeybee from mycocandida (Candida sp.) and torulopsis (Torulopsis sp.) gives birth to candiyeast (Candida apicola), Candida bombicola, separates fatty candiyeast (Candida lipolytica), Candida bogoriensis.Referring to: Environmental applications for biosurfactants (environmental applications of bio-surfactant)-Environmental Pollution, the 133rd volume, 2005, the 183-198 pages, Catherine N.Mulligan.Can also be referring to, Towards commercial production of microbial surfactants (commercial production of MICROBIAL SURFACTANT)-Trends in Biotechnology, the 24th volume, 2006,509-515 page: Soumen Mukherjee, Palashpriya Das, Ramkrishna Sen.
Mannosylerythritol lipid is conventionally from Pseudozyma (thinking in the past mycocandida) Antarctica.Cellobiose fat is conventionally from Ustilago maydis (D C.) Corola. (Ustilago maydis).Marine alga glycolipid is conventionally from Rhod (Rhodococcus sp.).
More information is referring to Production, Characterisation and Application of Biosurfactants Review (production, sign and the summary of Application of bio-surfactant)-Biotechnology-the 7th volume, 2008, the 370th page: Pattanathu, Rahman and Gakpe.
Conventionally the tensio-active agent that does not classify as " biotype " also can be included in the present invention.
Nonionic surface active agent comprises, the reaction product of the compound (for example fatty alcohol, acid, acid amides or alkylphenol) that specifically, there is hydrophobic grouping and hydrogen atoms and oxirane (especially oxyethane separately or together with propylene oxide).Concrete non-ionic detergent compound is C 6-C 22alkylphenol-oxyethane polycondensate, has 5 to 25 EO conventionally, i.e. 5 to 25 ethylene oxide units of per molecule, and the aliphatic C of straight or branched 8-C 18the polycondensation product of uncle or secondary alcohol and oxyethane, it has 5 to 40 EO conventionally.
Operable non-ionic detergent compound is generally has water-soluble organic sulfuric acid of the alkyl group that contains approximately 8 to approximately 22 carbon atoms and an alkali metal salt of sulfonic acid, uses term alkyl to comprise the moieties of senior acyl group.The example of applicable synthetic anionic detergent compound is alkyl sodium sulfonate and potassium, especially by the senior C of sulfation 8-C 18those that alcohol (for example producing from butter or Oleum Cocois) obtains, C 9-C 20the C of sodium alkyl benzene sulfonate and potassium, particularly straight chain 10-C 15secondary sodium alkyl benzene sulfonate; And alkyl glycerol ether sodium sulfate, especially derived from the higher alcohols of butter or Oleum Cocois with derived from those ethers of the synthol of oil.Preferred anionic detergent compound is C 11-C 15sodium alkyl benzene sulfonate and C 12-C 18sodium alkyl sulfate.Also applicable tensio-active agent is those that for example describe in EP-A-328 177 (Unilever), and it has shown salting-out resistance, the alkyl polyglucoside surfactant of describing in EP-A-070 074, and alkyl monoglycosides.
Preferred surfactant system is the mixture of anionic and non-ionic detergent active substance, the anionic of particularly pointing out in EP-A-346 995 (Unilever) and nonionic surface active agent category and example.Especially preferred surfactant system is C 16-C 18an alkali metal salt of primary alconol sulfuric acid and C 12-C 15the ethoxylate of 3 to 7 EO of primary alconol mixture together.
The preferred amount of non-ionic detergent is greater than 10% of surfactivity system, and for example 25 to 90wt%, the amount of aniorfic surfactant can be for example surfactant system approximately 5% to about 40wt%.
Detergent composition can be included in other compositions of conventionally finding in washing liquid.Especially polyester affinity soil release polymer, hydrotropic agent, opalizer, tinting material, spices, other enzyme, other tensio-active agent, composition is as polymkeric substance, SYNTHETIC OPTICAL WHITNER, bleach-activating agent and the bleaching catalyst, antioxidant, pH control agent and the buffer reagent that deposit again of micro-encapsulation object, tenderizer, anti-dirt of spices or nursing additive, thickening material, for external structure agent (having or do not have the functional ingredient being embedded in wherein) and other compositions well known to those skilled in the art rheology modified, vision instruction.
The present invention is described further with reference to following non-limiting examples.
Embodiment
All values are all wt%.
Detergent formulations A
Composition % by weight
Nonionic surface active agent Neodol25-7 6.2
Aniorfic surfactant LAS acid 11.8
Aniorfic surfactant SLES3EO 6.5
Lauric fatty acid P5908 5.2
Glycerine 5.0
MPG 9.0
Citric acid 3.9
Submember (Minors) 2.0
Water Add to 100
wherein:
Neodol25-7 (from Shell)=C 12-C 15alcohol 7-ethoxylate
LAS acid=C 10-C 14alkyl benzene sulphonate (ABS)
SLES=C12-C13 alcohol 3-ethoxylate sulfuric acid Na salt :=Zetesol NL (on average thering are 3 ethylene oxide groups);
lipolytic enzyme (lipase)
Bacterial enzyme is (from Genecor).This is the lipase of bacterial origin, for the lipase Variant M21L of Pseudomonas alcaligenes, be described in the WO94/25578 of Gist-Brocades (M.M.M.J.Cox, H.B.M.Lenting, L.J.S.M.M μ dleners and J.M.van der lann).
rhamnolipid
Rhamnolipid is from the RBR425 of Jeneil Biosurfactant Company (25%AM).
sulfonated lignin
Sulfonated lignin are the Ultrazine NA from Borregaard LignoTech.
embodiment 1
In this embodiment, test, according to enzyme-containing detergent preparation of the present invention, to determine its processing spot, is removed the ability of beef fat spot from cotton fabric.
CS61 (from CFT B.V.Vlaardingen, Holland), it is beef painted on cotton fat spot, utilizes 96 hole fabric drifts to be cut into disk, and is placed in the hole that 96 micropores drip plate.In the preparation of following various combination, wash spot:
(i) bio-surfactant is rhamnolipid (RL) solution (water solvent) 0.9g/L
(ii) sulfonated lignin (LS) solution (water solvent)-3 kind of concentration: 10g/L, 5g/L, 2.5g/L
(iii) fashionable when adding, the lipomax particle that comprising lipase of bacterial origin is 10mg/L:172g is added to the storing solution of making 100mg/L concentration in the water of 50ml, is then diluted in hole, obtains the ultimate density of 10mg/L.
(iv) washing composition A preparation is dissolved in water to obtain the stock solution of 6g/L.
That droplet hole is arranged is following (in hole, cumulative volume 200 μ are l):
1) enzyme of the water of the washing composition A of washing composition A100%:-100 μ l (6g/L storing solution), 80 μ l, 20 μ l (being the water of 20 μ l in the control wells that there is no enzyme)
2) enzyme of the water of the 24g/L rhamnolipid (25% activity) of the A6g/L storing solution of washing composition A70% & rhamnolipid 0.9g/L:-70 μ l, 30 μ l, 80 μ l, 20 μ l (being the water of 20 μ l in the contrast that there is no enzyme)
3) enzyme (being the water of 20 μ l in the contrast that there is no enzyme) of the 24g/L rhamnolipid (25% activity) of the washing composition A6g/L storing solution of washing composition A70% & rhamnolipid 0.9g/L & 10g/L sodium lignosulfonate-70 μ l, 30 μ l, 80 μ l sodium lignosulfonate 25g/L storing solutions, 20 μ l
4) enzyme (being the water of 20 μ l in the contrast that there is no enzyme) of the 24g/L rhamnolipid (25% activity) of the washing composition A6g/L storing solution of washing composition A70% & rhamnolipid 0.9g/L & 5g/L sodium lignosulfonate-70 μ l, 30 μ l, 80 μ l sodium lignosulfonate 12.5g/L storing solutions, 20 μ l
5) enzyme (being the water of 20 μ l in the contrast that there is no enzyme) of the 24g/L rhamnolipid (25% activity) of the washing composition A6g/L storing solution of washing composition A70% & rhamnolipid 0.9g/L & 2.5g/L sodium lignosulfonate-70 μ l, 30 μ l, 80 μ l sodium lignosulfonate 6.25g/L storing solutions, 20 μ l
6) enzyme of the sodium lignosulfonate 25g/L storing solution of the washing composition A6g/L storing solution of washing composition A100% & 10g/L sodium lignosulfonate-100 μ l, 80 μ l, 20 μ l (being the water of 20 μ l in the contrast that there is no enzyme)
7) enzyme of the sodium lignosulfonate 12.5g/L storing solution of the washing composition A6g/L storing solution of washing composition A100% & 5g/L sodium lignosulfonate-100 μ l, 80 μ l, 20 μ l (being the water of 20 μ l in the contrast that there is no enzyme)
8) enzyme of the sodium lignosulfonate 6.25g/L storing solution of the washing composition A6g/L storing solution of washing composition A100% & 2.5g/L sodium lignosulfonate-100 μ l, 80 μ l, 20 μ l (being the water of 20 μ l in the contrast that there is no enzyme).
At room temperature stir one hour in cultivation shaking table with 1400rpm, complete washing.After described washing operation, the demineralised water rinsing twice of 200 μ l for fabric disk, afterwards dried overnight at room temperature in the dark.
After washing, usage platform reflectance (remission) spectrophotometer is measured the situation of removing spot from fabric at 410nm place.Result is expressed as Δ reflectance, and it is to use CIEL*a*b (CIELAB) value to generate, and described CIEL*a*b (CIELAB) value utilizes Hunterlab Ultrascan VIS reflectance spectrophotometer to generate.
Result is presented in table 1:
Table 1 is presented in Fig. 1 in illustrated mode.
Result demonstration, sulfonated lignin have improved lipolytic enzyme (illustrating by Lipomax) removal spot at low temperatures, especially true in the situation that adding bio-surfactant (illustrating by rhamnolipid).
embodiment 2
In this embodiment, check various enzyme/bio-surfactants/lignosulfonic acid salt composition to remove the ability of various fat and greasy dirt stain to determine them.Spot is (lard and purple seven material and pigment vegetation fat spot-in Terg-O-Tometer under medium-scale wash conditions).
The spot using:
-many kinds of spots of 4 × 1em on brocade: lard and purple dye, meat pulp and 5% sunflower seed oil, green curry and instant gravy (only having comprised the result of lard and purple dye), spot is from Warwick Equest Limited.
-7 × 7cm pigment vegetation fat spot on polyester, from (from CFT B.V.Vlaardingen, Holland).
In Terg-O-Tometer at 1L under 20 DEG C (outlet temperature is 23 DEG C) by spot and brocade ballast weight in duplicate together with washing (all clothing load 20g, clothing and liquid weight ratio are 1: 50) 30 minutes, 100rpm stirring.Wash described spot with the preparation of following various combination:
(v) when bio-surfactant is rhamnolipid (RL)-interpolation, be 0.9g/L
10,5,2.5g/L (vi) when sulfonated lignin (LS)-interpolation, be 3 kinds of concentration:
(vii) comprising lipase of bacterial origin is 10mg/L in the time adding
(viii) washing composition A preparation is dissolved in water to provide the stock solution of various concentration.
The amount that is added into the stock solution in Terg-O-Tometer is as follows:
1) Lipomax (1g/L) of the washing composition A of washing composition A100%:20ml (stock solution of 150g/L), 10ml or the water that is 10ml for the contrast solution that there is no enzyme
2) Lipomax of the washing composition A of sulfonated lignin-20ml of washing composition A100% & 10g/L (stock solution of 150g/L), 10 grams of sodium lignosulfonates and 10ml (supplying with the 1g/L storing solution of 100 times of dilutions) or the water that is 10ml for the contrast solution that there is no enzyme
3) the rhamnolipid deposit (72g/L) of the washing composition A storing solution (150g/L) of washing composition A70% & rhamnolipid 0.9g/L-14ml, 50ml and the Lipomax (1g/L) of 10ml or the water that is 10ml for the contrast solution that there is no enzyme
4) the rhamnolipid storing solution (72g/L) of the washing composition A storing solution (150g/L) of sodium lignosulfonate-14ml of washing composition A70% & rhamnolipid 0.9g/L and 10g/L, 50ml, 10 grams of sodium lignosulfonates and the Lipomax storing solution (as above) of 10ml or the water that is 10ml for the contrast solution that there is no enzyme.
At room temperature stir one hour with 1400rpm, complete washing.After described washing operation, the demineralised water rinsing twice of 200 μ l for fabric disk, afterwards dried overnight at room temperature in the dark.
Before cleaning and afterwards, use the color reflectance of Hunterlab Ultrascan VIS reflectance spectrophotometer in 410nm place measurement spot.Result is expressed as Δ reflectance, and this is to use CIEL*a*b (CIELAB) value generating to generate.
Table 2 (being illustrated by Fig. 2)
Table 3 (being illustrated by Fig. 3)
Result shows that sulfonated lignin improve the performance of lipase in detergent composition, especially true in the situation that adding rhamnolipid.

Claims (10)

1. enzyme-containing detergent compositions, it comprises following combination:
(iv) surfactant system;
(v) one or more enzymes; And
(vi) one or more lignin compounds.
2. according to the enzyme-containing detergent compositions of claim 1, the specification sheets of wherein said composition and subzero treatment is packaging together, and described low temperature is less than 40 DEG C, and is preferably less than 30 DEG C, and is more preferably less than 25 DEG C.
3. according to the enzyme-containing detergent compositions of claim 1 or 2, it comprises has a liking for temperature or Zimadzhunt L 340 system.
4. according to the enzyme-containing detergent compositions of aforementioned any one claim, wherein said surfactant system comprises bio-surfactant.
5. according to the enzyme-containing detergent compositions of aforementioned any one claim, wherein said bio-surfactant and described or every kind of enzyme is bacterial origin.
6. the method for processing matrix, comprises the step of utilizing the enzyme-containing detergent compositions of claim 1-5 to process described matrix.
7. according to the method for claim 6, wherein said enzyme-containing detergent compositions is directly applied on part or all of fabric, thereby processes the one or more spots on described fabric.
8. according to the method for claim 6 or 7, wherein said matrix comprises fabric.
9. according to the method for claim 6-8 any one, the time length of wherein said method is less than 60 minutes, is preferably less than 30 minutes.
10. according to the method for claim 6-9 any one, the washing liq temperature of wherein said method is always less than 40 DEG C, and is preferably less than 30 DEG C, and is more preferably less than 25 DEG C.
CN201280045017.8A 2011-09-15 2012-08-30 Detergent compositions comprising surfactant and enzyme Pending CN103946359A (en)

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