EP2756063A1 - Compositions détergentes comprenant un tensioactif et une enzyme - Google Patents

Compositions détergentes comprenant un tensioactif et une enzyme

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Publication number
EP2756063A1
EP2756063A1 EP12756157.9A EP12756157A EP2756063A1 EP 2756063 A1 EP2756063 A1 EP 2756063A1 EP 12756157 A EP12756157 A EP 12756157A EP 2756063 A1 EP2756063 A1 EP 2756063A1
Authority
EP
European Patent Office
Prior art keywords
enzyme
detergent
phospholipase
enzymes
detergent composition
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.)
Granted
Application number
EP12756157.9A
Other languages
German (de)
English (en)
Other versions
EP2756063B1 (fr
Inventor
Andrew Thomas COOK
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
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Filing date
Publication date
Application filed by Unilever PLC, Unilever NV filed Critical Unilever PLC
Priority to EP12756157.9A priority Critical patent/EP2756063B1/fr
Publication of EP2756063A1 publication Critical patent/EP2756063A1/fr
Application granted granted Critical
Publication of EP2756063B1 publication Critical patent/EP2756063B1/fr
Active legal-status Critical Current
Anticipated expiration legal-status Critical

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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
    • 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

Definitions

  • This invention relates to enzymatic detergent compositions. Enzymes are used detergent formulations to aid cleaning and stain removal.
  • the objective of the invention is to improve enzyme performance in detergent formulations.
  • the present invention provides an enzymatic detergent composition comprising the combination of:
  • the invention provides a process for cleaning a substrate, comprising the step of treating the substrate with the enzymatic detergent composition of the first aspect of the invention. With the invention, cleaning performance is improved.
  • the term "substrate” includes fabric, and clothing and laundry items. Accordingly, preferably the process is for cleaning a fabric, i.e. stain/soil removal from fabric.
  • the cleaning process takes place in a washing receptacle containing a wash liquor comprising water and the enzymatic detergent composition.
  • the wash liquor may be applied to the substrate or the substrate may be immersed wholly or partially into the wash liquor.
  • the cleaning process may alternatively comprise direct application of the enzymatic detergent composition (undissolved i.e. without addition of water) on to part or whole of the fabric, so as to directly treat a stain or stains on the fabric.
  • Such a process is preferably a pre-treatment process, so may be followed by treatment with/in a wash liquor (e.g. as a 'main' wash process).
  • the main wash is preferably according to the second aspect of the invention.
  • the process duration is less than 60 minutes, more preferably less than 30 minutes. If it is a pre-treatment process, the pre-treatment step is preferably less than 5 mins, and more preferably less than 2 minutes (although cleaning by the enzyme so applied will continue during at least a part of any washing process which follows).
  • the synergistic combination of the invention is radically improved at low temperature where cleaning of oil and fat stain/soil is more problematic.
  • the wash liquor temperature of the process is less than 40 °C and preferably less than 30°C and more preferably less than 25°C at all times.
  • Low temperature wash liquor is advantageous environmentally and financially.
  • the enzymatic detergent composition is preferably a low temperature
  • the enzymatic detergent composition is preferably packaged with instructions to treat at low temperatures, the low temperatures being preferably less than 40 °C, more preferably less than 30°C even more preferably less than 25°C.
  • the invention is provides enzymatic performance of oily soil and/or stains in a low temperature cleaning processes (with low temperature wash liquor) without serious consideration to the temperature sensitivity of the enzyme.
  • the enzyme can therefore be selected more freely, on the basis of other considerations.
  • the invention is especially advantageous for the particular situation where one requires enzymatic cleaning of oily soil and/or stains in a low temperature cleaning processes (with low temperature wash liquor) but where compositions are by necessity stored at higher temperatures.
  • Psychrophilic enzymes are effective at low temperatures but are sensitive to raised temperatures due to their flexibility.
  • Mesophilic (and thermophilic) enzymes are stable at raised temperatures, but have reduced performance.
  • the invention affords low temperature enzymatic cleaning of a substrate using mesophilic enzymes without needing to expend effort in engineering psychrophilic enzymes which can withstand raised
  • the enzyme system preferably comprises a mesophilic or
  • thermophilic enzyme system The enzyme system may even be a mesophilic and/or thermophilic enzyme system with the exclusion of pyschrophilic enzymes.
  • Enzymes may be from bacterial origin (derived from bacteria) or fungal origin (derived from fungus) however enzymes from bacterial origin are preferred.
  • the composition preferably comprises between 1 to 70 wt % of a surfactant, most preferably 10 to 30 wt %.
  • the surfactant system comprises at least 1 wt% (based on the cleaning composition) of a biosurfactant.
  • a biosurfactant is of bacterial origin.
  • biosurfactant and the enzyme is of bacterial origin.
  • the one or more enzymes may be provided as a system.
  • the one or more enzymes comprises a lipase.
  • Preferred lipases include lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa (T. lanuginosus) or from H. insolens, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis, a
  • Bacillus lipase e.g. from B. subtilis (Dartois et al. (1993), Biochemica et
  • lipase enzymes include LipolaseTM and Lipolase UltraTM, LipexTM (Novozymes A/S) and the Bacterial enzyme, Lipomax ® ex Genecor.
  • This is a bacterially derived Lipase, of variant M21 L of the lipase of Pseudomonas alcaligenes as described in WO 94/25578 to Gist-Brocades (M. M.M.J. Cox, H.B.M. Lenting, L.J.S.M. Mulleners and J.M. van der Laan).
  • Preferred Phospholipases include enzymes which hydrolyse phospholipids.
  • Phospholipases Ai and A 2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form
  • lysophospholipid and lysophospholipase (or phospholipase B) which can hydrolyze the remaining fatty acyl group in lysophospholipid are included as are Phospholipase C and phospholipase D (phosphodiesterases)which release diacyl glycerol or phosphatidic acid respectively.
  • Phospholipase C and phospholipase D phosphodiesterases
  • phospholipase A used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase Ai and/or
  • the phospholipase activity may be provided by enzymes having other activities as well, such as, e.g., a lipase with phospholipase 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.
  • 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.
  • Enterobacter e.g., E. aerogenes, E. cloacae Edwardsiella, E. tarda; Erwinia, e.g., E. herbicola; Escherichia, e.g., E. coli; Klebsiella, e.g., K. pneumoniae; Proteus, e.g., P. vulgaris; Providencia, e.g., P. stuartii; Salmonella, e.g. S. typhimurium; Serratia, e.g., S. liquefasciens, S. marcescens; Shigella, e.g., S. 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, F. solani, or a strain of F. oxysporum.
  • the phospholipase may also be from a filamentous fungus strain within the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger or
  • Preferred phospholipases are derived from a strain of Humicola, especially
  • Humicola lanuginosa or variant and from strains of Fusarium, especially Fusarium oxysporum.
  • the phospholipase may be derived from Fusarium oxysporum DSM 2672.
  • phospholipases comprise a phospholipase Ai (EC. 3.1 .1 .32). or 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).
  • protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, DyrazymTM, EsperaseTM, EverlaseTM, PolarzymeTM, and KannaseTM, (Novozymes A/S), MaxataseTM, MaxacalTM, MaxapemTM,
  • Other enzymes may be selected from the group comprising: cellulases, esterases, peroxidases/oxidases, oxidoreductases, pectases, lyases,
  • Bacterial enzymes for use in the invention are cellulases, esterases, and
  • peroxidases/oxidases peroxidases/oxidases, pectases, lyases, and mannanases, or mixtures thereof.
  • Bacterial genes encoding such enzymes can be transferred to preferred
  • bacterial enzyme as used herein includes enzymes originally from bacteria, however expressed.
  • the composition may comprise cutinase as classified in EC 3.1 .1 .74.
  • An example of bacterial cutinase is that from a strain of Pseudomonas, in particular
  • the enzyme may be a 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 that participate in the hydrolysis of phospholipids. Several types of phospholipase activity can be distinguished, including phospholipases Ai and A 2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form
  • lysophospholipid lysophospholipid
  • lysophospholipase or phospholipase B which can hydrolyze the remaining fatty acyl group in lysophospholipid.
  • Phospholipase C and phospholipase D release diacyl glycerol or
  • 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
  • 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 is of bacterial origin 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. coli; Klebsiella, e.g., K. pneumoniae; Proteus, e.g., P. vulgaris; Providencia, e.g., P. stuartii; Salmonella, e.g. S. typhimurium; Serratia, e.g., S. liquefasciens, S. marcescens; Shigella, e.g., S. flexneri;
  • Suitable cellulases are especially of bacterial origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas and Clostridia. Suitable peroxidases/oxidases are especially of bacterial origin. Chemically modified or protein engineered mutants are included. An example of an oxidative bacterium is, but not limited to, are Aeromonas sp wherefrom oxidases can be sou reed.
  • pectate lyases examples include pectate lyases that have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and
  • mannanases examples include those isolated from several bacteria, including Bacillus organisms.
  • Talbot et al., Appl. Environ. Microbiol, Vol.56, No. 1 1 , pp. 3505-3510 (1990) describes a beta-mannanase derived from Bacillus stearothermophilus. Mendoza et al., World J. Microbiol.
  • Biotech., Vol. 10, No. 5, pp. 551 -555 (1994) describes a beta-mannanase derived from Bacillus subtilis.
  • JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp.
  • JP-A-63056289 describes the production of an alkaline, thermostable beta-mannanase.
  • JP-A-63036775 relates to the Bacillus microorganism FERM P- 8856 which produces beta-mannanase and beta-mannosidase.
  • JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001 .
  • a purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/1 1 164.
  • WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active.
  • composition may further comprise other enzymes of bacterial origin and/or enzymes that are not of bacterial origin.
  • Lignin compounds may further comprise other enzymes of bacterial origin and/or enzymes that are not of bacterial origin.
  • the lignin compound comprises a lignin polymer and more preferably it is a modified lignin polymer.
  • a modified lignin polymer is intended to mean lignin that has been subjected to a chemical reaction to covalently attach chemical moieties to the lignin. The attached chemical moieties are usually randomly substituted.
  • Preferred modified lignin polymers are lignins substituted with anionic, cationic or alkoxy groups, or mixtures thereof. Preferably the substitution occurs on the aliphatic portion of the lignin and is random.
  • the modified lignin polymer is substituted with an anionic group, and preferably it is a sulfonate.
  • a preferred cationic group is a quanternary amine.
  • Preferred alkoxy groups are polyalkylene oxide chains having repeat units of alkoxy moieties in the range from 5 to 30, most preferably ethoxy.
  • the modified lignin sulfonate is substituted with anionic or alkoxy groups.
  • Modified lignin polymers are discussed in WO/2010/033743. Most preferably the modified lignin polymer is lignin sulfonate (lignosulfonate). Lignin sulfonate may be obtained by the Howard process.
  • Exemplary lignin sulfonate may be obtained from a variety of sources including hardwoods, softwoods and recycling or effluent streams.
  • the lignin sulfonate may be utilized in crude or pure forms, e.g., in an "as is” or whole liquor condition, or in a purified lignin sulfonate form from which or in which sugars and other saccharide constituents have been removed or destroyed, or from which or in which inorganic constituents have been partially or fully eliminated.
  • the lignin sulfonate may be utilized in salt forms including calcium lignin sulfonate, sodium lignin sulfonate, ammonium lignin sulfonate, potassium lignin sulfonate, magnesium lignin sulfonate and mixtures or blends thereof.
  • the lignin sulfonate preferably has a weight average molecular weight of from 2000 to 100000. Their basic structural unit is phenylpropane. The degree of sulfonation is preferably from 0.3 and 1 .0 sulfate groups per phenylpropane unit.
  • Commercially available Lignin sulfonates include Ultrazine from Borregaard
  • LignoTech Other suppliers include Georgia-Pacific Corporation, Lenzing AG and Tembec Inc. Lignin sulfonates are discussed in Lauten, R. A., Myrvold, B. O. and Gundersen, S. A. (2010) New Developments in the Commercial Utilization of Lignosulfonates, in Surfactants from Renewable Resources (eds M. Kjellin and I. Johansson), John Wiley & Sons, Ltd, Chichester, UK.
  • the biosurfactant comprises a Rhamnolipid, which may be derived from Pseudomonas sp.
  • bacterially derived biosurfactants are available from "Mapping of Patents in Bioemulsifiers and biosurfactants - review, published in the Journal of Scientific and Industrial Research Vol 65, 2006, P91 . Within the definition of bacterially produced biosurfactants, we include those where a bacterial gene is cloned and subsequently expressed from another organism as a manufacturing technique. For example, Rhamnolipids have been produced from E. coli in this way. b) Biosurfactants from non-bacterial sources
  • Biosurfactants within the scope of this invention may also be derived from yeasts and fungi.
  • Biosurfactants from non-bacterial microbial sources include those derived from fungi and yeasts, e.g. sophorolipids from Candida sp and Torulopsis sp.
  • Candida apicola, Candida bombicola, Candida lipolytica, Candida bogoriensis See:
  • Mannosylerythritol Lipids are typically from Pseudozyma (formerly Candida) Antarctica. Cellobiose lipids are typically from Ustilago maydis. Trehalose Lipids typically from Rhodococcus sp.
  • Nonionic surfacants include, in particular, the reaction products of compounds having a hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids, amides or alkyl phenols with alkylene oxides, especially ethylene oxide either alone or with propylene oxide.
  • Specific nonionic detergent include, in particular, the reaction products of compounds having a hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids, amides or alkyl phenols with alkylene oxides, especially ethylene oxide either alone or with propylene oxide.
  • C6 to C22 alkyl phenol-ethylene oxide condensates generally 5 to 25 EO, i.e. 5 to 25 units of ethylene oxide per molecule, and the condensation products of aliphatic Cs to C18 primary or secondary linear or branched alcohols with ethylene oxide, generally 5 to 40 EO.
  • Nonionic detergent compounds which may be used are usually water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher acyl radicals.
  • suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, especially those obtained by sulphating higher Cs to Cis alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl Cg to C20
  • benzene sulphonates particularly sodium linear secondary alkyl C10 to C15 benzene sulphonates; and sodium alkyl glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.
  • the preferred anionic detergent compounds are sodium C11 to C15 alkyl benzene sulphonates and sodium C12 to Cis alkyl sulphates.
  • surfactants such as those described in EP-A-328 177 (Unilever), which show resistance to salting-out, the alkyl polyglycoside surfactants described in EP-A-070 074, and alkyl monoglycosides.
  • Preferred surfactant systems are mixtures of anionic with nonionic detergent active materials, in particular the groups and examples of anionic and nonionic surfactants pointed out in EP-A-346 995 (Unilever).
  • surfactant system that is a mixture of an alkali metal salt of a C16 to Cis primary alcohol sulphate together with a C12 to C15 primary alcohol 3 to 7 EO ethoxylate.
  • the nonionic detergent is preferably present in amounts greater than 10%, e.g. 25 to 90 wt % of the surfactant system.
  • Anionic surfactants can be present for example in amounts in the range from about 5% to about 40 wt % of the surfactant system.
  • the detergent composition may comprise other ingredients commonly found in laundry liquids. Especially polyester substantive soil release polymers,
  • hydrotropes opacifiers, colorants, perfumes, other enzymes, other surfactants, microcapsules of ingredients such as perfume or care additives, softeners, polymers for anti redeposition of soil, bleach, bleach activators and bleach catalysts, antioxidants, pH control agents and buffers, thickeners, external structurants for rheology modification, visual cues, either with or without functional ingredients embedded therein and other ingredients known to those skilled in the
  • Neodol 25-7 ex.Shell C12-C15 alcohol 7-ethoxylate
  • LAS acid C10-C14 alkyl benzene sulphonic acid
  • Lipomax ® ex Genecor This is a bacterially derived Lipase, of variant M21 L of the lipase of Pseudomonas alcaligenes as described in WO 94/25578 to Gist-Brocades (M. M.M.J. Cox, H.B.M. Lenting, L.J.S.M.
  • the rhamnolipid is RBR425 (25% AM) ex Jeneil Biosurfactant Company. Lignosulphonate
  • Lignosulphonate is Ultrazine NA ex Borregaard LignoTech. Example 1
  • enzymatic detergent formulations according to the invention were tested to determine their ability to treat i.e. remove beef fat stains from cotton fabric.
  • CS61 (ex. CFT B.V. Vlaardingen, the Netherlands) which is coloured beef fat stain on cotton, was cut into round discs with a 96 well fabric punch and placed in the wells of a 96 micro titre well plate. Stains were washed in formulations in different combinations of:
  • biosurfactant being rhamnolipid (RL) solution (solvent water) 0.9 g/L
  • bacterial lipase is10mg/L when added : 172g of lipomax granules are added to 50mls water to make a 100mg/L concentration stock solution which is then diluted in the well to give final concentration of 10g/L.
  • micro titre well layout was as follows (200ul total volume in well):
  • Detergent A 100% :- 10Oul of detergent A (6g/L stock), 80ul water, 20ul enzyme (20ul water in no enzyme control wells)
  • Detergent A 70% & Rhamnolipid 0.9g/L - 70ul A 6g/L stock, 30ul 24g/L Rhamnolipid (25% active), 80ul water, 20ul enzyme (20ul water in no enzyme control)
  • Stain removal from the fabric was measured at 410 nm using a flatbed remission spectrophotometer after the wash.
  • the results are expressed as delta remission, which was generated using the CIEL * a * b (CIELAB) values generated using the Hunterlab Ultrascan VIS remission spectrophotometer.
  • lignin sulphonate improves stain removal by a lipolytic enzyme (exemplified by Lipomax) at low temperature especially when a biosurfactant (exemplified by rhamnolipid) is incorporated.
  • Stains were washed together with woven cotton ballast (total cloth load 20g, 1 :50 cloth to liquor ratio by weight) in duplicate in 1 Litre tergotometers at 20 °C (final temperature 23 °C. for 30 mins, 100 rpm agitation. Stains were washed in formulations in different combinations of:
  • biosurfactant being rhamnolipid (RL) - 0.9 g/L when added
  • Lipomax (1 g/L) or 10ml water for the no enzyme control solutions 2) Detergent A 100% & 10g/L Sodium Lignosulphonate - 20ml Detergent A (150g/L), 10 grams sodium lignosulphonate and 10ml Lipomax (make up x100 stock at 1g/L) or 10ml water for the no enzyme control solutions 3) Detergent A & 70% Rhamnolipid 0.9g/L - 14ml Detergent A stock

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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

L'invention concerne une composition détergente enzymatique comprenant une combinaison constituée d'un système de tensioactif, d'une ou de plusieurs enzymes et d'un ou de plusieurs composés de lignine. L'invention concerne aussi un procédé de traitement d'un substrat, qui comporte les étapes consistant à: traiter le substrat à l'aide d'une composition détergente enzymatique comprenant la combinaison constituée du système de tensioactif, d'une ou de plusieurs enzymes et d'un ou de plusieurs composés de lignine.
EP12756157.9A 2011-09-15 2012-08-30 Compositions détergentes comprenant un tensioactif et une enzyme Active EP2756063B1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP12756157.9A EP2756063B1 (fr) 2011-09-15 2012-08-30 Compositions détergentes comprenant un tensioactif et une enzyme

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
EP11181392 2011-09-15
EP12756157.9A EP2756063B1 (fr) 2011-09-15 2012-08-30 Compositions détergentes comprenant un tensioactif et une enzyme
PCT/EP2012/066860 WO2013037643A1 (fr) 2011-09-15 2012-08-30 Compositions détergentes comprenant un tensioactif et une enzyme

Publications (2)

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EP2756063A1 true EP2756063A1 (fr) 2014-07-23
EP2756063B1 EP2756063B1 (fr) 2017-10-04

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EP (1) EP2756063B1 (fr)
CN (1) CN103946359A (fr)
AR (1) AR087847A1 (fr)
BR (1) BR112014005687A2 (fr)
CL (1) CL2014000636A1 (fr)
WO (1) WO2013037643A1 (fr)
ZA (1) ZA201401260B (fr)

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DE102013205755A1 (de) * 2013-04-02 2014-10-02 Evonik Industries Ag Waschmittelformulierung für Textilien enthaltend Rhamnolipide mit einem überwiegenden Gehalt an di-Rhamnolipiden
EP3002328A1 (fr) * 2014-09-30 2016-04-06 Evonik Degussa GmbH Formule contenant des bio-tenseurs
DE102014221889B4 (de) * 2014-10-28 2023-12-21 Henkel Ag & Co. Kgaa Waschmittel mit Mannosylerythritollipid, Verstärkung der Reinigungsleistung von Waschmitteln durch Mannosylerythritollipid, und Waschverfahren unter Einsatz von Mannosylerythritollipid
GB201505287D0 (en) 2015-03-27 2015-05-13 Bangor University And Croda Internat Plc Method of seperating Mannosylerythitol Lipids
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WO2013037643A1 (fr) 2013-03-21
CL2014000636A1 (es) 2014-08-22
ZA201401260B (en) 2016-05-25
AR087847A1 (es) 2014-04-23
CN103946359A (zh) 2014-07-23
EP2756063B1 (fr) 2017-10-04

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