EP2756063B1 - Compositions détergentes comprenant un tensioactif et une enzyme - Google Patents

Compositions détergentes comprenant un tensioactif et une enzyme Download PDF

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EP2756063B1
EP2756063B1 EP12756157.9A EP12756157A EP2756063B1 EP 2756063 B1 EP2756063 B1 EP 2756063B1 EP 12756157 A EP12756157 A EP 12756157A EP 2756063 B1 EP2756063 B1 EP 2756063B1
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Prior art keywords
enzyme
detergent
phospholipase
enzymes
detergent composition
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German (de)
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EP2756063A1 (fr
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Andrew Thomas COOK
Neil James Parry
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Unilever PLC
Unilever NV
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Unilever PLC
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

Definitions

  • This invention relates to enzymatic detergent compositions.
  • Enzymes are used in detergent formulations to aid cleaning and stain removal.
  • US 2010/0075878 A1 , US 2003/0139319 A1 and US 6,271,190 B1 disclose detergent compositions comprising a surfactant system, one or more enzymes and one or more lignin compounds.
  • 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 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.
  • 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 composition. Accordingly, 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 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 temperatures.
  • 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.
  • the 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 Biophysica Acta, 1131, 253-360 ), B . stearothermophilus ( JP 64/744992 ) or B . pumilus ( WO 91/16422 ).
  • 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 M21L 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 A 1 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 A used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase A 1 and/or Phospholipase A 2 activity.
  • the phospholipase activity may be provided by enzymes having other activities as well, such as, e.g., a lipase with phospholipase activity.
  • the phospholipase may be of any origin, e.g., of animal origin (such as, e.g., mammalian), e.g. from pancreas (e.g., bovine or porcine pancreas), or snake venom or bee venom.
  • animal origin such as, e.g., mammalian
  • pancreas e.g., bovine or porcine pancreas
  • snake venom or bee venom e.g., from snake venom or bee venom.
  • the phospholipase may be of microbial origin, e.g., from filamentous fungi, yeast or bacteria, such as the genus or species Aspergillus, e.g., A. niger, Dictyostelium, e.g., D. discoideum; Mucor, e.g. M. javanicus, M. mucedo, M.
  • subtilissimus Neurospora, e.g. N. crassa; Rhizomucor, e.g., R. pusillus; Rhizopus, e.g. R . arrhizus, R. japonicus, R. stolonifer; Sclerotinia, e.g., S . libertiana; Trichophyton, e.g. T. rubrum; Whetzelinia, e.g., W. sclerotiorum; Bacillus, e.g., B . megaterium, B. subtilis; Citrobacter, e.g., C . freundii; Enterobacter, e.g., E.
  • aerogenes E. cloacae Edwardsiella, E. tarda; Erwinia, e.g., E. herbicola; Escherichia, e.g., E. 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; Streptomyces, e.g., S .
  • the phospholipase may be fungal, e.g., from the class Pyrenomycetes, such as the genus Fusarium, such as a strain of F. culmorum, F. heterosporum, F. solani, or a strain of F. oxysporum.
  • the phospholipase may also be from a filamentous fungus strain within the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger or Aspergillus oryzae.
  • Preferred phospholipases are derived from a strain of Humicola, especially Humicola lanuginosa or variant; and from strains of Fusarium, especially Fusarium oxysporum.
  • the phospholipase may be derived from Fusarium oxysporum DSM 2672.
  • phospholipases comprise a phospholipase A 1 (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, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
  • enzymes may be selected from the group comprising: cellulases, esterases, peroxidases/oxidases, oxidoreductases, pectases, lyases, mannanases and mixtures thereof.
  • Bacterial enzymes for use in the invention are cellulases, esterases, peroxidases/oxidases, pectases, lyases, and mannanases, or mixtures thereof. Bacterial genes encoding such enzymes can be transferred to preferred expression production hosts, which are not limited to bacterial and includes for example other microbial hosts.
  • the term 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 Pseudomonas mendocina, or Pseudomonas putida.
  • 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.
  • phospholipases A 1 and A 2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid
  • lysophospholipase or phospholipase B
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (A 1 or A 2 ), phospholipase B activity, phospholipase C activity or phospholipase D activity.
  • phospholipase A used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase A 1 and/or Phospholipase A 2 activity.
  • the phospholipase activity may be provided by enzymes having other activities as well, such as, e.g., a lipase with phospholipase activity.
  • the phospholipase activity may, e.g., be from a lipase with phospholipase side activity.
  • the phospholipase enzyme activity is provided by an enzyme having essentially only phospholipase activity and wherein the phospholipase enzyme activity is not a side activity.
  • the phospholipase 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 sourced.
  • pectate lyases examples include pectate lyases that have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, as well as from Bacillus subtilis ( Nasser et al. (1993) FEBS Letts. 335:319-326 ) and Bacillus sp. YA-14 ( Kim et al. (1994) Biosci. Biotech. Biochem. 58:947-949 ).
  • mannanases examples include those isolated from several bacteria, including Bacillus organisms.
  • Talbot et al., Appl. Environ. Microbiol, Vol.56, No. 11, pp. 3505-3510 (1990 ) describes a beta-mannanase derived from Bacillus stearothermophilus.
  • Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994 ) describes a beta-mannanase derived from Bacillus subtilis.
  • JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp.
  • JP-A-63056289 describes the production of an alkaline, thermostable beta-mannanase.
  • JP-A-63036775 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase.
  • JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001.
  • a purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/11164 .
  • WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active.
  • composition 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 .
  • 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.
  • 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 .
  • 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.
  • 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: Environmental applications for biosurfactants - Environmental Pollution, Volume 133, 2005, Pages 183-198 Catherine N. Mulligan. See also, Towards commercial production of microbial surfactants - Trends in Biotechnology, Volume 24, 2006, Pages 509-515 : Soumen Mukherjee, Palashpriya Das, Ramkrishna Sen.
  • 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 compounds are C 6 to C 22 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 C 8 to C 18 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 C 8 to C 18 alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl C 9 to C 20 benzene sulphonates, particularly sodium linear secondary alkyl C 10 to C 15 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 C 11 to C 15 alkyl benzene sulphonates and sodium C 12 to C 18 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 C 16 to C 18 primary alcohol sulphate together with a C 12 to C 15 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 art.
  • the invention will now be further described with reference to the following nonlimiting examples.
  • Detergent formulation A Ingredient % by weight Non-ionic surfactant Neodol 25-7 6.2 Anionic surfactant LAS acid 11.8 Anionic surfactant SLES 3EO 6.5 Lauric Fatty Acid P5908 5.2 Glycerol 5.0 Monopropylene Glycol 9.0 Citric acid 3.9 Minors 2.0 Water balance to 100 Wherein:
  • Lipomax® ex Genecor This is a bacterially derived Lipase, of variant M21L 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).
  • the rhamnolipid is RBR425 (25% AM) ex Jeneil Biosurfactant Company.
  • Lignosulphonate is Ultrazine NA ex Borregaard LignoTech.
  • 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:
  • micro titre well layout was as follows 200 ⁇ l total volume in well):
  • 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.
  • Table 1 is graphically illustrated in Fig1. 1 2 3 4 5 6 7 8 with Lipomax average 37.64 44.85 58.04 53.58 49.09 39.66 37.60 37.77 std dev 0.56 1.35 1.75 1.78 1.63 0.92 0.84 0.42 without Lipomax average 37.15 36.10 35.86 35.42 35.97 35.67 36.27 36.30 std dev 1.03 1.13 0.59 0.25 0.87 0.97 1.08 0.45
  • lignin sulphonate improves stain removal by a lipolytic enzyme (exemplified by Lipomax) at low temperature especially when a biosurfactant (exemplified by rhamnolipid) is incorporated.
  • various enzyme/biosurfactant/lignin sulphonate compositions were examined to determine their ability to remove a range of fat and oil stains.
  • the stains were (lard and violet dye and pigment vegetable fat stain -under medium scale wash conditions in tergotometers).
  • 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:
  • washes were carried out at room temperature, at 1400 rpm agitation for an hour. Following the washing operation, the fabric discs were rinsed twice with 200 ⁇ L demineralised water, prior to drying at room temperature in the dark overnight.

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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)

Claims (9)

  1. Composition de détergent enzymatique comprenant la combinaison de :
    (i) un système de tensioactif ;
    (ii) une ou plusieurs enzymes ; et
    (iii) un ou plusieurs composés de lignine, où le système de tensioactif comprend un biotensioactif.
  2. Composition de détergent enzymatique selon la revendication 1, où la composition est emballée avec des instructions pour traiter à basses températures, les basses températures étant inférieures à 40°C et de préférence inférieures à 30°C et encore mieux inférieures à 25°C.
  3. Composition de détergent enzymatique selon la revendication 1 ou la revendication 2, laquelle comprend un système d'enzyme mésophile ou thermophile.
  4. Composition de détergent enzymatique selon l'une quelconque des revendications précédentes, où le biotensioactif et le ou chaque enzyme sont dérivés par voie bactérienne.
  5. Procédé de traitement d'un substrat, comprenant les étapes de traitement du substrat avec la composition de détergent enzymatique des revendications 1-4.
  6. Procédé selon la revendication 5, où la composition de détergent enzymatique est directement appliquée à une partie ou la totalité du textile, afin de traiter une tache ou des taches sur le textile.
  7. Procédé selon la revendication 5 ou 6, où le substrat comprend un textile.
  8. Procédé selon l'une quelconque des revendications 5-7, où la durée du procédé est inférieure à 60 minutes, de préférence inférieure à 30 minutes.
  9. Procédé selon l'une quelconque des revendications 5-8, où la température de liqueur de lavage du procédé est inférieure à 40°C et de préférence inférieure à 30°C et bien mieux encore inférieure à 25°C à tout moment.
EP12756157.9A 2011-09-15 2012-08-30 Compositions détergentes comprenant un tensioactif et une enzyme Active EP2756063B1 (fr)

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

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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
AR105805A1 (es) * 2015-08-28 2017-11-08 Unilever Nv Composiciones de lavado mejoradas
WO2017103947A1 (fr) * 2015-12-17 2017-06-22 Proklean Technologies Pvt. Ltd Composition détergente biodégradable
EP4291625A1 (fr) * 2021-02-12 2023-12-20 Novozymes A/S Détergents biologiques stabilisés
JP2024514838A (ja) * 2021-04-06 2024-04-03 リグノソル・アイピー・リミテッド リグニンベースの組成物及び関連方法
AU2022338142A1 (en) * 2021-08-30 2024-03-07 Locus Solutions Ipco, Llc Compositions for improving the environmental impact of printing and dyeing
CN117957300A (zh) * 2021-09-20 2024-04-30 联合利华知识产权控股有限公司 洗涤剂组合物

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AR087847A1 (es) 2014-04-23
EP2756063A1 (fr) 2014-07-23
CN103946359A (zh) 2014-07-23
CL2014000636A1 (es) 2014-08-22
WO2013037643A1 (fr) 2013-03-21
ZA201401260B (en) 2016-05-25
BR112014005687A2 (pt) 2017-04-04

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