EP2756063A1 - Detergent compositions comprising surfactant and enzyme - Google Patents

Detergent compositions comprising surfactant and 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)
French (fr)
Other versions
EP2756063B1 (en
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
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Unilever PLC, Unilever NV filed Critical Unilever PLC
Priority to EP12756157.9A priority Critical patent/EP2756063B1/en
Publication of EP2756063A1 publication Critical patent/EP2756063A1/en
Application granted granted Critical
Publication of EP2756063B1 publication Critical patent/EP2756063B1/en
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

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

DETERGENT COMPOSITIONS COMPRISING SURFACTANT AND ENZYME
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. In a first aspect, the present invention provides an enzymatic detergent composition comprising the combination of:
(i) a surfactant system;
(ii) one or more enzymes
(iii) one or more lignin compounds.
In a second aspect, 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.
As used herein, 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.
Preferably 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.
Preferably 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.
Preferably 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 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
temperatures.
Accordingly, 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 %.
Preferably the surfactant system comprises at least 1 wt% (based on the cleaning composition) of a biosurfactant. Preferably the biosurfactant is of bacterial origin.
Preferably the biosurfactant and the enzyme is of bacterial origin.
Chemically modified or protein engineered mutants are included. The one or more enzymes may be provided as a system.
Preferably 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, 1 131 , 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).
Commercially available lipase enzymes include Lipolase™ and Lipolase Ultra™, Lipex™ (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 ( EC 3.1 .1 .4 and/or EC 3.1 .1 .32) include enzymes which hydrolyse phospholipids. Phospholipases Ai and A2 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.
The term "phospholipase A" used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase Ai and/or
Phospholipase A2 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. Preferably 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. violeceoruber; Yersinia, e.g., Y. enterocolitica. Thus, 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.
Preferably phospholipases comprise a phospholipase Ai (EC. 3.1 .1 .32). or a phospholipase A2 (EC.3.1 .1 .4.). Examples of commercial phospholipases include LECITASE™ and LECITASE™ ULTRA, YIELSMAX, or LIPOPAN F (available from Novozymes A/S, Denmark).
Commercially available protease enzymes include Alcalase™, Savinase™, Primase™, Duralase™, Dyrazym™, Esperase™, Everlase™, Polarzyme™, and Kannase™, (Novozymes A/S), Maxatase™, Maxacal™, Maxapem™,
Properase™, Purafect™, Purafect OxP™, FN2™, and FN3™ (Genencor
International Inc.). Other 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. As used herein, the term 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 A2 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. Phospholipase C and phospholipase D (phosphodiesterases) release diacyl glycerol or
phosphatidic acid respectively.
The term phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (Ai or A2), phospholipase B activity, phospholipase C activity or phospholipase D activity. The term "phospholipase A" used herein in connection with an enzyme of the invention is intended to cover an enzyme with
Phospholipase Ai and/or Phospholipase A2 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. In other embodiments of the invention, 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.
Preferably, 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.
Examples of pectate lyases 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).
Examples of mannanases (EC 3.2.1 .78) include those isolated from several bacteria, including Bacillus organisms. For example, 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. Bacillus sp. mannanases concerned in the Examples in WO 99/64619.
The composition may further comprise other enzymes of bacterial origin and/or enzymes that are not of bacterial origin. Lignin compounds
Preferably the lignin compound comprises a lignin polymer and more preferably it is a modified lignin polymer. As used herein "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. Preferably 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. Preferably 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.
Surfactant
Surfactants
a) Bacte ally derived Biosurfactants
Preferably the biosurfactant comprises a Rhamnolipid, which may be derived from Pseudomonas sp.
Other 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:
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.
Further information is given in Production, Characterisation and Applications of Biosurfactants Review - Biotechnology - Volume 7, 2008, page 370: Pattanathu, Rahman and Gakpe. Surfactants not generally classified as "biological" may also be included in the invention.
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 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. Examples of 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. Also applicable are 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). Especially preferred is 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
The invention will now be further described with reference to the following limiting examples.
Examples
All values throughout are wt%/. Detergent formulation A
Ingredient % by weight
Non-ionic surfactant Neodol 25-7 6.2
Anionic surfactant LAS acid 1 1 .8
Anionic surfactant SLES 3EO 6.5
Laurie Fatty Acid P5908 5.2
Glycerol 5.0
Monopropylene Glycol 9.0
Citric acid 3.9
Minors 2.0
Water balance to 100
Wherein:
Neodol 25-7 ex.Shell = C12-C15 alcohol 7-ethoxylate
LAS acid = C10-C14 alkyl benzene sulphonic acid;
SLES = C12-C13 alcohol 3-ethoxylate sulphate, Na salt
sulphate (with on average 3 ethylene oxide groups);
Lipolytic Enzyme (lipase)
Bacterial enzyme is 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).
Rhamnolipid
The rhamnolipid is RBR425 (25% AM) ex Jeneil Biosurfactant Company. Lignosulphonate
Lignosulphonate is Ultrazine NA ex Borregaard LignoTech. Example 1
In this example, 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:
(i) biosurfactant being rhamnolipid (RL) solution (solvent water) 0.9 g/L
(ii) lignin sulphonate (LS) solution (sovent water) - 3 concentrations: 10g/L;
5g/L; 2.5 g/L
(iii) 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.
(iv) detergent A formulation dissolved in water to give 6g/L stock solution.
The micro titre well layout was as follows (200ul total volume in well):
1 ) 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) ) Detergent A 70% & Rhamnolipid 0.9g/L & 10g/L Sodium
Lignosulphonate - 70ul Detergent A 6g/L stock, 30ul 24g/L Rhamnolipid (25% active), 80ul Sodium lignosulphonate 25g/L stock, 20ul enzyme (20ul water in no enzyme control) ) Detergent A 70% & Rhamnolipid 0.9g/L & 5g/L Sodium
Lignosulphonate - 70ul Detergent A 6g/L stock, 30ul 24g/L Rhamnolipid (25% active), 80ul Sodium lignosulphonate 12.5g/L stock, 20ul enzyme (20ul water in no enzyme control) ) Detergent A 70% & Rhamnolipid 0.9g/L & 2.5g/L Sodium
Lignosulphonate - 70ul Detergent A 6g/L stock, 30ul 24g/L Rhamnolipid (25% active), 80ul Sodium lignosulphonate 6.25g/L stock, 20ul enzyme (20ul water in no enzyme control) ) Detergent A 100% & 10g/L Sodium Lignosulphonate - 10Oul Detergent A 6g/L stock, 80ul Sodium lignosulphonate 25g/L stock, 20ul enzyme (20ul water in no enzyme control) ) Detergent A 100% & 5g/L Sodium Lignosulphonate - 10Oul Detergent A 6g/L stock, 80ul Sodium lignosulphonate 12.5g/L stock, 20ul enzyme (20ul water in no enzyme control) ) Detergent A 100% & 2.5g/L Sodium Lignosulphonate - 10Oul Detergent A 6g/L stock, 80ul Sodium lignosulphonate 6.25g/L stock, 20ul enzyme (20ul water in no enzyme control) Washes were carried out at room temperature, at 1400 rpm agitation for an hour hour in an incubator shaker. Following the washing operation, the fabric discs were rinsed twice with 200μΙ_ demineralised water, prior to drying at room temperature in the dark overnight.
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.
Results are shown in Table 1 :
Table 1 is graphically illustrated in Fig 1 The results show that lignin sulphonate improves stain removal by a lipolytic enzyme (exemplified by Lipomax) at low temperature especially when a biosurfactant (exemplified by rhamnolipid) is incorporated.
Example 2
In this example, 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 used:
-4x 1 cm multi stain on woven cotton: lard and violet dye, ragu and 5% sunflower oil, green curry and instant gravy (only results for lard and violet dye are included), stains from Warwick Equest Limited.
-7 x 7cm pigment vegetable fat stain on polyester from (ex. CFT B.V. Vlaardingen, the Netherlands)
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:
(v) biosurfactant being rhamnolipid (RL) - 0.9 g/L when added
(vi) lignin sulphonate (LS)- 3 concentrations: 10, 5, 2.5 g/L when added
(vii) bacterial lipase 10mg/L when added
(viii) detergent A formulation dissolved in water to give varying
concentrations of stock solutions. The quantities of stock solutions added to the tergotometers were as follows:
1 ) Detergent A 100% : 20ml Detergent A (150g/L stock solution), 10ml
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
(150g/L), 50ml of Rhamnolipid stock (72g/L) and 10ml Lipomax stock (1 g/L) or 10ml water for the no enzyme control solutions 4) Detergent A 70% Rhamnolipid 0.9g/L and 10g/L Sodium Lignosulphonate - 14ml Detergent A stock (150g/L), 50ml of Rhamnolipid stock (72g/L), 10 grams of Sodium Lignosulphonate and 10ml Lipomax stock (see above) or 10ml water for the no enzyme control solutions 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 μί demineralised water, prior to drying at room temperature in the dark overnight.
Colour remission of the stains was measured at 410nm using a Hunterlab Ultrascan VIS remission spectrophotometer before and after wash. The results are expressed as delta remission, which was generated using the CIEL*a*b (CIELAB) values generated.
Table 2 (illustrated in figure 2)
Lard and violet dye
MTS 100% MTS 100% 10g/L NaL MTS 70%/ Rham 0.9g/L MTS 70%/ Rham 0.9g/L, 10g/L NaL with Lipomax
Control Average 12.73 9.56 13.32 12.78
Std Dev 2.03 2.65 2.35 2.44 Table 3 (illustrated in figure 3)
The results show that lignin sulphonate improves lipase performance in a detergent composition especially when a rhamnolipid is incorporated.

Claims

1 . An enzymatic detergent composition comprising the combination of :
(iv) a surfactant system;
(v) one or more enzymes; and
(vi) one or more lignin compounds.
2. An enzymatic detergent composition according to claiml wherein the
composition is packaged with instructions to treat at low temperatures, the low temperatures being less than 40 °C and preferably less than 30°C and more preferably less than 25°C.
3. An enzymatic detergent composition according to claim 1 or claim 2 which comprises a mesophilic or thermophilic enzyme system.
4. An enzymatic treatment composition according to any preceding claim
wherein the surfactant system comprises a biosurfactant.
5. An enzymatic detergent composition according to any preceding claim
wherein the biosurfactant and the or each enzyme is bacterially derived.
6. A process for treating a substrate, comprising the steps of treating the
substrate with the enzymatic detergent composition of claims 1 - 5.
7. A process according to claim 6 in which the enzymatic detergent
composition is directly applied on to part or whole of the fabric, so as to treat a stain or stains on the fabric.
8. A process according to claim 6 or 7 wherein the substrate comprises a
fabric.
9. A process according to any of claims 6 - 8 wherein the process duration is less than 60 minutes, preferably less than 30 minutes.
10. A process according to any of claims 6 - 9 wherein 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.
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Families Citing this family (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE102013205755A1 (en) * 2013-04-02 2014-10-02 Evonik Industries Ag Detergent formulation for textiles containing rhamnolipids with a predominant content of di-rhamnolipids
EP3002328A1 (en) * 2014-09-30 2016-04-06 Evonik Degussa GmbH Formulation containing biotensides
DE102014221889B4 (en) * 2014-10-28 2023-12-21 Henkel Ag & Co. Kgaa Detergents with mannosylerythritol lipid, enhancing the cleaning performance of detergents through mannosylerythritol lipid, and washing processes using mannosylerythritol lipid
GB201505287D0 (en) 2015-03-27 2015-05-13 Bangor University And Croda Internat Plc Method of seperating Mannosylerythitol Lipids
AR105805A1 (en) * 2015-08-28 2017-11-08 Unilever Nv IMPROVED WASH COMPOSITIONS
MX2018007252A (en) * 2015-12-17 2018-09-28 Proklean Tech Pvt Ltd Biodegradable detergent composition.
US20250075152A1 (en) * 2021-02-12 2025-03-06 Novozymes A/S Stabilized biological detergents
AU2022255803A1 (en) 2021-04-06 2023-10-26 LignoSol IP Limited Lignin-based compositions and related cleaning methods
US12600896B2 (en) 2021-04-06 2026-04-14 LignoSol IP Limited Lignin-based compositions and related hydrocarbon recovery methods
WO2022214954A1 (en) 2021-04-06 2022-10-13 LignoSol IP Limited Lignin-based drilling fluids and related methods
US12275894B2 (en) 2021-04-06 2025-04-15 LignoSol IP Limited Lignin-based fracturing fluids and related methods
JP2024514838A (en) * 2021-04-06 2024-04-03 リグノソル・アイピー・リミテッド Lignin-based compositions and related methods
MX2023011899A (en) 2021-04-06 2024-05-06 Lignosol Ip Ltd Lignin-based diluent and related methods.
AU2022338142A1 (en) * 2021-08-30 2024-03-07 Locus Solutions Ipco, Llc Compositions for improving the environmental impact of printing and dyeing
EP4405450B1 (en) * 2021-09-20 2025-01-29 Unilever IP Holdings B.V. Detergent composition
EP4621035A1 (en) 2024-03-18 2025-09-24 Borregaard AS Lignin-based soil release agent

Family Cites Families (18)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
AU556758B2 (en) 1981-07-13 1986-11-20 Procter & Gamble Company, The Foaming compositions based on alkylpolysaccharide
JPS6356289A (en) 1986-07-30 1988-03-10 Res Dev Corp Of Japan Beta-mannanase and production thereof
JPS6336775A (en) 1986-07-31 1988-02-17 Res Dev Corp Of Japan Novel alkalophilic strain of bacillus genus capable of producing beta-mannanase and beta-mannosidase and use thereof
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
GB8803036D0 (en) 1988-02-10 1988-03-09 Unilever Plc Liquid detergents
GB8813978D0 (en) 1988-06-13 1988-07-20 Unilever Plc Liquid detergents
JPH0347076A (en) 1989-08-25 1991-02-28 Res Dev Corp Of Japan Beta-mannase and production thereof
KR100236540B1 (en) 1990-04-14 2000-01-15 레클로우크스 라우에르 Alkaline bacillus lipases, coding dna sequences thereof and bacilli which produce these lipases
WO1991018974A1 (en) 1990-05-29 1991-12-12 Chemgen Corporation HEMICELLULASE ACTIVE AT EXTREMES OF pH AND TEMPERATURE AND THE MEANS FOR THE PRODUCTION THEREOF
JP2626662B2 (en) 1991-10-09 1997-07-02 科学技術振興事業団 Novel β-mannanase and method for producing the same
KR950702240A (en) 1993-04-27 1995-06-19 한스 발터 라벤 New lipase variant for use as a detergent
JP2859520B2 (en) 1993-08-30 1999-02-17 ノボ ノルディスク アクティーゼルスカブ Lipase, microorganism producing the same, method for producing lipase, and detergent composition containing lipase
JPH08228778A (en) 1995-02-27 1996-09-10 Showa Denko Kk Novel lipase gene and method for producing lipase using the same
DE69628656D1 (en) 1995-09-20 2003-07-17 Genencor Int MANNASE OF BACILLUS AMYLOLIQUEFACIENS AND METHOD FOR YOUR PREPARATION
BRPI9911086B1 (en) 1998-06-10 2016-08-02 Novozymes As cleaning composition, process for treating machine tissues, and use of a mannanase
GB9913551D0 (en) * 1999-06-10 1999-08-11 Unilever Plc Cleaning compositions
US6689737B2 (en) * 2002-01-17 2004-02-10 The Procter & Gamble Company Household cleaning and/or laundry detergent compositions comprising lignin-derived materials
MX2011003032A (en) * 2008-09-19 2011-04-12 Procter & Gamble Modified lignin biopolymer useful in cleaning compositions.

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO2013037643A1 *

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CN103946359A (en) 2014-07-23
EP2756063B1 (en) 2017-10-04
AR087847A1 (en) 2014-04-23
ZA201401260B (en) 2016-05-25
WO2013037643A1 (en) 2013-03-21
CL2014000636A1 (en) 2014-08-22

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