EP2596089B1 - Compositions détergentes comprenant un biosurfactant et une lipase - Google Patents

Compositions détergentes comprenant un biosurfactant et une lipase Download PDF

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Publication number
EP2596089B1
EP2596089B1 EP11729626.9A EP11729626A EP2596089B1 EP 2596089 B1 EP2596089 B1 EP 2596089B1 EP 11729626 A EP11729626 A EP 11729626A EP 2596089 B1 EP2596089 B1 EP 2596089B1
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EP
European Patent Office
Prior art keywords
biosurfactant
enzyme
lipase
cleaning
bacterial
Prior art date
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EP11729626.9A
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German (de)
English (en)
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EP2596089A1 (fr
Inventor
Alyn James Parry
Neil James Parry
Anne Cynthia Peilow
Paul Simon Stevenson
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Unilever PLC
Unilever NV
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Unilever PLC
Unilever NV
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Priority to EP11729626.9A priority Critical patent/EP2596089B1/fr
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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
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • 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
    • C11D1/04—Carboxylic acids or salts thereof
    • C11D1/06—Ether- or thioether carboxylic acids

Definitions

  • This invention relates to detergent compositions comprising biosurfactant and lipase.
  • Enzymes have been used in detergent formulations as a cleaning aid for many years. They may be derived from bacterial of other sources. The most commonly employed enzymes are proteases, amylases, mannanases, lipases and cellulases. They are often derived from fungal or yeast cultures.
  • Lipases are used in surfactant containing detergent formulations to aid the cleaning of oily soils from fabrics. Despite their isolation and characterisation some decades ago, these enzymes have been difficult to formulate in conventional surfactant formulations because there is a competition between the enzyme and the surfactant for the target substrate oil. Surfactants will win this competition for the surface and will out-compete or displace enzymes from the oily surface and therefore reduce the enzyme performance on those soils. Thus, the practical impact of lipases in detergent cleaning products is limited, especially when compared to the impact of other cleaning enzymes, such as proteases and amylases.
  • JP5168489A describes a method of making a biosurfactant using a lipase enzyme.
  • the biosurfactant that is present in combination with the lipase does not have any acid moieties.
  • the presence of a disaccharide moiety is optional.
  • US2006106120 describes a mixture of microorganism, biosurfactant and a plastic degrading enzyme for the bioremediation of man-made materials.
  • the biosurfactant may be derived from bacterial or other sources; the preferred enzyme used in the examples is a cutinase of bacterial origin. It may be co expressed with amylase and hydrophobin. The compositions are not used for cleaning.
  • CN101126052 describes a biosurfactant containing cleaning composition that also contains a protease.
  • the origin of the protease is a pineapple plant.
  • US5417879 (Unilever) describes synergistic dual surfactant laundry composition containing sophorolipid (from yeast), cellobiose lipid (from fungus) or rhamnolipid (from bacteria) glycolipid biosurfactant. Examples using these biosurfactants did not comprise any enzyme. In column 12 lines 24 to 25, it is mentioned as possible to combine the biosurfactants with an undisclosed amount of enzyme of undisclosed origin.
  • US2004171512A (Igarashi Keisuke ; Hirata Yoshihiko ; Furuta Taro ) discloses low-foaming detergent compositions comprising a biosurfactant (sophorolipid from yeast) which can replace a conventional low foaming block polymer nonionic surfactant.
  • the biosurfactant may be used with an undisclosed type of enzyme selected from amylase, protease, cellulose, lipase, pullulanase, isopullulanase, isoamylase, catalase, peroxidase, or the like.
  • the enzyme can be added by selecting appropriately in light of its substrate specificity.
  • protease may be selected for a protein stain
  • amylase may be selected for a starch stain.
  • sophorolipids for dishwashing (hard surface cleaning) in combination with Savinase 6.0T a protease from Novo Nordisk and Duramyl 60T a starch lytic enzyme (amylase) from Novo Nordisk.
  • Duramyl is produced from Bacillus Licheniformis and Savinase is produced from Bacillus Clausi / lentus, both bacterial sources. These are not taught to be generically preferred sources in this document.
  • US2009188055A discloses compositions comprising sulfonated estolides and other derivatives of fatty acids.
  • Table 20 provides prophetic examples of these surfactants in combination with other surfactants, including rhamnolipids. Enzymes are not included in these examples. Elsewhere in the document, it is said that the cleaning performance on greasy soils is synergistically improved with the estolides by using lipases.
  • Suitable lipase enzymes include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034 .
  • Suitable lipases include those that show a positive immunological cross-reaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescens IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano,” hereafter referred to as "Amano-P". Further suitable lipases are lipases such as M1 Lipase.RTM and Lipomax.RTM (Gist-Brocades). Highly preferred lipases are the D96L lipolytic enzyme variant of the native lipase derived from Humicola lanuginosa (a fungus) as described in U.S.
  • the Humicola lanuginosa strain DSM 4106 is used.
  • This enzyme is incorporated into the composition in accordance with the present technology at a level of from 50 LU to 8500 LU per litre wash solution.
  • the variant D96L is present at a level of from 100 LU to 7500 LU per litre of wash solution. More preferably at a level of from 150 LU to 5000 LU per litre of wash solution.
  • US2006080785A (Nero ) describes carpet cleaning by applying a cleaning composition having biosurfactants and enzymes to the carpet; and bonnet cleaning the material.
  • the enzymes are derived from Sea Kelp.
  • US2004072713A discloses an article for use in an enzymatic fabric cleaning process, said article containing one or more types of harmless micro-organisms capable of excreting enzymes useful in said fabric cleaning process.
  • the microorganism may be a bacterium, although fungal microorganisms are also exemplified.
  • the examples all express bleaching enzymes.
  • biosurfactants for example lipopolysaccharides.
  • No wash liquor or concentrate comprising a mixture of biosurfactants derived from bacteria together with enzymes derived from bacteria is actually disclosed in this document. We are confident that the concentration of biosurfactant would have been much less than 0.5 g/L.
  • a cleaning composition comprising an effective amount of surfactant system and an enzyme system characterised in that the surfactant system comprises at least 1 wt% (based on the cleaning composition) of a biosurfactant, which is a glycolipid surfactant comprising at least 20 mol% of glycolipid having both disaccharide and acid moieties and at least one lipase enzyme of bacterial origin.
  • a biosurfactant which is a glycolipid surfactant comprising at least 20 mol% of glycolipid having both disaccharide and acid moieties and at least one lipase enzyme of bacterial origin.
  • Lipases are a key enzyme for insertion into detergent compositions, especially laundry detergents, but also compositions designed to clean hard surfaces such as dishwashing compositions, that clean everyday dirt and stains effectively at reduced surfactant levels to enable concentration of the formulation.
  • biosurfactant (fungal, bacterial and yeast) in combination with two types of lipase enzyme (fungal and bacterial).
  • the bacterial enzymes consistently outperformed the fungal ones with the biosurfactants.
  • the best result comes from a combination of bacterially derived enzyme with bacterially derived biosurfactant comprising at least 80mol% of biosurfactant having disaccharide and acid moieties (di-Rhamnolipid).
  • a process for cleaning a substrate comprising the steps of immersing the substrate in water adding a composition according to any preceding claim to the water to form a wash liquor and washing the substrate characterised in that the wash cycle time is less than 60 minutes, preferably less than 30 minutes and the water temperature is less than 35 °C at all times.
  • Suitable lipases include those of bacterial origin. Chemically modified or protein engineered mutants are included. Examples of useful bacterial lipases include lipases from P . alcaligenes or P. pseudoalcaligenes ( EP 218 272 ), P . cepacia ( EP 331 376 ), P . stutzeri ( GB 1,372,034 ), P . fluorescens, Pseudomonas sp. strain SD 705 ( WO 95/06720 and WO 96/27002 ), P . wisconsinensis ( WO 96/12012 ), 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 ).
  • useful bacterial lipases include
  • Bacterial genes encoding bacterial lipase enzymes can be transferred to preferred expression production hosts, which are not limited to bacterial and includes for example other microbial hosts.
  • preferred expression production hosts which are not limited to bacterial and includes for example other microbial hosts.
  • bacterial lipase includes lipase produced from such expression hosts but originating from bacteria.
  • 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;
  • composition may further comprise Enzymes that are not of bacterial origin. Particularly protease, amylase and cellulase, although non-bacterial lipases could also be included.
  • Biosurfactant in this patent specification does not include surfactants derived from plant material such as Alkyl polyglucosides (APG).
  • Rhamnolipids typically from Pseudomonas sp.
  • Information about other bacterially derived biosurfactants is 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 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.
  • 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 composition is preferably a liquid and is advantageously packaged in either a multidose bottle or in a unit dose soluble pouch
  • Wash solutions were prepared by dispersing lipase at a concentration of 4mg protein per litre together with detergent surfactant at the required concentration in phosphate buffered saline (PBS) adjusted to pH 8 and 12° FH water hardness. 10 mls of the wash solution were mixed in 25 ml plastic vials at 37°C with agitation at 200 rpm in an orbital incubator for 30 minutes. Swatches (approximately 1 cm 2 ) of cotton cloth stained with Sudan Red coloured Beef fat were then added and the vials returned to the shaking incubator. Swatches were removed at timed intervals, rinsed in cold water and dried at 37°C. The residual colour was monitored using a Macbeth Colour Eye, and compared with untreated stained cloths. Results are shown in Table 1 for 30 minutes and Table 2 for 4 hours.
  • Bacterial enzyme is "Lipomax", a bacterially derived Lipase 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).
  • Fungal enzyme is "Lipolase”, derived from Humicola languginosa as described in EP 0 258 068 and available from NovoZymes A/S.
  • the bacterial lipase enzyme consistently outperforms the fungal lipase enzyme across all stain types. For the Sophorolipids at higher concentration and long wash times the presence of the fungal lipase enzyme provides no benefit over using the surfactant without a lipase.
  • the enzymes were all dosed at the same level by determining the amount of active enzyme protein in each of the samples by use of a standard BCA protein Assay kit (ex Pierce) following the manufacturer's protocol.
  • Example 2 The same experimentation was carried out as in Example 1 except the rhamnolipid material was separated into its mono-rhamnolipid and di-rhamnolipid components.
  • the di rhamnolipid having two rhamnose sugars on the acyl group.
  • R1 for the mono rhamnolipid
  • R2 for the di-rhamnolipid material.
  • the cleaning results for 1 hour and 4 hours are given in Tables 3 and 4.

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

Claims (6)

  1. Composition de nettoyage comprenant une quantité efficace de système tensioactif et un système d'enzyme caractérisée en ce que le système tensioactif comprend au moins 1 % en poids (rapporté à la composition de nettoyage) d'un biotensioactif, qui est un tensioactif de glycolipide, comprenant au moins 20 % en mol de glycolipide présentant à la fois des moitiés disaccharide et acide et au moins une enzyme de lipase d'origine bactérienne.
  2. Composition selon la revendication 1, dans laquelle le biotensioactif est choisi parmi des rhamnolipides, des sophorolipides et des mélanges de ceux-ci.
  3. Composition selon la revendication 1, dans laquelle le biotensioactif est d'origine bactérienne.
  4. Composition selon l'une quelconque des revendications précédentes, dans laquelle le biotensioactif est un rhamnolipide.
  5. Composition selon la revendication 4, dans laquelle le rhamnolipide comprend deux ou plusieurs unités rhamnose sur la chaîne acyle et est constitué d'au moins 60 % de di-rhamnolipide.
  6. Procédé pour le nettoyage d'un substrat comprenant les étapes d'immersion du substrat dans de l'eau, d'addition d'une composition selon l'une quelconque des revendications précédentes à l'eau pour former une liqueur de lavage et de lavage du substrat, caractérisé en ce que la durée de cycle de lavage est inférieure à 60 min, de préférence inférieure à 30 minutes et la température de l'eau est inférieure à 35°C à tout instant.
EP11729626.9A 2010-07-22 2011-07-04 Compositions détergentes comprenant un biosurfactant et une lipase Active EP2596089B1 (fr)

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Application Number Priority Date Filing Date Title
EP11729626.9A EP2596089B1 (fr) 2010-07-22 2011-07-04 Compositions détergentes comprenant un biosurfactant et une lipase

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
EP10170404 2010-07-22
EP11729626.9A EP2596089B1 (fr) 2010-07-22 2011-07-04 Compositions détergentes comprenant un biosurfactant et une lipase
PCT/EP2011/061216 WO2012010407A1 (fr) 2010-07-22 2011-07-04 Compositions de détergent comprenant un biosurfactant et une lipase

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EP2596089A1 EP2596089A1 (fr) 2013-05-29
EP2596089B1 true EP2596089B1 (fr) 2014-12-17

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EP (1) EP2596089B1 (fr)
CN (1) CN103052703A (fr)
BR (1) BR112013000114B1 (fr)
ES (1) ES2532537T3 (fr)
WO (1) WO2012010407A1 (fr)
ZA (1) ZA201300376B (fr)

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CN105992814A (zh) * 2013-12-19 2016-10-05 荷兰联合利华有限公司 组合物
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
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CN104876405A (zh) * 2015-04-21 2015-09-02 南开大学 一种清洗老化油泥的清洗方法
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WO2018049182A2 (fr) 2016-09-08 2018-03-15 Locus Solutions, Llc Systèmes distribués pour la production et l'utilisation efficaces de compositions à base de microbes
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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US10017710B2 (en) 2015-03-27 2018-07-10 Croda International Plc Method of separating mannosylerythritol lipids

Also Published As

Publication number Publication date
BR112013000114B1 (pt) 2020-12-29
EP2596089A1 (fr) 2013-05-29
WO2012010407A1 (fr) 2012-01-26
CN103052703A (zh) 2013-04-17
ZA201300376B (en) 2014-03-26
ES2532537T3 (es) 2015-03-27
BR112013000114A2 (pt) 2017-05-30

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