EP2596088B1 - Waschmittelzusammensetzungen mit einem biotensid und enzym - Google Patents

Waschmittelzusammensetzungen mit einem biotensid und enzym Download PDF

Info

Publication number
EP2596088B1
EP2596088B1 EP11729310.0A EP11729310A EP2596088B1 EP 2596088 B1 EP2596088 B1 EP 2596088B1 EP 11729310 A EP11729310 A EP 11729310A EP 2596088 B1 EP2596088 B1 EP 2596088B1
Authority
EP
European Patent Office
Prior art keywords
enzyme
biosurfactant
enzymes
cleaning
bacterial
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.)
Active
Application number
EP11729310.0A
Other languages
English (en)
French (fr)
Other versions
EP2596088A1 (de
Inventor
Alyn James Parry
Neil James Parry
Anne Cynthia Peilow
Paul Simon Stevenson
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 EP11729310.0A priority Critical patent/EP2596088B1/de
Publication of EP2596088A1 publication Critical patent/EP2596088A1/de
Application granted granted Critical
Publication of EP2596088B1 publication Critical patent/EP2596088B1/de
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/38Products with no well-defined composition, e.g. natural products
    • C11D3/386Preparations containing enzymes, e.g. protease or amylase
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02Anionic compounds
    • C11D1/04Carboxylic acids or salts thereof
    • C11D1/06Ether- or thioether carboxylic acids
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/38Products with no well-defined composition, e.g. natural products
    • C11D3/386Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38627Preparations containing enzymes, e.g. protease or amylase containing lipase
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/38Products with no well-defined composition, e.g. natural products
    • C11D3/386Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/38Products with no well-defined composition, e.g. natural products
    • C11D3/386Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38654Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase

Definitions

  • This invention relates to detergent compositions comprising biosurfactant and enzyme.
  • 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.
  • DE10 2008 038479 A1 discloses potential mixtures of alpha amylase enzyme that may be bacterially derived with surfactants that may be biosurfactants and may be produced from bacteria.
  • WO2006/031554A2 discloses as one of its examples a mixture of a bacterially derived protease with the biosurfactant surfactin. No importance appears to be attached to bacterially derived enzymes, moist of the cited enzymes are derived from fungi.
  • 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.
  • 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 and are thus not bacterially derived.
  • 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 Clausii / 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.
  • 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 of bacterial origin and at least one enzyme of bacterial origin selected from the group comprising: cellulases, lipases, esterases, peroxidases/oxidases, oxidoreductases, pectases, lyases, mannanases and mixtures thereof characterised in that the biosurfactant is a 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.
  • 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 best result comes from a combination of bacterially derived enzyme with bacterially derived biosurfactant (Rhamnolipid).
  • Bacterial enzymes for use in the invention are cellulases, lipases, 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.
  • biosurfactant in this patent specification does not include surfactants derived from plant material, such as Alkyl polyglucosides (APG).
  • APG Alkyl polyglucosides
  • 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 enzyme consistently outperforms the fungal enzyme across all stain types. For the Sophorolipids the presence of the fungal enzyme provides no benefit over the surfactant used without any enzyme.
  • 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.

Landscapes

  • 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 (5)

  1. Eine Reinigungszusammensetzung, umfassend eine wirksame Menge von Tensidsystem und eines Enzymsystems, dadurch gekennzeichnet, dass das Tensidsystem mindestens 1 Gew.-% (bezogen auf die Reinigungszusammensetzung) eines Biotensids bakteriellen Ursprungs und mindestens ein Enzym bakteriellen Ursprungs, ausgewählt aus der Cellulasen, Lipasen, Esterasen, Peroxidasen/Oxidasen, Oxidoreduktasen, Pectasen, Lyasen, Mannanasen und Mischungen davon umfassenden Gruppe, umfasst, dadurch gekennzeichnet, dass das Biotensid ein Rhamnolipid ist.
  2. Zusammensetzung, wie in Anspruch 1 beansprucht, worin das Enzym aus der aus Lipase, Cellulase, Mannanase, Esterase, Oxidoreductase und Mischungen davon bestehenden Gruppe ausgewählt ist.
  3. Zusammensetzung nach Anspruch 2, worin das Enzym Lipase und/oder Esterase, vorzugsweise Lipase, umfasst.
  4. Zusammensetzung nach irgendeinem vorhergehenden Anspruch, worin das Rhamnolipid zwei oder mehr Rhamnose-Einheiten auf der Acylkette umfasst, vorzugsweise mindestens 60% Dirhamnolipid.
  5. Verfahren zum Reinigen eines Substrats, umfassend die Schritte des Eintauchens des Substrats in Wasser, Zugeben einer Zusammensetzung gemäß irgendeinem vorhergehenden Anspruch zu dem Wasser, um eine Waschflotte zu bilden, und Waschen des Substrats, dadurch gekennzeichnet, dass die Waschzykluszeit weniger als 60 Minuten, vorzugsweise weniger als 30 Minuten, und die Wassertemperatur zu allen Zeiten weniger als 35°C beträgt.
EP11729310.0A 2010-07-22 2011-07-04 Waschmittelzusammensetzungen mit einem biotensid und enzym Active EP2596088B1 (de)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP11729310.0A EP2596088B1 (de) 2010-07-22 2011-07-04 Waschmittelzusammensetzungen mit einem biotensid und enzym

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
EP10170401 2010-07-22
EP11729310.0A EP2596088B1 (de) 2010-07-22 2011-07-04 Waschmittelzusammensetzungen mit einem biotensid und enzym
PCT/EP2011/061210 WO2012010405A1 (en) 2010-07-22 2011-07-04 Detergent compositions comprising biosurfactant and enzyme

Publications (2)

Publication Number Publication Date
EP2596088A1 EP2596088A1 (de) 2013-05-29
EP2596088B1 true EP2596088B1 (de) 2016-09-28

Family

ID=43307425

Family Applications (1)

Application Number Title Priority Date Filing Date
EP11729310.0A Active EP2596088B1 (de) 2010-07-22 2011-07-04 Waschmittelzusammensetzungen mit einem biotensid und enzym

Country Status (6)

Country Link
EP (1) EP2596088B1 (de)
CN (1) CN103025856B (de)
BR (1) BR112013000110B1 (de)
ES (1) ES2609023T3 (de)
WO (1) WO2012010405A1 (de)
ZA (1) ZA201300378B (de)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2024002738A1 (en) * 2022-06-28 2024-01-04 Evonik Operations Gmbh Composition comprising biosurfactant and persicomycin

Families Citing this family (18)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN104222158A (zh) * 2013-06-19 2014-12-24 深圳市绿微康生物工程有限公司 生物菌群去除剂
CN103773623B (zh) * 2014-02-25 2017-05-17 衢州华宇科技有限公司 一种复合酶洗涤剂及其制备方法和用途
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
DE102014225789A1 (de) 2014-12-15 2016-06-16 Henkel Ag & Co. Kgaa Wasch- und Reinigungsmittel
GB201505287D0 (en) 2015-03-27 2015-05-13 Bangor University And Croda Internat Plc Method of seperating Mannosylerythitol Lipids
US20160362632A1 (en) * 2015-06-15 2016-12-15 Henkel Ag & Co. Kgaa Flavolipids as surfactants in cleansing compositions
AR105803A1 (es) * 2015-08-28 2017-11-08 Unilever Nv Composiciones de lavado mejoradas
DE102016216539A1 (de) 2016-09-01 2018-03-01 Henkel Ag & Co. Kgaa Waschmittel mit Saponin
CN106591013A (zh) * 2016-11-30 2017-04-26 大连百奥泰科技有限公司 一种生物洗涤剂组合物
CN106987452A (zh) * 2017-03-19 2017-07-28 长沙协浩吉生物工程有限公司 一种外墙瓷砖酵素清洗液的配制方法
DE102017214265A1 (de) 2017-08-16 2019-02-21 Henkel Ag & Co. Kgaa Rhamnolipidhaltige Wasch- und Reinigungsmittel
CN108219677A (zh) * 2017-12-06 2018-06-29 王建东 一种餐具催干剂及其制备方法
CN113667547A (zh) * 2021-08-27 2021-11-19 广州市爱家有方日用品有限公司 一种可食用清洁乳液及其制备方法、应用
DE102021214680A1 (de) 2021-12-20 2023-06-22 Henkel Ag & Co. Kgaa Neue Tensidkombination und Wasch- und Reinigungsmittel, welche diese enthalten
EP4234671A1 (de) * 2022-02-24 2023-08-30 Evonik Operations GmbH Zusammensetzungen mit biotensiden und einer lipase aus stachybotrys chlorohalonata
EP4234664A1 (de) 2022-02-24 2023-08-30 Evonik Operations GmbH Zusammensetzung mit glucolipiden und enzymen
DE102022210879A1 (de) 2022-10-14 2024-04-25 Henkel Ag & Co. Kgaa Tensidmischungen
CN115895795A (zh) * 2022-12-26 2023-04-04 媞颂日化用品(广州)有限公司 一种含生物表面活性剂的清洁组合物及其制备方法和应用

Family Cites Families (22)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
GB2094826B (en) * 1981-03-05 1985-06-12 Kao Corp Cellulase enzyme detergent composition
JPS6356289A (ja) 1986-07-30 1988-03-10 Res Dev Corp Of Japan β−マンナナ−ゼおよびその製法
JPS6336775A (ja) 1986-07-31 1988-02-17 Res Dev Corp Of Japan β―マンナナーゼおよびβ―マンノシダーゼ生産能を有するアルカリ性バチルス属新菌株
US4810414A (en) 1986-08-29 1989-03-07 Novo Industri A/S Enzymatic detergent additive
JPH0347076A (ja) 1989-08-25 1991-02-28 Res Dev Corp Of Japan β―マンナナーゼおよびその製法
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
GB9102945D0 (en) 1991-02-12 1991-03-27 Unilever Plc Detergent composition
JP2626662B2 (ja) 1991-10-09 1997-07-02 科学技術振興事業団 新規なβ−マンナナーゼとその製造方法
DK0652946T3 (da) 1993-04-27 2005-05-30 Genencor Int Nye lipase-varianter til anvendelse i detergenter
DE69434962T2 (de) 1993-10-14 2008-01-17 The Procter & Gamble Company, Cincinnati Proteasehaltige reinigungsmittel
JPH11514856A (ja) 1995-09-20 1999-12-21 ジェネンコア インターナショナル インコーポレーテッド バチルスアミロリケファシエンスからの精製マンナーゼおよびその調製方法
EP1086211B1 (de) 1998-06-10 2011-10-12 Novozymes A/S Neuartige mannasen
JP2003013093A (ja) 2001-06-27 2003-01-15 Saraya Kk 低泡性洗浄剤組成物
BR0311200A (pt) 2002-05-23 2005-02-22 Unilever Nv Artigo para uso em um processo enzimático de limpeza de tecido, kit de partes e método para limpeza de tecido
JP4273504B2 (ja) 2002-10-23 2009-06-03 株式会社 東北テクノアーチ プラスチックの分解法及びそれを利用した有用物質の製造方法
CN102919273B (zh) * 2004-09-10 2016-03-16 诺维信北美公司 防止、去除、减少或破坏生物膜的方法
US7300913B2 (en) 2004-10-15 2007-11-27 Naturell Clean, Inc. Systems and methods for cleaning materials
US7291585B2 (en) * 2004-10-15 2007-11-06 Naturell Clean, Inc. Systems and methods for spot cleaning materials
CN101126052A (zh) 2007-08-16 2008-02-20 王锦容 环保洗净液
US7666828B2 (en) 2008-01-22 2010-02-23 Stepan Company Sulfonated estolides and other derivatives of fatty acids, methods of making them, and compositions and processes employing them
DE102008038479A1 (de) 2008-08-20 2010-02-25 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2024002738A1 (en) * 2022-06-28 2024-01-04 Evonik Operations Gmbh Composition comprising biosurfactant and persicomycin

Also Published As

Publication number Publication date
ES2609023T3 (es) 2017-04-18
ZA201300378B (en) 2015-02-25
BR112013000110A2 (pt) 2017-05-30
CN103025856B (zh) 2017-04-12
EP2596088A1 (de) 2013-05-29
WO2012010405A1 (en) 2012-01-26
BR112013000110B1 (pt) 2021-05-11
CN103025856A (zh) 2013-04-03

Similar Documents

Publication Publication Date Title
EP2596088B1 (de) Waschmittelzusammensetzungen mit einem biotensid und enzym
EP2596089B1 (de) Waschmittelzusammensetzungen mit einem Biotensid und Lipase
EP2596087B1 (de) Kombinationen aus rhamnolipiden und enzymen für verbesserte reinigung
EP3341459B1 (de) Waschmittel zusammensetzungen mit einer lipase und einem biotensid
US7183248B2 (en) Enzymatic cleaner having high pH stability
US8628765B2 (en) Bacteria cultures and compositions comprising bacteria cultures
EP2756063B1 (de) Waschmittelzusammensetzungen mit tensiden und enzymen
WO1988009367A1 (en) Cutinase cleaning composition
CA2010986A1 (en) Unique microbial lipases with activity at high temperatures and phs suitable for use in detergents
EP3158044B1 (de) Enzymbehandlungszusammensetzung
EP2935549B1 (de) Verfahren zur fett- und/oder ölfleckenentfernung
US4981611A (en) Cutinase cleaning compositions

Legal Events

Date Code Title Description
PUAI Public reference made under article 153(3) epc to a published international application that has entered the european phase

Free format text: ORIGINAL CODE: 0009012

17P Request for examination filed

Effective date: 20130116

AK Designated contracting states

Kind code of ref document: A1

Designated state(s): AL AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO RS SE SI SK SM TR

DAX Request for extension of the european patent (deleted)
GRAP Despatch of communication of intention to grant a patent

Free format text: ORIGINAL CODE: EPIDOSNIGR1

INTG Intention to grant announced

Effective date: 20160429

GRAS Grant fee paid

Free format text: ORIGINAL CODE: EPIDOSNIGR3

GRAA (expected) grant

Free format text: ORIGINAL CODE: 0009210

AK Designated contracting states

Kind code of ref document: B1

Designated state(s): AL AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO RS SE SI SK SM TR

REG Reference to a national code

Ref country code: GB

Ref legal event code: FG4D

REG Reference to a national code

Ref country code: CH

Ref legal event code: EP

REG Reference to a national code

Ref country code: AT

Ref legal event code: REF

Ref document number: 832769

Country of ref document: AT

Kind code of ref document: T

Effective date: 20161015

REG Reference to a national code

Ref country code: IE

Ref legal event code: FG4D

REG Reference to a national code

Ref country code: DE

Ref legal event code: R096

Ref document number: 602011030751

Country of ref document: DE

REG Reference to a national code

Ref country code: LT

Ref legal event code: MG4D

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: LT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: NO

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20161228

Ref country code: HR

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: RS

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: FI

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

REG Reference to a national code

Ref country code: NL

Ref legal event code: MP

Effective date: 20160928

REG Reference to a national code

Ref country code: AT

Ref legal event code: MK05

Ref document number: 832769

Country of ref document: AT

Kind code of ref document: T

Effective date: 20160928

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: LV

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: NL

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: SE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: GR

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20161229

REG Reference to a national code

Ref country code: ES

Ref legal event code: FG2A

Ref document number: 2609023

Country of ref document: ES

Kind code of ref document: T3

Effective date: 20170418

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: EE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: RO

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: PL

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: SK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: SM

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: BE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: PT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20170130

Ref country code: BG

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20161228

Ref country code: CZ

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: AT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: IS

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20170128

REG Reference to a national code

Ref country code: DE

Ref legal event code: R097

Ref document number: 602011030751

Country of ref document: DE

REG Reference to a national code

Ref country code: FR

Ref legal event code: PLFP

Year of fee payment: 7

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: DK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

PLBE No opposition filed within time limit

Free format text: ORIGINAL CODE: 0009261

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: NO OPPOSITION FILED WITHIN TIME LIMIT

26N No opposition filed

Effective date: 20170629

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: SI

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

REG Reference to a national code

Ref country code: CH

Ref legal event code: PL

REG Reference to a national code

Ref country code: IE

Ref legal event code: MM4A

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: LI

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20170731

Ref country code: IE

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20170704

Ref country code: CH

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20170731

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: LU

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20170704

REG Reference to a national code

Ref country code: FR

Ref legal event code: PLFP

Year of fee payment: 8

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: MT

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20170704

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: AL

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: MC

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

Ref country code: HU

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT; INVALID AB INITIO

Effective date: 20110704

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: CY

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20160928

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: MK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20160928

REG Reference to a national code

Ref country code: DE

Ref legal event code: R081

Ref document number: 602011030751

Country of ref document: DE

Owner name: UNILEVER GLOBAL IP LIMITED, WIRRAL, GB

Free format text: FORMER OWNER: UNILEVER N.V., ROTTERDAM, NL

REG Reference to a national code

Ref country code: ES

Ref legal event code: PC2A

Owner name: UNILEVER IP HOLDINGS B.V.

Effective date: 20211228

REG Reference to a national code

Ref country code: GB

Ref legal event code: 732E

Free format text: REGISTERED BETWEEN 20220127 AND 20220202

P01 Opt-out of the competence of the unified patent court (upc) registered

Effective date: 20230428

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: TR

Payment date: 20230626

Year of fee payment: 13

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: IT

Payment date: 20230719

Year of fee payment: 13

Ref country code: GB

Payment date: 20230720

Year of fee payment: 13

Ref country code: ES

Payment date: 20230926

Year of fee payment: 13

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: FR

Payment date: 20230725

Year of fee payment: 13

Ref country code: DE

Payment date: 20230719

Year of fee payment: 13