WO2012010406A1 - Combinations of rhamnolipids and enzymes for improved cleaning - Google Patents

Combinations of rhamnolipids and enzymes for improved cleaning Download PDF

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Publication number
WO2012010406A1
WO2012010406A1 PCT/EP2011/061214 EP2011061214W WO2012010406A1 WO 2012010406 A1 WO2012010406 A1 WO 2012010406A1 EP 2011061214 W EP2011061214 W EP 2011061214W WO 2012010406 A1 WO2012010406 A1 WO 2012010406A1
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WIPO (PCT)
Prior art keywords
rhamnolipids
rhamnolipid
composition according
rha
less
Prior art date
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PCT/EP2011/061214
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English (en)
French (fr)
Inventor
Alyn James Parry
Neil James Parry
Anne Cynthia Peilow
Paul Simon Stevenson
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Unilever Plc
Unilever N.V.
Hindustan Unilever Limited
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Application filed by Unilever Plc, Unilever N.V., Hindustan Unilever Limited filed Critical Unilever Plc
Priority to CN2011800357973A priority Critical patent/CN103052704A/zh
Priority to EP11728878.7A priority patent/EP2596087B1/de
Priority to BR112013000108-9A priority patent/BR112013000108B1/pt
Priority to ES11728878.7T priority patent/ES2561553T3/es
Publication of WO2012010406A1 publication Critical patent/WO2012010406A1/en
Priority to ZA2013/00377A priority patent/ZA201300377B/en

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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
    • C11D1/00Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02Anionic compounds
    • C11D1/37Mixtures of compounds all of which are anionic
    • 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
    • C11D3/0005Other compounding ingredients characterised by their effect
    • C11D3/0036Soil deposition preventing compositions; Antiredeposition agents
    • 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
    • C11D3/37Polymers
    • C11D3/3703Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3715Polyesters or polycarbonates
    • 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
    • C11D1/00Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02Anionic compounds
    • C11D1/12Sulfonic acids or sulfuric acid esters; Salts thereof
    • C11D1/22Sulfonic acids or sulfuric acid esters; Salts thereof derived from aromatic compounds
    • 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
    • C11D2111/00Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10Objects to be cleaned
    • C11D2111/12Soft surfaces, e.g. textile

Definitions

  • This invention relates to cleaning compositions comprising mono-rhamnolipids in combination with enzymes.
  • Rhamnolipids are a class of glycolipid. They are constructed of rhamnose combined with beta- hydroxy fatty acids. Rhamnose is a sugar. Fatty acids are ubiquitous in animals and plants. The carboxyl end of the fatty acid end is connected to the rhamnose. Rhamnolipids are compounds of only three common elements; carbon, hydrogen, and oxygen. They are a crystalline acid.
  • Rhamnolipids may be produced by strains of the bacteria Pseudomonas aeruginosa. There are two major groups of rhamnolipids; mono-rhamnolipids and di-rhamnolipids.
  • Mono-rhamnolipids have a single rhamnose sugar ring.
  • a typical mono-rhamnolipid produced by P. aeruginosa is L-rhamnosyl- -hydroxydecanoyl- -hydroxydecanoate (RhaCi 0 Ci 0 ). It may be referred to as Rha-Ci 0 -Ci 0 , with a formula of C26H48O9.
  • Mono-rhamnolipids have a single rhamnose sugar ring.
  • the lUPAC Name is 3-[3-[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan- 2-yl]oxydecanoyloxy]decanoic acid.
  • Di-rhamnolipids have two rhamnose sugar rings.
  • a typical di-rhamnolipid is L-rhamnosyl-L- rhamnosyl- -hydroxydecanoyl- -hydroxydecanoate (Rha2Ci 0 Ci 0 ). It may be referred to as Rha- Rha-C-io-C-io, with a formula of C 3 2H5 8 0i 3 .
  • the lUPAC name is 3-[3-[4,5-dihydroxy-6-methyl-3- (3 ,4 , 5-tri hyd roxy-6-m ethyloxan-2-yl)oxyoxan-2-yl]oxyd ecanoyloxy]d ecanoic acid .
  • rhamnolipid 2 is a mono-rhamnolipid and "rhamnolipid 1 " is a di-rhamnolipid. This leads to some ambiguity in the usage or "RL1 " and “RL2” in the literature. Throughout this patent specification, we use the terms mono- and di-rhamnolipid in order to avoid this possible confusion. However, if abbreviations are used R1 is mono-rhamnolipid and R2 is di-rhamnolipid. For more information on the confusion of terminology in the prior art see the introduction to US 4814272.
  • Rha-Rha-C 8 -Cio Rha-Rha-C 8 -Ci 2: i , Rha-Rha-Ci 0 -C 8 , Rha-Rha-Ci 0 -Ci 0 , Rha-Rha-Cio-Ci 2: i , Rha-
  • Rhamnolipids produced by P. aeruginosa (unidentified as either mono- or di-rhamnolipids):
  • Rha-Cio-C ⁇ 8 Rha-C"io-C"io> Rha-Ci2-Cio
  • Rhamnolipids produced by Burkholdera pseudomallei (di-rhamnolipids only):
  • rhamnolipids are produced in various chemical formulas, each with a different HLB, it is known that rhamnolipids can be produced or mixed to have a range of foaming properties.
  • Rhamnolipids are an anionic surfactant with both hydrophilic end and a lipophilic end. When their concentration increases to a certain level it is known that the rhamnolipids join together inside a liquid in a micelle.
  • rhamnolipids with two shorter fatty acids are more active in reducing surface tension and as an emulsifier. Those rare rhamnolipids with a single fatty acid chain are not as effective.
  • the bacterium Pseudomonas aeruginosa is found naturally in soils, in water, and on plants.
  • P. aeruginosa is chemoheterotrophic, generally aerobic, utilizing a wide range of organic compounds for sources of carbon and nitrogen.
  • ATCC American Type Culture Collection
  • strains of P. aeruginosa can be isolated to produce
  • Strains can also be selected to produce less byproduct and to metabolize different feedstock or pollutants. This production is greatly affected by the environment in which the bacterium is grown.
  • US 5417879 A1 suggests a mixed micellar Glycolipid and lamellar surfactant composition, that can be either glycolipid, or not. Compositions are proposed for use at 0.5 to 50 g/l. Examples using Rhamnolipid did not use any enzyme. In column 12 lines 24 to 25, it is mentioned as possible to combine the biosurfactants with an undisclosed amount of enzyme. To arrive at a combination of enzyme with Rhamnolipid it is necessary to make several selections from this document.
  • US2006106120 describes a mixture of micro-organism, biosurfactant and a plastic degrading enzyme for the bioremediation of man-made materials.
  • the biosurfactant may be a rhamnolipid (para 62).
  • the enzyme may be a lipase (para 64). No preference is given for any components of the rhamnolipid. Neither rhamnolipids nor lipases are exemplified and rhamnolipids are not specifically claimed.
  • US2004072713A (Unilever) 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 micro-organisms are also capable of producing other chemical entities that contribute to the cleaning process, e.g. biosurfactants, for example lipopolysaccharides as described in EP924221. These biosurfactants are not Rhamnolipids. The levels of biosurfactants generated were very low indeed and certainly would not have exceeded 0.5g/l.
  • the micro-organisms are said to be capable of producing and secreting useful laundry enzymes such as Oxidoreductases, Carbohyd rases, Proteases, Lipases, Transferases and Glycosidases.
  • a detergent composition with a novel ratio of mono to di rhamnolipids in combination with lipase.
  • the amount of mono-rhamnolipid present is more than the amount of di-rhamnolipid present (if any).
  • at least 80 wt%, more preferably at least 90 wt% or even 100 wt% of the rhamnolipid in the composition is mono- Rhamnolipid.
  • the lipase is preferably derived from either fungal or bacterial sources.
  • bacterial sources we include expression from other microbes, such as yeast, of genes that have been cloned from bacteria.
  • the rhamnolipid is preferably present in an amount of from 0.5 to 40 wt%.
  • the lipase is preferably present in an amount of from 0.0001 to 5 wt%.
  • the detergent composition is preferably unbuilt. That is zeolite, phosphate or silicate builders are absent.
  • the detergent composition is preferably a liquid detergent composition and if citric acid builder is present, it is limited to a maximum level of 2 wt%.
  • the composition is especially useful as a laundry detergent and may be used with advantage for washing in water with a low water hardness of less than 15°F.
  • a process whereby the laundry and the composition are washed in presoftened water is particularly advantageously used with the compositions of the invention.
  • the compositions are used to remove fatty soils from laundry, especially from cotton cloths.
  • Using mono-rhamnolipids and lipase in a detergent composition according to the invention leads to enhanced cleaning benefits and possibly synergies with synthetic anionic surfactants, for example C12-14 alkyl benzene sulphonate synthetic anionic surfactant.
  • This surfactant is commonly employed in laundry detergent compositions and is typically used with a nonionic surfactant, such as the ethoxylated nonionic surfactant used in US5417879. For environmental reasons it is desirable to eliminate this nonionic surfactant from the composition.
  • the rhamnolipids with mono to di rhamnolipid ratio claimed provide a suitable substitute for the nonionic surfactant component, especially when used to remove fatty soils and particularly when used to remove soils from cotton cloth.
  • the compositions are suited to low wash temperatures and fast wash times, which support energy and time savings.
  • a preferred fatty soil is beef fat.
  • biosurfactants are generated by the action of bacteria on renewable feedstocks and are increasingly becoming more and more viable options as sustainable replacements of current synthetic surfactants.
  • Rhamnolipids formed by the degradation of oils and fats by
  • Pseudomonas Aeg show poor cleaning benefits when used at concentrations of components generated by the bacterial breakdown process.
  • the mono and di rhamnolipid components of the expressed rhamnolipids are extracted and the mono-rhamnolipid is used with lipase superior cleaning results.
  • by producing blends and mixing with synthetic anionic surfactants further enhancement in detergency may be achieved.
  • 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.
  • Suitable lipases for use in the compositions of the invention include those of bacterial, fungal or yeast origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa (T. lanuginosus) as described in EP 258 068 and EP 305 216 or from H. insolens as described in WO 96/13580, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P.
  • lipase variants such as those described in WO 92/05249, WO 94/01541 , EP 407 225, EP 260 105, WO 95/35381 , WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079, WO 97/07202, US2008004186, US2006205628, US5869438, US6017866, US20021 10854, US6939702, US2009221034, US200802425, US2004053360, US2005281912, US2006075518, US2005059130, US20041542180, US2003199069,
  • lipases are described and referenced but not limited to those in Juardo et al J Surfact Deterg (2007) 10: 61-70, Horchani et al J Molecular Catalysis: Enzymatic 56 (2009) 237-245, Aloulou et al Biochimica et Biophysica acta 1771 (2007) 1446-1456, Mogensen et al Biochemistry (2005) 44: 1719-1730, Nicanuzia dos Prazeres et al Brazilian J of Microbiology
  • Preferred commercially available lipase enzymes include LipolaseTM and Lipolase UltraTM, LipexTM, Novozym 525L (Novozymes A/S).
  • the composition may comprise a cutinase. classified in EC 3.1.1 .74.
  • the cutinase used according to the invention may be of any origin.
  • cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.
  • Cutinases are enzymes that are able to degrade cutin.
  • the cutinase is derived from a strain of Aspergillus, in particular Aspergillus oryzae, a strain of Alternaria, in particular Alternaria brassiciola, a strain of Fusarium, in particular Fusarium solani, Fusarium solani pisi, Fusarium roseum culmorum, or Fusarium roseum sambucium, a strain of Helminthosporum, in particular Helminthosporum sativum, a strain of Humicola, in particular Humicola insolens, a strain of Pseudomonas, in particular Pseudomonas mendocina, or
  • Rhizoctonia in particular Rhizoctonia solani
  • Rhizoctonia solani a strain of Rhizoctonia
  • Streptomyces in particular Streptomyces scabies, or a strain of Ulocladium, in particular
  • the cutinase is derived from a strain of Humicola insolens, in particular the strain Humicola insolens DSM 1800. Humicola insolens cutinase is described in WO 96/13580.
  • the cutinase may be a variant, such as one of the variants disclosed in WO 00/34450 and WO 01/92502, which are hereby incorporated by reference.
  • Preferred cutinase variants include variants listed in Example 2 of WO 01/92502, which is hereby specifically incorporated by reference.
  • esterases are those described in US2002012959, WO09085743, WO09002480, US2002137177, US2003024009, US2010151542, US2003032161 , US2002007518 and
  • Preferred commercial cutinases include NOVOZYMTM 51032 (available from Novozymes A/S, Denmark).
  • the composition may also comprise 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 which participate in the hydrolysis of phospholipids. Several types of phospholipase activity can be distinguished, including phospholipases A-i 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.
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (A-i 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-i 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 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. javanicus, M. mucedo, M. subtilissimus; Neurospora, e.g. N. crassa; Rhizomucor, e.g., R. pusillus; Rhizopus, e.g. R. arrhizus, R. japonicus, R.
  • filamentous fungi e.g., yeast or bacteria
  • Aspergillus e.g., A. niger
  • Dictyostelium e.g., D. discoideum
  • Mucor e.g. M. javanicus, M. mucedo, M. subtil
  • 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.
  • 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 Aspergillus oryzae.
  • Preferred phospholipases are derived from a strain of Humicola, especially Humicola lanuginosa.
  • the phospholipase may be a variant, such as one of the variants disclosed in WO 00/32758, which are hereby incorporated by reference.
  • Preferred phospholipase variants include variants listed in Example 5 of WO 00/32758, which is hereby specifically incorporated by reference.
  • the phospholipase is one described in WO 04/1 1 1216, especially the variants listed in the table in Example 1.
  • the phospholipase is derived from a strain of Fusarium, especially Fusarium oxysporum.
  • the phospholipase may be the one concerned in WO 98/026057 displayed in SEQ ID NO: 2 derived from Fusarium oxysporum DSM 2672, or variants thereof.
  • the phospholipase is a phospholipase A-i (EC.
  • the phospholipase is 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).
  • the composition may further comprise other enzymes enhancing the detergency of the composition such as softening agents, an amylase (e.g. Fungamyl(R) from Novo Nordisk A/S, Denmark), a lipase (e.g. Novocor(R) AD from Novo Nordisk A/S, Denmark), a cellulase (e.g. Celluzyme(R), Carezyme(R), and/or Celluclast(R), all from Novo Nordisk A/S, Denmark), a xylanase (e.g. Biofeed(R) PLUS or Shearzyme(TM) from Novo Nordisk A/S, Denmark), a beta- glucanase (e.g.
  • an amylase e.g. Fungamyl(R) from Novo Nordisk A/S, Denmark
  • a lipase e.g. Novocor(R) AD from Novo Nordisk A/S, Denmark
  • a cellulase e.g. Cell
  • a pectinase e.g. Pectinex(TM) Ultra from Novo Nordisk A/S, Denmark
  • a peroxidase e.g. Guardzyme(TM) from Novo Nordisk A/S, Denmark
  • a laccase e.g. obtained from Myceliophthora or Polyporus
  • 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 mis 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.
  • PBS phosphate buffered saline
  • Bacterial enzyme is "Lipomax", a bacterially derived Lipase variant M21 L of the lipase of
  • Fungal enzyme is "Lipolase”, derived from Humicola languginosa as described in EP 0 258 068 and available from NovoZymes A S.
  • RBR425 Rhamnolipid: a biosurfactant of bacterial origin. Commercially available from Jeneil as RBR425 (25%AM). The composition of this material was analysed and is given in Table 3 below.
  • the mobile phase water (mobile phase A) and acetonitrile (mobile phase B) were used to separate via a gradient of 60:40 (A:B) changing to 30:70 (A:B) over 30 minutes. The system was then held for 5 minutes before returning to the start conditions all at a flow rate of 0.5ml/min.
  • the injection volume was 10 ⁇ .

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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)
PCT/EP2011/061214 2010-07-22 2011-07-04 Combinations of rhamnolipids and enzymes for improved cleaning WO2012010406A1 (en)

Priority Applications (5)

Application Number Priority Date Filing Date Title
CN2011800357973A CN103052704A (zh) 2010-07-22 2011-07-04 用于提高清洁的鼠李糖脂和酶的组合物
EP11728878.7A EP2596087B1 (de) 2010-07-22 2011-07-04 Kombinationen aus rhamnolipiden und enzymen für verbesserte reinigung
BR112013000108-9A BR112013000108B1 (pt) 2010-07-22 2011-07-04 composição detergente, seus usos, e processo para a limpeza de um substrato
ES11728878.7T ES2561553T3 (es) 2010-07-22 2011-07-04 Combinaciones de ramnolípidos y enzimas para una limpieza mejorada
ZA2013/00377A ZA201300377B (en) 2010-07-22 2013-01-15 Combinations of rhamnolipids and enzymes for improved cleaning

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EP10170403 2010-07-22
EP10170403.9 2010-07-22

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WO2012010406A1 true WO2012010406A1 (en) 2012-01-26

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EP (1) EP2596087B1 (de)
CN (2) CN103052704A (de)
BR (1) BR112013000108B1 (de)
ES (1) ES2561553T3 (de)
WO (1) WO2012010406A1 (de)
ZA (1) ZA201300377B (de)

Cited By (23)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2014027249A3 (en) * 2012-05-07 2014-07-17 Rhodia Operations Aqueous coatings and paints incorporating one or more antimicrobial biosurfactants and methods for using same
EP2786743A1 (de) * 2013-04-02 2014-10-08 Evonik Industries AG Mischungszusammensetzung enthaltend Rhamnolipide
EP2787065A1 (de) * 2013-04-02 2014-10-08 Evonik Industries AG Waschmittelformulierung für Textilien enthaltend Rhamnolipide mit einem überwiegenden Gehalt an di-Rhamnolipiden
WO2015091457A1 (en) * 2013-12-19 2015-06-25 Unilever Plc Composition
WO2015091294A1 (en) * 2013-12-18 2015-06-25 Unilever Plc Mono-rhamnolipid based compositions.
WO2016055591A1 (fr) 2014-10-08 2016-04-14 Centre National De La Recherche Scientifique (Cnrs) Biosurfactants de pseudomonas pour lutter contre les legionelles
WO2016066464A1 (de) * 2014-10-28 2016-05-06 Henkel Ag & Co. Kgaa Waschmittel mit mannosylerythritollipid
DE102014225789A1 (de) 2014-12-15 2016-06-16 Henkel Ag & Co. Kgaa Wasch- und Reinigungsmittel
WO2016139032A1 (en) * 2015-03-02 2016-09-09 Unilever Plc Compositions with reduced dye-transfer properties
EP3070155A1 (de) 2015-03-18 2016-09-21 Evonik Degussa GmbH Zusammensetzung enthaltend peptidase und biotensid
WO2017036901A1 (en) * 2015-08-28 2017-03-09 Unilever Plc Improved wash compositions
US9884883B2 (en) 2015-01-12 2018-02-06 Logos Technologies, Llc Production of rhamnolipid compositions
DE102017214265A1 (de) 2017-08-16 2019-02-21 Henkel Ag & Co. Kgaa Rhamnolipidhaltige Wasch- und Reinigungsmittel
US10259837B2 (en) 2015-03-02 2019-04-16 Conopco, Inc. Method of separating rhamnolipids from a fermentation broth
WO2019154970A1 (en) * 2018-02-09 2019-08-15 Evonik Degussa Gmbh Mixture composition comprising glucolipids
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US20210204571A1 (en) * 2020-01-06 2021-07-08 Vinay Bhalchandra PARANJPE Vegetable and Fruit Wash Formulation and Uses Thereof
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WO2023099346A1 (en) * 2021-12-02 2023-06-08 Evonik Operations Gmbh Composition comprising glucolipids
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EP4353806A1 (de) 2022-10-14 2024-04-17 Henkel AG & Co. KGaA Tensidmischungen

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* Cited by examiner, † Cited by third party
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Citations (62)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1542180A (en) 1924-04-28 1925-06-16 Clarence C Selden Art of and apparatus for the treatment of plant fiber or the like
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
EP0218272A1 (de) 1985-08-09 1987-04-15 Gist-Brocades N.V. Lipolytische Enzyme und deren Anwendung in Reinigungsmitteln
EP0258068A2 (de) 1986-08-29 1988-03-02 Novo Nordisk A/S Enzymhaltiger Reinigungsmittelzusatz
EP0260105A2 (de) 1986-09-09 1988-03-16 Genencor, Inc. Herstellung von Enzymen mit geänderter Aktivität
EP0305216A1 (de) 1987-08-28 1989-03-01 Novo Nordisk A/S Rekombinante Humicola-Lipase und Verfahren zur Herstellung von rekombinanten Humicola-Lipasen
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
US4814272A (en) 1984-02-17 1989-03-21 Wintershall Ag Process for the biotechnical production of rhamnolipids including rhamnolipids with only one β-hydroxydecanoic acid residue in the molecule
EP0331376A2 (de) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. Rekombinante DNA, sie enthaltendes Bakterium der Gattung Pseudomonas und ihre Verwendung zur Herstellung von Lipase
EP0407225A1 (de) 1989-07-07 1991-01-09 Unilever Plc Enzyme und enzymhaltiges Reinigungsmittel
WO1991016422A1 (de) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Alkalische bacillus-lipasen, hierfür codierende dna-sequenzen sowie bacilli, die diese lipasen produzieren
WO1992005249A1 (en) 1990-09-13 1992-04-02 Novo Nordisk A/S Lipase variants
EP0499434A1 (de) * 1991-02-12 1992-08-19 Unilever Plc Waschmittelzusammensetzungen
WO1994001541A1 (en) 1992-07-06 1994-01-20 Novo Nordisk A/S C. antarctica lipase and lipase variants
WO1994025578A1 (en) 1993-04-27 1994-11-10 Gist-Brocades N.V. New lipase variants for use in detergent applications
WO1995006720A1 (fr) 1993-08-30 1995-03-09 Showa Denko K.K. Nouvelle lipase, micro-organisme la produisant, procede de production de cette lipase, et utilisation de ladite lipase
US5417879A (en) 1991-02-12 1995-05-23 Lever Brothers Company, Division Of Conopco, Inc. Synergistic dual-surfactant detergent composition containing sophoroselipid
WO1995014783A1 (fr) 1993-11-24 1995-06-01 Showa Denko K.K. Gene de lipase et lipase variante
WO1995022615A1 (en) 1994-02-22 1995-08-24 Novo Nordisk A/S A method of preparing a variant of a lipolytic enzyme
WO1995030744A2 (en) 1994-05-04 1995-11-16 Genencor International Inc. Lipases with improved surfactant resistance
WO1995035381A1 (en) 1994-06-20 1995-12-28 Unilever N.V. Modified pseudomonas lipases and their use
WO1996000292A1 (en) 1994-06-23 1996-01-04 Unilever N.V. Modified pseudomonas lipases and their use
WO1996012012A1 (fr) 1994-10-14 1996-04-25 Solvay S.A. Lipase, micro-organisme la produisant, procede de preparation de cette lipase et utilisation de celle-ci
WO1996013580A1 (en) 1994-10-26 1996-05-09 Novo Nordisk A/S An enzyme with lipolytic activity
WO1996027002A1 (fr) 1995-02-27 1996-09-06 Novo Nordisk A/S Nouveau gene de lipase et procede de production de lipase a l'aide de celui-ci
WO1997004079A1 (en) 1995-07-14 1997-02-06 Novo Nordisk A/S A modified enzyme with lipolytic activity
WO1997007202A1 (en) 1995-08-11 1997-02-27 Novo Nordisk A/S Novel lipolytic enzymes
WO1998016215A1 (en) 1996-10-14 1998-04-23 Scotia Holdings Plc Use of essential fatty acids for the treatment and prevention of radiation damage to erythrocytes
DE19648439A1 (de) * 1996-11-22 1998-05-28 Henkel Kgaa Verwendung von Mischungen aus Glycolipiden und Tensiden
US5767090A (en) 1996-01-17 1998-06-16 Arizona Board Of Regents, On Behalf Of The University Of Arizona Microbially produced rhamnolipids (biosurfactants) for the control of plant pathogenic zoosporic fungi
WO1998026057A1 (en) 1996-12-09 1998-06-18 Novo Nordisk A/S Reduction of phosphorus containing components in edible oils comprising a high amount of non-hydratable phosphorus by use of a phospholipase, a phospholipase from a filamentous fungus having phospholipase a and/or b activity
US5869438A (en) 1990-09-13 1999-02-09 Novo Nordisk A/S Lipase variants
EP0924221A2 (de) 1997-12-19 1999-06-23 ENITECNOLOGIE S.p.a. Neues Lipopolysaccharid als Biotensid
WO2000032758A1 (en) 1998-11-27 2000-06-08 Novozymes A/S Lipolytic enzyme variants
WO2000034450A1 (en) 1998-12-04 2000-06-15 Novozymes A/S Cutinase variants
WO2001092502A1 (en) 2000-06-02 2001-12-06 Novozymes A/S Cutinase variants
US20020007518A1 (en) 1999-08-20 2002-01-24 Kellis James T. Enzymatic modification of the surface of a polyester fiber or article
US20020012959A1 (en) 1998-01-23 2002-01-31 Jones J. Bryan Chemically modified mutant enzymes and methods for producing them, and screening them for amidase and/or esterase activity
US20020110854A1 (en) 2000-06-26 2002-08-15 Novozymes A/S Lipolytic enzymes
US20020137177A1 (en) 1998-01-23 2002-09-26 Jones J. Bryan Modified enzymes and their use for peptide synthesis
US20030024009A1 (en) 2000-11-17 2003-01-30 Nigel Dunn-Coleman Manipulation of the phenolic acid content and digestibility of plant cell walls by targeted expression of genes encoding cell wall degrading enzymes
US20030032161A1 (en) 1996-09-30 2003-02-13 Borneman William S. Esterase enzymes, DNA encoding esterase enzymes and vectors and host cells incorporating same
US20030199069A1 (en) 1995-07-14 2003-10-23 Novozymes A/S Novel lipolytic enzymes
US20040053360A1 (en) 2001-02-07 2004-03-18 Signe Munk Lipase variants
US20040072713A1 (en) 2002-05-23 2004-04-15 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Article and process for cleaning fabrics
US20040152613A1 (en) 2003-01-28 2004-08-05 Dirk Develter Detergent compositions
WO2004111216A2 (en) 2003-06-19 2004-12-23 Novozymes A/S Phospholipase variants
US20050059130A1 (en) 1998-11-27 2005-03-17 Novozymes A/S Lipolytic enzyme variants
US6939702B1 (en) 1999-03-31 2005-09-06 Novozymes A/S Lipase variant
US20050281912A1 (en) 1999-06-02 2005-12-22 Novozymes A/S Chemically modified lipolytic enzyme
US20060075518A1 (en) 2004-09-30 2006-04-06 Novozymes, Inc. Polypeptides having lipase activity and polynucleotides encoding same
US20060080785A1 (en) 2004-10-15 2006-04-20 Nero Michael D Systems and methods for cleaning materials
US20060106120A1 (en) 2002-10-23 2006-05-18 Tohopku Techno Arch Co., Ltd. Method of degrading plastic and process for producing useful substance using the same
US20060205628A1 (en) 2003-02-18 2006-09-14 Novozymes A/S Detergent compositions
US20070167344A1 (en) 2003-12-03 2007-07-19 Amin Neelam S Enzyme for the production of long chain peracid
US20080002425A1 (en) 2006-07-03 2008-01-03 Junhon Lin Lighting Device With Fluid Wave Projection
US20080004186A1 (en) 2006-06-23 2008-01-03 Estell David A Systematic evaluation of sequence and activity relationships using site evaluation libraries for engineering multiple properties
WO2008088489A2 (en) 2006-12-22 2008-07-24 Danisco Us, Inc., Genencor Division Enzyme-assisted de-emulsification of aqueous lipid extracts
WO2009002480A2 (en) 2007-06-26 2008-12-31 Danisco Us, Inc., Genencor Division Acyl transferase having altered substrate specificity
WO2009085743A1 (en) 2007-12-20 2009-07-09 Danisco Us Inc., Genencor Division Enzymatic prevention and control of biofilm
US20090221034A1 (en) 2008-02-29 2009-09-03 Novozymes A/S Lipolytic Enzyme Variant With Improved Stability And Polynucleotides Encoding Same
US20100151542A1 (en) 2007-02-27 2010-06-17 Mcauliffe Joseph C Cleaning Enzymes and Fragrance Production

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN100419126C (zh) * 2005-06-16 2008-09-17 广州天至环保科技有限公司 一种应用于金属加工业前处理除油脱脂的生物除油剂及其处理金属表面油污的方法

Patent Citations (64)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1542180A (en) 1924-04-28 1925-06-16 Clarence C Selden Art of and apparatus for the treatment of plant fiber or the like
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
US4814272A (en) 1984-02-17 1989-03-21 Wintershall Ag Process for the biotechnical production of rhamnolipids including rhamnolipids with only one β-hydroxydecanoic acid residue in the molecule
EP0218272A1 (de) 1985-08-09 1987-04-15 Gist-Brocades N.V. Lipolytische Enzyme und deren Anwendung in Reinigungsmitteln
EP0258068A2 (de) 1986-08-29 1988-03-02 Novo Nordisk A/S Enzymhaltiger Reinigungsmittelzusatz
EP0260105A2 (de) 1986-09-09 1988-03-16 Genencor, Inc. Herstellung von Enzymen mit geänderter Aktivität
EP0305216A1 (de) 1987-08-28 1989-03-01 Novo Nordisk A/S Rekombinante Humicola-Lipase und Verfahren zur Herstellung von rekombinanten Humicola-Lipasen
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
EP0331376A2 (de) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. Rekombinante DNA, sie enthaltendes Bakterium der Gattung Pseudomonas und ihre Verwendung zur Herstellung von Lipase
EP0407225A1 (de) 1989-07-07 1991-01-09 Unilever Plc Enzyme und enzymhaltiges Reinigungsmittel
WO1991016422A1 (de) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Alkalische bacillus-lipasen, hierfür codierende dna-sequenzen sowie bacilli, die diese lipasen produzieren
WO1992005249A1 (en) 1990-09-13 1992-04-02 Novo Nordisk A/S Lipase variants
US5869438A (en) 1990-09-13 1999-02-09 Novo Nordisk A/S Lipase variants
EP0499434A1 (de) * 1991-02-12 1992-08-19 Unilever Plc Waschmittelzusammensetzungen
US5417879A (en) 1991-02-12 1995-05-23 Lever Brothers Company, Division Of Conopco, Inc. Synergistic dual-surfactant detergent composition containing sophoroselipid
WO1994001541A1 (en) 1992-07-06 1994-01-20 Novo Nordisk A/S C. antarctica lipase and lipase variants
WO1994025578A1 (en) 1993-04-27 1994-11-10 Gist-Brocades N.V. New lipase variants for use in detergent applications
WO1995006720A1 (fr) 1993-08-30 1995-03-09 Showa Denko K.K. Nouvelle lipase, micro-organisme la produisant, procede de production de cette lipase, et utilisation de ladite lipase
WO1995014783A1 (fr) 1993-11-24 1995-06-01 Showa Denko K.K. Gene de lipase et lipase variante
WO1995022615A1 (en) 1994-02-22 1995-08-24 Novo Nordisk A/S A method of preparing a variant of a lipolytic enzyme
US6017866A (en) 1994-05-04 2000-01-25 Genencor International, Inc. Lipases with improved surfactant resistance
WO1995030744A2 (en) 1994-05-04 1995-11-16 Genencor International Inc. Lipases with improved surfactant resistance
WO1995035381A1 (en) 1994-06-20 1995-12-28 Unilever N.V. Modified pseudomonas lipases and their use
WO1996000292A1 (en) 1994-06-23 1996-01-04 Unilever N.V. Modified pseudomonas lipases and their use
WO1996012012A1 (fr) 1994-10-14 1996-04-25 Solvay S.A. Lipase, micro-organisme la produisant, procede de preparation de cette lipase et utilisation de celle-ci
WO1996013580A1 (en) 1994-10-26 1996-05-09 Novo Nordisk A/S An enzyme with lipolytic activity
WO1996027002A1 (fr) 1995-02-27 1996-09-06 Novo Nordisk A/S Nouveau gene de lipase et procede de production de lipase a l'aide de celui-ci
WO1997004079A1 (en) 1995-07-14 1997-02-06 Novo Nordisk A/S A modified enzyme with lipolytic activity
US20030199069A1 (en) 1995-07-14 2003-10-23 Novozymes A/S Novel lipolytic enzymes
WO1997007202A1 (en) 1995-08-11 1997-02-27 Novo Nordisk A/S Novel lipolytic enzymes
US5767090A (en) 1996-01-17 1998-06-16 Arizona Board Of Regents, On Behalf Of The University Of Arizona Microbially produced rhamnolipids (biosurfactants) for the control of plant pathogenic zoosporic fungi
US20030032161A1 (en) 1996-09-30 2003-02-13 Borneman William S. Esterase enzymes, DNA encoding esterase enzymes and vectors and host cells incorporating same
WO1998016215A1 (en) 1996-10-14 1998-04-23 Scotia Holdings Plc Use of essential fatty acids for the treatment and prevention of radiation damage to erythrocytes
DE19648439A1 (de) * 1996-11-22 1998-05-28 Henkel Kgaa Verwendung von Mischungen aus Glycolipiden und Tensiden
WO1998026057A1 (en) 1996-12-09 1998-06-18 Novo Nordisk A/S Reduction of phosphorus containing components in edible oils comprising a high amount of non-hydratable phosphorus by use of a phospholipase, a phospholipase from a filamentous fungus having phospholipase a and/or b activity
EP0924221A2 (de) 1997-12-19 1999-06-23 ENITECNOLOGIE S.p.a. Neues Lipopolysaccharid als Biotensid
US20020012959A1 (en) 1998-01-23 2002-01-31 Jones J. Bryan Chemically modified mutant enzymes and methods for producing them, and screening them for amidase and/or esterase activity
US20020137177A1 (en) 1998-01-23 2002-09-26 Jones J. Bryan Modified enzymes and their use for peptide synthesis
WO2000032758A1 (en) 1998-11-27 2000-06-08 Novozymes A/S Lipolytic enzyme variants
US20050059130A1 (en) 1998-11-27 2005-03-17 Novozymes A/S Lipolytic enzyme variants
WO2000034450A1 (en) 1998-12-04 2000-06-15 Novozymes A/S Cutinase variants
US6939702B1 (en) 1999-03-31 2005-09-06 Novozymes A/S Lipase variant
US20050281912A1 (en) 1999-06-02 2005-12-22 Novozymes A/S Chemically modified lipolytic enzyme
US20020007518A1 (en) 1999-08-20 2002-01-24 Kellis James T. Enzymatic modification of the surface of a polyester fiber or article
WO2001092502A1 (en) 2000-06-02 2001-12-06 Novozymes A/S Cutinase variants
US20020110854A1 (en) 2000-06-26 2002-08-15 Novozymes A/S Lipolytic enzymes
US20030024009A1 (en) 2000-11-17 2003-01-30 Nigel Dunn-Coleman Manipulation of the phenolic acid content and digestibility of plant cell walls by targeted expression of genes encoding cell wall degrading enzymes
US20040053360A1 (en) 2001-02-07 2004-03-18 Signe Munk Lipase variants
US20040072713A1 (en) 2002-05-23 2004-04-15 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Article and process for cleaning fabrics
US20060106120A1 (en) 2002-10-23 2006-05-18 Tohopku Techno Arch Co., Ltd. Method of degrading plastic and process for producing useful substance using the same
US20040152613A1 (en) 2003-01-28 2004-08-05 Dirk Develter Detergent compositions
EP1445302A1 (de) 2003-01-28 2004-08-11 Ecover Belgium Reinigungsmittelzusammensetzungen
US20060205628A1 (en) 2003-02-18 2006-09-14 Novozymes A/S Detergent compositions
WO2004111216A2 (en) 2003-06-19 2004-12-23 Novozymes A/S Phospholipase variants
US20070167344A1 (en) 2003-12-03 2007-07-19 Amin Neelam S Enzyme for the production of long chain peracid
US20060075518A1 (en) 2004-09-30 2006-04-06 Novozymes, Inc. Polypeptides having lipase activity and polynucleotides encoding same
US20060080785A1 (en) 2004-10-15 2006-04-20 Nero Michael D Systems and methods for cleaning materials
US20080004186A1 (en) 2006-06-23 2008-01-03 Estell David A Systematic evaluation of sequence and activity relationships using site evaluation libraries for engineering multiple properties
US20080002425A1 (en) 2006-07-03 2008-01-03 Junhon Lin Lighting Device With Fluid Wave Projection
WO2008088489A2 (en) 2006-12-22 2008-07-24 Danisco Us, Inc., Genencor Division Enzyme-assisted de-emulsification of aqueous lipid extracts
US20100151542A1 (en) 2007-02-27 2010-06-17 Mcauliffe Joseph C Cleaning Enzymes and Fragrance Production
WO2009002480A2 (en) 2007-06-26 2008-12-31 Danisco Us, Inc., Genencor Division Acyl transferase having altered substrate specificity
WO2009085743A1 (en) 2007-12-20 2009-07-09 Danisco Us Inc., Genencor Division Enzymatic prevention and control of biofilm
US20090221034A1 (en) 2008-02-29 2009-09-03 Novozymes A/S Lipolytic Enzyme Variant With Improved Stability And Polynucleotides Encoding Same

Non-Patent Citations (15)

* Cited by examiner, † Cited by third party
Title
ALOULOU ET AL., BIOCHIMICA ET BIOPHYSICA ACTA, vol. 1771, 2007, pages 1446 - 1456
BORA, KALITA, J OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY, vol. 83, 2008, pages 688 - 693
DARTOIS ET AL., BIOCHEMICA ET BIOPHYSICA ACTA, vol. 1131, 1993, pages 253 - 360
FERNANDEZ-LORENTE ET AL., BIOTECHNOLOGY AND BIOENGINEERING, vol. 2, 1997, pages 242 - 250
GILBERT, ENZYME MICROB. TECHNOL., vol. 15, 1993, pages 634 - 645
HORCHANI ET AL., J MOLECULAR CATALYSIS: ENZYMATIC, vol. 56, 2009, pages 237 - 245
JOSHI, VINAY, RES J BIOTECH, vol. 2, no. 2, 2007, pages 50 - 56
JUARDO ET AL., J SURFACT DETERG, vol. 10, 2007, pages 61 - 70
LIU ET AL., BIOCHEMICAL ENGINEERING JOURNAL, vol. 46, 2009, pages 265 - 270
MARTINS VG ET AL.: "Lipase and biosurfactant production for utilisation in bioremediation of vegetable oils and hydrocarbon", QUIMICA NOVA, vol. 8, no. 31, 2008, pages 1942 - 1947
MATSUMIYA Y. ET AL.: "Isolation and characterisation of a lipid degrading bacterium and its application to lipid containing wastewater treatment", JOURNAL OF BIOSCIENCE AND BIOENGINEERING, vol. 4, no. 103, 2007, pages 325 - 330
MOGENSEN ET AL., BIOCHEMISTRY, vol. 44, 2005, pages 1719 - 1730
NICANUZIA DOS PRAZERES ET AL., BRAZILIAN J OF MICROBIOLOGY, vol. 37, 2006, pages 505 - 509
SAISUBRAMANIAN ET AL., APPL BIOCHEM BIOTECHNOL, vol. 150, 2008, pages 139 - 156
THIRUNAVUKARASU ET AL., PROCESS BIOCHEMISTRY, vol. 43, 2008, pages 701 - 706

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US8957129B2 (en) 2012-05-07 2015-02-17 Rhodia Operations Aqueous coatings and paints incorporating one or more antimicrobial biosurfactants and methods for using same
EP2786743A1 (de) * 2013-04-02 2014-10-08 Evonik Industries AG Mischungszusammensetzung enthaltend Rhamnolipide
EP2787065A1 (de) * 2013-04-02 2014-10-08 Evonik Industries AG Waschmittelformulierung für Textilien enthaltend Rhamnolipide mit einem überwiegenden Gehalt an di-Rhamnolipiden
JP2014201745A (ja) * 2013-04-02 2014-10-27 エヴォニク インダストリーズ アーゲー ジ−ラムノ脂質含量が大部分を占めるラムノ脂質を含むテキスタイル用洗剤製剤
US9243212B2 (en) 2013-04-02 2016-01-26 Evonik Degussa Gmbh Detergent formulation for textiles, comprising rhamnolipids with a predominant content of di-rhamnolipids
US10292924B2 (en) 2013-04-02 2019-05-21 Evonik Industries Ag Mixture composition comprising rhamnolipids
WO2015091294A1 (en) * 2013-12-18 2015-06-25 Unilever Plc Mono-rhamnolipid based compositions.
WO2015091457A1 (en) * 2013-12-19 2015-06-25 Unilever Plc Composition
CN105992814A (zh) * 2013-12-19 2016-10-05 荷兰联合利华有限公司 组合物
US10674726B2 (en) 2013-12-19 2020-06-09 Conopco, Inc. Composition
WO2016055591A1 (fr) 2014-10-08 2016-04-14 Centre National De La Recherche Scientifique (Cnrs) Biosurfactants de pseudomonas pour lutter contre les legionelles
WO2016066464A1 (de) * 2014-10-28 2016-05-06 Henkel Ag & Co. Kgaa Waschmittel mit mannosylerythritollipid
WO2016096478A1 (de) 2014-12-15 2016-06-23 Henkel Ag & Co. Kgaa Wasch- und reinigungsmittel
DE102014225789A1 (de) 2014-12-15 2016-06-16 Henkel Ag & Co. Kgaa Wasch- und Reinigungsmittel
US9884883B2 (en) 2015-01-12 2018-02-06 Logos Technologies, Llc Production of rhamnolipid compositions
WO2016139032A1 (en) * 2015-03-02 2016-09-09 Unilever Plc Compositions with reduced dye-transfer properties
US10487294B2 (en) 2015-03-02 2019-11-26 Conopco, Inc. Compositions with reduced dye-transfer properties
US10259837B2 (en) 2015-03-02 2019-04-16 Conopco, Inc. Method of separating rhamnolipids from a fermentation broth
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WO2016146497A1 (de) 2015-03-18 2016-09-22 Evonik Degussa Gmbh Zusammensetzung enthaltend peptidase und biotensid.
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US10988713B2 (en) 2015-03-18 2021-04-27 Evonik Operations Gmbh Composition containing peptidase and biosurfactant
WO2017036901A1 (en) * 2015-08-28 2017-03-09 Unilever Plc Improved wash compositions
WO2017036902A1 (en) * 2015-08-28 2017-03-09 Unilever Plc Detergent compositions with lipase and biosurfactant
US10400197B2 (en) 2015-08-28 2019-09-03 Conopco Inc. Detergent compositions with lipase and biosurfactant
US10829507B2 (en) 2017-02-06 2020-11-10 Stepan Company Decolorization of concentrated rhamnolipid composition
WO2019034490A1 (de) 2017-08-16 2019-02-21 Henkel Ag & Co. Kgaa Rhamnolipidhaltige wasch- und reinigungsmittel
DE102017214265A1 (de) 2017-08-16 2019-02-21 Henkel Ag & Co. Kgaa Rhamnolipidhaltige Wasch- und Reinigungsmittel
WO2019154970A1 (en) * 2018-02-09 2019-08-15 Evonik Degussa Gmbh Mixture composition comprising glucolipids
US11993803B2 (en) 2018-02-09 2024-05-28 Evonik Operations Gmbh Mixture composition comprising glucolipids
US11744269B2 (en) * 2020-01-06 2023-09-05 Vinay Bhalchandra PARANJPE Vegetable and fruit wash formulation and uses thereof
US20210204571A1 (en) * 2020-01-06 2021-07-08 Vinay Bhalchandra PARANJPE Vegetable and Fruit Wash Formulation and Uses Thereof
WO2023099346A1 (en) * 2021-12-02 2023-06-08 Evonik Operations Gmbh Composition comprising glucolipids
DE102021214680A1 (de) 2021-12-20 2023-06-22 Henkel Ag & Co. Kgaa Neue Tensidkombination und Wasch- und Reinigungsmittel, welche diese enthalten
EP4198112A1 (de) 2021-12-20 2023-06-21 Henkel AG & Co. KGaA Neue tensidkombination und wasch- und reinigungsmittel, welche diese enthalten
WO2023116569A1 (en) * 2021-12-21 2023-06-29 Novozymes A/S Composition comprising a lipase and a booster
EP4234664A1 (de) 2022-02-24 2023-08-30 Evonik Operations GmbH Zusammensetzung mit glucolipiden und enzymen
EP4155371A1 (de) * 2022-08-29 2023-03-29 Evonik Operations GmbH Mono-rhamnolipidreiche zusammensetzung
EP4353806A1 (de) 2022-10-14 2024-04-17 Henkel AG & Co. KGaA Tensidmischungen
DE102022210879A1 (de) 2022-10-14 2024-04-25 Henkel Ag & Co. Kgaa Tensidmischungen

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ES2561553T3 (es) 2016-02-26
BR112013000108B1 (pt) 2021-05-11
EP2596087B1 (de) 2015-12-16
EP2596087A1 (de) 2013-05-29
ZA201300377B (en) 2014-03-26
CN103052704A (zh) 2013-04-17
BR112013000108A2 (pt) 2017-06-13

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