WO2013024143A1 - Système enzymatique - Google Patents

Système enzymatique Download PDF

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Publication number
WO2013024143A1
WO2013024143A1 PCT/EP2012/066050 EP2012066050W WO2013024143A1 WO 2013024143 A1 WO2013024143 A1 WO 2013024143A1 EP 2012066050 W EP2012066050 W EP 2012066050W WO 2013024143 A1 WO2013024143 A1 WO 2013024143A1
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WO
WIPO (PCT)
Prior art keywords
enzymes
aha
psychrophilic
mesophilic
stainzyme
Prior art date
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PCT/EP2012/066050
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English (en)
Inventor
Neil James Parry
Stephen Wilson
Original Assignee
Unilever Plc
Unilever N.V.
Hindustan Unilever Limited
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 N.V., Hindustan Unilever Limited filed Critical Unilever Plc
Priority to EP12751483.4A priority Critical patent/EP2744882A1/fr
Priority to CN201280040074.7A priority patent/CN103748205A/zh
Publication of WO2013024143A1 publication Critical patent/WO2013024143A1/fr
Priority to ZA2014/00850A priority patent/ZA201400850B/en

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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
    • C11D2111/12—

Definitions

  • the present invention concerns the delivery of enzymes in a washing process.
  • the use of enzyme mixtures during a laundering process is known.
  • a first aspect of the present invention provides an enzymatic fabric treatment composition comprising the combination of:
  • a second aspect of the invention provides a method of treating a fabric using an enzymatic fabric treatment composition according to the first aspect wherein the temperature of the wash liquor varies between psychrophilic and mesophilic and optionally thermophilic temperatures throughout a single washing cycle.
  • the term "single washing cycle" as used herein means a single washing process, including one or more aqueous washing phases and one or more aqueous rinse phases. The cycle is completed after a final rinsing and the fabric is then ready for drying and re-use. The cycle may include a pre-treatment phase. Preferably the temperature varies between psychrophilic and mesophilic and thermophilic temperatures throughout a single washing cycle.
  • the invention is highly advantageous where the temperature of the wash liquor is uncontrolled in at least one part by the user.
  • the wash liquor temperature is uncontrolled in a substantial amount and more preferably is uncontrolled to the extent that temperature is entirely driven by ambient conditions.
  • the method may comprise a hand-washing treatment or be carried out in a washing machine, the washing machine preferably without any water heating.
  • wash liquor temperature is often both varying and uncontrolled. Varying of the temperature may happen within a single washing process or over successive washes.
  • the washing water may be drawn from a tap fed by underground pipes and the washing process may begin at low temperatures (5-15 °C) and then rise under warmer ambient conditions to 20°C, 30°C, 40°C or higher.
  • Varying climatic conditions mean ambient temperatures differ seasonally at the least.
  • pyschrophilic enzyme means enzymes that are effective at a temperature of 0°C - 25°C.
  • the term "mesophilic enzyme” means enzymes that are effective at a temperature in the range 25°C-50°C.
  • thermoophilic means enzymes that are effective at a temperature in the range 50°-90° C.
  • the term “effective” means that the enzyme has the ability to achieve stain removal or catalytic capability (in the given temperature zone).
  • the term “enzyme” includes enzyme variants (produced, for example, by recombinant techniques). Examples of such enzyme variants are disclosed, e.g., in EP 251 ,446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV).
  • stain removal is measured in terms of Remission units or a Remission index. Effective stain removal is preferably represented by remission equal to or greater than 2 Remission units.
  • treatment in the context of enzymatic fabric treatment composition preferably means cleaning and more preferably stain removal.
  • Enzymes may be from bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • the one or more psychrophilic and/or one or more mesophilic and/or one or more thermophilic enzymes comprise a common class of enzymes. This has the advantage of addressing a particular type of stains at different
  • the common class is a protease or a lipase or a glycosyl hydrolase or a lyase or a oxidoreductase.
  • the invention may comprise a mixed class of enzymes.
  • this comprises a psychrophilic lipase and a mesophilic protease.
  • the advantage of this combination is with washing processes which begin with low temperature, in which the lipase is effective but where the protease is inhibited from attacking the lipase.
  • the one or more psychrophilic enzymes comprise esterases (ester hydrolases) and more preferably carboxylic ester hydrolases and more preferably e.g. lipases and/or phospholipases.
  • esterases ester hydrolases
  • carboxylic ester hydrolases preferably e.g. lipases and/or phospholipases.
  • lipases are highly advantageous psychrophilic enzymes because fats and oil based stains are more difficult to remove at psychrohilic temperatures.
  • the one or more psychrophilic enzymes comprise glycosyl hydrolases (glycosylases) for example cellulases, amylases (including alpha-amylases), xylanases, etc.
  • Psychrophilic lipases include lipases from Acinetobacter sp. Strain No. 6 (Suzuki et al. (2001 ) J. Biosci. Bioeng. 92: 144-148; Acinetobacter sp. Strain No.Oi 6
  • Psychrophilic esterases preferably include esterases EstATI and EstAT1 1 described by Jeon et al. Mar Biotechnol (2009) 1 1 :307-316.
  • Psychrophlic glycosyl hyrdolases preferably include glycosidases such as amylases, eg. a-amylases from Pseudoalteromonas haloplanktis strain TAC 125 and from Alteromonas haloplanktis A23 (Feller et al (1998) Journal Biological Chemistry Vol 273, No. 20 pp 12109-121 15) and from Nocardiopsis sp. 7326; cellulases and xylanase from e.g. Clostridium sp. PXYL1 (G. Akila, T.S.Chandra (2003) FEMS Microbiol. Letters 219, 63-67). Psychrophilic xylanases include E.coli phagemid (Lee et al. 2006b).
  • Preferred pyschrophilic proteases include those derived from Flavobacterium balustinum P104 (isolated from the internal organs of salmon and has been deposited in National Institute of Bioscience and Human-Technology, Agency of Industrial Science and Technology as the deposit number of FERM BP-5006 on February 17, 1995 and described in WO/1996/025489) and from Arthrobacter globiformis S155 (Poitier et al, (1995) J. Gen. Microbiol. 133:2797-2806).
  • Pschrophilic lyases preferably include pectate lyases e.g. from
  • the one or more mesophilic enzymes comprise proteases and/or glycosidases and/or pectate lyases.
  • Preferred mesophilic proteases include serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease.
  • Alkaline proteases include subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168.
  • Trypsin-like i.e. capable of cleaving peptide bonds at the C-terminal side of lysine or arginine.
  • proteases may be of porcine or bovine origin. Fusarium derived trypsin proteases are also included.
  • protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, DyrazymTM, EsperaseTM, EverlaseTM, PolarzymeTM, and KannaseTM, (Novozymes A/S), MaxataseTM, MaxacalTM, MaxapemTM,
  • Preferred mesophilic lipases include lipases from Humicola (synonym
  • Thermomyces e.g. from H. lanuginosa (7. lanuginosus) or from H. insolens, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes,
  • mesophilic lipase enzymes include LipolaseTM and CrelipolaseTM
  • Lipolase UltraTM LipexTM (Novozymes A/S).
  • Preferred mesophilic Phospholipases include enzymes which hydrolyse phospholipids.
  • Phospholipases Ai and A 2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B) which can hydrolyze the remaining fatty acyl group in lysophospholipid are included as are Phospholipase C and phospholipase D (phosphodiesterases)which release diacyl glycerol or phosphatidic acid respectively.
  • phospholipase A used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase Ai 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 mesophilic phospholipase may be of any origin, e.g., of animal origin (such as, e.g., mammalian), e.g. from pancreas (e.g., bovine or porcine pancreas), or snake venom or bee venom.
  • animal origin such as, e.g., mammalian
  • pancreas e.g., bovine or porcine pancreas
  • snake venom or bee venom e.g., from snake venom or bee venom.
  • the phospholipase may be of microbial origin, e.g., from filamentous fungi, yeast or bacteria, such as the genus or species Aspergillus, e.g., A. niger, Dictyostelium, e.g., D. discoideum; Mucor, e.g. M. javanicus, M. mucedo, M. subtil
  • Rhizomucor e.g., R. pusillus
  • Rhizopus e.g. R. arrhizus, R. japonicus, R.
  • Sclerotinia e.g., S. libertiana
  • Trichophyton e.g. T. rubrum
  • Whetzelinia e.g., W. sclerotiorum
  • Bacillus e.g., B. megaterium, B. subtilis
  • Citrobacter e.g., C. freundii
  • Enterobacter e.g., E. aerogenes, E. cloacae
  • Edwardsiella E. tarda
  • Erwinia e.g., E. herbicola
  • Escherichia e.g., E. coli
  • Klebsiella e.g., K. pneumoniae
  • Proteus e.g., P. vulgaris
  • Providencia e.g., P. stuartii
  • Salmonella e.g. S. typhimurium
  • Serratia e.g., S. liquefasciens, S.
  • 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 class Pyrenomycetes such as the genus Fusarium, such as a strain of F. culmorum, F. heterosporum, F. solani, or a strain of F. oxysporum.
  • phospholipase may also be from a filamentous fungus strain within the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus,
  • Preferred mesophilic phospholipases are derived from a strain of Humicola, especially Humicola lanuginosa or variant; and from strains of Fusarium, especially Fusarium oxysporum.
  • the phospholipase may be derived from
  • mesophilic phospholipases comprise a phospholipase Ai (EC.
  • mesophilic phospholipases examples include LECITASETM and LECITASETM ULTRA, YIELSMAX, or LIPOPAN F (available from Novozymes A/S, Denmark).
  • Preferred mesophilic cutinases are 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 Heiminthosporum, in particular Heiminthosporum sativum, a strain of Humicoia, in particular Humicoia insoiens, a strain of Pseudomonas, in particular Pseudomonas mendocina, or Pseudomonas putida, a strain of
  • Rhizoctonia in particular Rhizoctonia solani
  • a strain of Streptomyces in particular Streptomyces scabies
  • a strain of Ulocladium in particular Ulocladium
  • cutinase is derived from a strain of Humicoia insoiens, in particular the strain Humicoia insoiens DSM 1800.
  • cutinases include NOVOZYMTM 51032 (available from Novozymes A/S, Denmark).
  • Preferred mesophilic amylases are included for example, alpha-amylases obtained from Bacillus, e.g. from strains of B. licheniformis
  • mesophilic amylases are DuramylTM, TermamylTM,
  • Preferred mesophilic cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicoia, Fusarium, Thielavia, Acremonium, e.g. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila, and Fusarium oxysporum.
  • Especially preferred mesophilic cellulases are the alkaline or neutral cellulases having color care benefits.
  • Commercially available cellulases include
  • Preferred mesophilic pectate lyases include pectate lyases that are derived/cloned from bacterial genera such as Erwinia, Pseudomonas, Klebsiella and
  • alkaline mesophilic pectate lyases examples include BIOPREPTM and SCOURZYMETM L from Novozymes A/S, Denmark.
  • Preferred mesophilic mnanases include derived from a strain of the filamentous fungus genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus or Trichoderma reseei or from the Bacillus microorganism FERM P- 8856 which produces beta-mannanase and beta-mannosidase or from alkalophilic Bacillus sp. AM-001 or from Bacillus amyloliquefaciens.
  • the mannanase may comprise alkaline family 5 and 26 mannanases derived from Bacillus
  • mannanases examples include MannawayTM available from Novozymes A/S Denmark.
  • Preferred mesophilic peroxidases/oxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof.
  • Commercially available peroxidases include GuardzymeTM and NovozymTM 51004 (Novozymes A/S).
  • Thermophilic proteases include proteases derived from Thermophilic Bacillus strain HS08 (African Journal of Biotechnology Vol. 5 (24), pp. 2433-2438, 18 December 2006) and B.Stearothermophilius 1503; Thermos caldophilus GK24; T. Aquaticus lZS ; T. aquaticus Yl Aq. l and Aq. II.
  • Thermophilic Lipases include those derived from Bacillus thermocatenulatus BTL1 and preferably BTL2 (Schimdt-Dannert et at., Biochim. Biophys. Acta (1994) 1214, pp. 43-5 and Biochim. Biophys. Acta (1996) 1301 , pp. 105-1 14).
  • Thermophilic glycosyl hydrolases include alpha-amylases from B.
  • Thermophilic lyases include the pectate lyases from Thermoanaerobacter italicus sp. nov. strain Ab9 (Kozianowski et al., (1997) Extremophiles Vol 1 , 4: 171 -182).
  • the fabric treatment composition may comprise a laundry/fabric cleaning/care composition and may comprise one or more surfactants and/or optionally other ingredients.
  • Such compositions of the invention may be in dry solid form e.g. powdered, granules or tableted powders or liquid or gel form. It may also be in the form of a solid detergent bar.
  • the composition may be a concentrate to be diluted, rehydrated and/or dissolved in a solvent, including water, before use.
  • the composition may also be a ready-to-use (in-use) composition.
  • the present invention is suitable for use in industrial or domestic fabric wash compositions, fabric conditioning compositions and compositions for both washing and conditioning fabrics (so-called through the wash conditioner compositions).
  • the present invention can also be applied to industrial or domestic non-detergent based fabric care compositions, for example direct application e.g. roll-on or spray-on compositions which may be used as a pre-treatment of e.g. localised portions of fabric prior to a 'main' wash.
  • the enzymes may be present at 0-5 wt%, preferably 2-4 wt%, and most preferably 2.5-3.5 wt% of the composition (where wt% means percentage of the total weight of the composition).
  • the total protein concentration (of the total range of enzymes according to the invention) in the wash liquor preferably ranges from 0.01 to 10.0 mg /L and more preferably 2 to 5 mg/L.
  • composition will comprise individual levels of psychrophilic/mesophilic and optionally thermophilic enzymes
  • the enzymes may be the sole fabric treatment agent or other stain removal agents may be incorporated.
  • detergent ingredients may be included including surfactants, builders, sequestring agents, hydrotropes, preservatives, complexing agents, polymers, stabilizers, perfumes, optical brighteners, or other ingredients such as e.g. fabric conditioners including clays, foam boosters, suds suppressors (anti-foams), anti- corrosion agents, soil-suspending agents, anti-soil redeposition agents, antimicrobials, tarnish inhibitors, or combinations of one or more thereof, provided that these ingredients are compatible with the enzymes.
  • fabric conditioners including clays, foam boosters, suds suppressors (anti-foams), anti- corrosion agents, soil-suspending agents, anti-soil redeposition agents, antimicrobials, tarnish inhibitors, or combinations of one or more thereof, provided that these ingredients are compatible with the enzymes.
  • the fabric wash compositions may comprise a fabric wash detergent material selected from non-soap anionic surfactant, nonionic surfactants, soap, amphoteric surfactants, zwitterionic surfactants and mixtures thereof.
  • the surfactants may be present in the composition at a level of from 0.1 % to 60% by weight.
  • Any enzyme present in a composition may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid.
  • a polyol such as propylene glycol or glycerol
  • a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid.
  • Figures 1 -3 correspond with Tables 1 -3a,b respectively, and show effectiveness data for enzymes AHA and Stainzyme separately and both together in various conditions.
  • an alpha amylase (hereafter termed AHA) was identified from peer-reviewed literature as having desirable psychrophilic properties (Feller, G. et al, 1992; J. Biol. Chem. 267 (8), 5217-5221 ).
  • the gene sequence (GenBank accession number: X58627.1 ) comprising the amylase was accessed from a publicly available database
  • FIG. 1 shows the modified sequence, for protein production in E. coli and figure 3 is the sequence of AHA once incorporated into the pUC19 vector.
  • the sequence shown in figure 2 was chemically synthesized and inserted into the pUC19 plasmid (as shown in figure 3) as a service by Eurogentec Ltd (Southampton, UK) using their own proprietary methodologies.
  • amylase The constitutive production of amylase was confirmed using reagents supplied by Roche Diagnostics in kit form (catalogue number 1 1876473 316) in 96-well microtitre plates as follows: 10 ⁇ of each sample to be assessed (or dilution thereof) was added to a well of the microtitre plate (in duplicate). 75 ⁇ reagent 1 was added followed by 15 ⁇ of reagent 2.
  • An assay blank comprised the additions described, replacing AHA-containing growth media with unused LB. Plates were incubate for 30 minutes at prescribed temperatures (normally 20°C) and then assessed for p-nitrophenol release (as a result of amylase activity) on a FluoStar Optima microplate reader set for absorbance detection at 405nm.
  • Enzyme combinations A, B, C, D, E are as follows.
  • the combination comprises the psychrophilic enzyme/s and the mesophilic enzyme and/or the thermophilic enzyme.
  • the a-amylases enzymatic activity of AHA, Stainzyme and of AHA and Stainzyme together between the temperatures of 20°C and 50°C was determined using reagents supplied by Roche Diagnostics in kit form (catalogue number 1 1876473 316).
  • the instrument was set up to run a temperature gradient between 20°C and 50°C.
  • the samples aliquoted into the 96-well PCR plate were incubated for exactly 30 minutes under the above conditions, at which point the PCR plate was rapidly cooled to 4°C.
  • 50 ⁇ of 1 M tris.base (unbuffered) was added to each well to stop the reaction (prevention of further p-nitrophenol reaction product release).
  • 10 ⁇ of each reaction cocktail was transferred to a clear flat-bottomed microtitre plate and assessed for absorbance at 405nm using a Fluostar Optima plate reader. Blank values at each tested temperature were subtracted from the results obtained for enzyme- containing cocktails. Results are shown in Figure 1 .
  • the instrument was set up to run a temperature gradient between 20 and 50°C.
  • the samples aliquoted into the 96-well PCR plate were incubated for exactly 30 minutes under the above conditions, at which point the PCR plate was rapidly cooled to 4°C.
  • 50 ⁇ of 1 M tris.base (unbuffered) was added to each well to stop the reaction (prevention of further p-nitrophenol reaction product release).
  • 10 ⁇ of each reaction cocktail was transferred to a clear flat-bottomed microtitre plate and assessed for absorbance at 405nm using a Fluostar Optima plate reader. Blank values at each tested temperature were subtracted from the results obtained for enzyme- containing cocktails. Results are shown in Figure 2.
  • the instrument was set up to run a temperature gradient between 20 and 50°C.
  • the samples aliquoted into the 96-well PCR plate were incubated for exactly 30 minutes under the above conditions, at which point the PCR plate was rapidly cooled to 4°C.
  • 50 ⁇ of 1 M tris.base (unbuffered) was added to each well to stop the reaction (prevention of further p-nitrophenol reaction product release).
  • 10 ⁇ of each reaction cocktail was transferred to a clear flat-bottomed microtitre plate and assessed for absorbance at 405nm using a Fluostar Optima plate reader. Blank values at each tested temperature were subtracted from the results obtained for enzyme- containing cocktails. Results are shown in Figure 3.
  • Table 1 a and 1 b Activity data for AHA, Stainzyme and both enzymes together, where stock solutions of each enzyme were diluted 1 in 125 for use in assay (data values are Absorbance readings using a Fluostar Optima microplate reader set to 405nm, after incubation with assay substrate for 30 minutes in a gradient of temperatures between 20°C and 50°C). Graphically represented in Figure 5.
  • n data Mean value 1.044 1.060 1.116 1.171 1.157 1.108 (0.5x Mean minus 0.913 0.931 0.988 1.039 1.021 0.971
  • AHA data Raw data value 1 1.674 1.709 1.770 1.742 1.653 1.444
  • Tables 2a, 2b Activity data for AHA, Stainzyme and both enzymes together, where stock solutions of each enzyme were diluted 1 in 250 for use in assay (data values are Absorbance readings using a Fluostar Optima microplate reader set to 405nm, after incubation with assay substrate for 30 minutes in a gradient of temperatures between 20°C and 50°C). Graphically represented in Figure 2. Table 2a Temperatures 22.5
  • Table 3 Activity data for AHA, Stainzyme and both enzymes together, where stock solutions of each enzyme were diluted 1 in 417 for use in assay (data values are Absorbance readings using a Fluostar Optima microplate reader set to 405nm, after incubation with assay substrate for 30 minutes in a gradient of temperatures between 20°C and 50°C). Graphically represented in Figure 3. Table 3a Temperatures 22.5
  • Stainzyme mean blank value 0.513 0.518 0.545 0.566 0.561 0.525 + 0.5x 1 Standard
  • AHA data Raw data value 1 0.906 0.925 0.947 0.924 0.871 0.752
  • AHA and Stainzyme a-amylase enzymes were diluted to appropriate concentrations (as indicated) using 100mM HEPES buffer pH7 plus 100mM sodium chloride and 1 mM calcium chloride.
  • Table 4 Data demonstrating stain removal of C-S-27 potato starch-stained fabric by AHA and Stainzyme, either alone or in combination. Wash temperatures were 10°C, 20°C and 60°C (top, middle and bottom panels respectively). Data is expressed as SRI's and replicates are presented along with the arithmetic mean values and the standard deviation (1 SD).
  • Non-Limiting examples of laundry enzymatic fabric treatment compositions are described below where the following example enzyme combinations are: A. Lipase Combination
  • Psychrophilic Lipase from Pseudoalteromonas sp W27.
  • Thermophilic Lipase from Bacillus thermocatenlatus BTL2 B. Protease Combination
  • Thermophilic Protease from Thermophilic Bacillus strain HS08
  • Psychrophilic amylase alpha-amylase from Pseudoalteromonas haloplanktis strain TAC 125 and/or Pseudoalteromonas haloplanktis strain TAB 23 (as above)
  • Mesophilic amylase StainzymeTM 2.0 T (Novozymes)
  • Thermophilic amylase alpha-amylase from B. stearothermophilus Donk BS-1 .
  • Psychrophilic pectate lyase from Pseudoalteromonas haloplanktis ANT/505 Mesophilic pectate lyase: BioprepTM Novozymes
  • Thermophilic pectate lyase from Thermoanaerobacter italicus sp. Nov. AB9.
  • Psychrophilic Lipase from Pseudoalteromonas sp W27 and
  • Thermophilic amylase alpha-amylase from B. stearothermophilus Donk BS-1 .
  • Liquid Enzymatic Fabric Treatment Composition comprising enzyme combinations above :
  • Sequestrant (Dequest 2066) 0.5 Fluorescor 0.3

Abstract

L'invention porte sur une composition enzymatique de traitement des tissus comprenant une combinaison (i) d'au moins une enzyme psychrophile, et (ii) d'au moins une enzyme mésophile et/ou d'au moins une enzyme thermophile.
PCT/EP2012/066050 2011-08-18 2012-08-16 Système enzymatique WO2013024143A1 (fr)

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CN201280040074.7A CN103748205A (zh) 2011-08-18 2012-08-16 酶体系
ZA2014/00850A ZA201400850B (en) 2011-08-18 2014-02-04 Enzyme system

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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US10400197B2 (en) * 2015-08-28 2019-09-03 Conopco Inc. Detergent compositions with lipase and biosurfactant
CN112322547A (zh) * 2020-11-23 2021-02-05 江苏海洋大学 来自海洋的假交替单胞菌hl9及其产磷脂酶b的方法

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CN112322547A (zh) * 2020-11-23 2021-02-05 江苏海洋大学 来自海洋的假交替单胞菌hl9及其产磷脂酶b的方法
CN112322547B (zh) * 2020-11-23 2021-10-08 江苏海洋大学 来自海洋的假交替单胞菌hl9及其产磷脂酶b的方法

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