WO2021105336A1 - Compositions comprising polymer and enzyme - Google Patents

Compositions comprising polymer and enzyme Download PDF

Info

Publication number
WO2021105336A1
WO2021105336A1 PCT/EP2020/083599 EP2020083599W WO2021105336A1 WO 2021105336 A1 WO2021105336 A1 WO 2021105336A1 EP 2020083599 W EP2020083599 W EP 2020083599W WO 2021105336 A1 WO2021105336 A1 WO 2021105336A1
Authority
WO
WIPO (PCT)
Prior art keywords
composition
enzyme
protease
lipase
polymer
Prior art date
Application number
PCT/EP2020/083599
Other languages
French (fr)
Inventor
Oliver Spangenberg
Alejandra Garcia Marcos
Menno Hazenkamp
Claudia Esper
Ivette Garcia Castro
Sandra Gloria KÖNIG
Eva Maria BETTHAUSEN
Stephan Hueffer
Susanne Carina ENGERT
Anna Maria MUELLER-CRISTADORO
Matthias KELLERMEIER
Grit BAIER
Florian Ludwig GEYER
Original Assignee
Basf Se
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 Basf Se filed Critical Basf Se
Publication of WO2021105336A1 publication Critical patent/WO2021105336A1/en

Links

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
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3723—Polyamines or polyalkyleneimines
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08G—MACROMOLECULAR COMPOUNDS OBTAINED OTHERWISE THAN BY REACTIONS ONLY INVOLVING UNSATURATED CARBON-TO-CARBON BONDS
    • C08G65/00—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule
    • C08G65/02—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring
    • C08G65/26—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds
    • C08G65/2603—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds the other compounds containing oxygen
    • C08G65/2606—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds the other compounds containing oxygen containing hydroxyl groups
    • C08G65/2609—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds the other compounds containing oxygen containing hydroxyl groups containing aliphatic hydroxyl groups
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08G—MACROMOLECULAR COMPOUNDS OBTAINED OTHERWISE THAN BY REACTIONS ONLY INVOLVING UNSATURATED CARBON-TO-CARBON BONDS
    • C08G65/00—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule
    • C08G65/02—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring
    • C08G65/26—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds
    • C08G65/2618—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds the other compounds containing nitrogen
    • C08G65/2621—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds the other compounds containing nitrogen containing amine groups
    • C08G65/2624—Macromolecular compounds obtained by reactions forming an ether link in the main chain of the macromolecule from cyclic ethers by opening of the heterocyclic ring from cyclic ethers and other compounds the other compounds containing nitrogen containing amine groups containing aliphatic amine groups
    • 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
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/0008—Detergent materials or soaps characterised by their shape or physical properties aqueous liquid non soap compositions
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3707—Polyethers, e.g. polyalkyleneoxides
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/37—Polymers
    • C11D3/3788—Graft polymers
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38618—Protease or amylase in liquid compositions only
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08G—MACROMOLECULAR COMPOUNDS OBTAINED OTHERWISE THAN BY REACTIONS ONLY INVOLVING UNSATURATED CARBON-TO-CARBON BONDS
    • C08G73/00—Macromolecular compounds obtained by reactions forming a linkage containing nitrogen with or without oxygen or carbon in the main chain of the macromolecule, not provided for in groups C08G12/00 - C08G71/00
    • C08G73/02—Polyamines
    • C08G73/024—Polyamines containing oxygen in the form of ether bonds in the main chain
    • 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
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile

Definitions

  • compositions comprising polymer and enzyme
  • compositions comprising (A) at least one polymer comprising
  • X 1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the fore going, preferred are methyl and more preferred is hydrogen, n is in the range of from 1 to 4,
  • the present invention is directed to polymers useful for such compositions, and to a process for making such polymers.
  • the present invention is directed to the use of the compositions comprising the poly mer and the at least one enzyme described herein for cleaning of textiles or hard surfaces.
  • the compositions described herein are suitable for biofilm and/or sebum stain remov al and/or malodour reduction.
  • Laundry detergents and detergents for dish washing have to fulfil several re- quirements. They need to remove all sorts of soiling from laundry or hard surfaces, for example all sorts of pigments, clay, fatty soil, sebum and body soils and dyestuffs including dyestuff from food and drinks such as red wine, tea, coffee, and fruit including berry juices.
  • Laundry deter gents and dish wash detergents also need to exhibit a certain storage stability. Especially laun dry detergents and dish washing detergents that are liquid or that contain hygroscopic ingredi ents often lack a good storage stability, e.g. enzymes tend to be deactivated.
  • Fatty soilings including sebum, are still a challenge, in particular in laundering.
  • nu merous suggestions for removal have been made - polymers, enzymes, surfactants - solutions that work well are still of interest.
  • Malodor on clothes may be formed when body soils, like sebum are not well removed from clothes during washing. Bacteria can transform residual sebum on clothes into malodorous substances. More over, bacterial biofilms sometimes are formed in washing machines, especially when the wash ing temperatures are too low to kill all microorganisms. Also such biofilms can contribute to mal odor formation on clothes washed in that machine.
  • a laundry detergent in particular a liquid laundry detergent, can remove sebum soils well from clothes and if it could prevent and/or remove the formation of bacterial biofilms in washing machines.
  • compositions defined at the outset have been found, hereinafter also referred to as inventive compositions or compositions according to the present invention.
  • compositions comprise (A) least one polymer comprising
  • C 2 -Ci2-alkylene for example -CH 2 CH 2 -, -(CH 2 ) 3 -, -(CH 2 ) 4 -, -(CH 2 ) 5 -, -(CH 2 ) 6 -, -(CH 2 ) 8 -, -(CH 2 ) 10 -, -(CH 2 )i2-, wherein C 2 -Ci 2 -alkylene may be straight-chain or branched, non-substituted or substi tuted with one or more 0-CrC 4 -alkyl groups and
  • C3-Ci2-cycloalkylene wherein C3-Ci 2 -cycloalkylene may be non-substituted or substituted with one or more 0-CrC 4 -alkyl groups, and where C3-Ci 2 -cycloalkylene may bear one to three me thyl groups, preferably Cs-Cio-cycloalkylene such as 1,3-cyclopentylene, 1,2-cyclopentylidene, 1,2-cyclohexylene, 1,3-cyclohexylene, 1,4-cyclohexylene, 1 -methyl-2, 4-cyclohexylene, 1- methyl-2, 6-cyclohexylene, 1,3-cycloheptylene, 1,4-cylooctylene, 1,5-cyclooctylene, wherein C 2 -Ci 2 -alkylene and C3-Ci 2 -cycloalkylene may be non-substituted or substituted with one or more 0-Cr
  • X 1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the fore going, preferred are methyl and more preferred is hydrogen, preferred is hydrogen, n is in the range of from 1 to 4, preferably 1 to 3 and more preferably 1 to 2,
  • the free valences on the nitrogen atoms in formula (I) bear polyalkylene chains (b) or -CH 2 -CH(X 1 )-0-CHX 1 -CH 2 -N-Z-N units, or hydrogen atoms. In embodiments with molecular weights M w of 10,000 g/mol or more, the free valences on the nitrogen atoms in formula (I) bear polyalkylene chains (b) or-CH 2 -CH(X 1 )-0-CHX 1 -CH 2 -N-Z-N units.
  • all Z in polymer (A) are selected from cyclo hexylene and cyclopentylene, each non-substituted or substituted with one to two methyl or methoxy groups.
  • Z are isomers to each other and/or differ in the variable n. Even more preferably, Z are isomers.
  • a preferred example of Z is a combination - thus a mixture of isomers - according to the formu lae
  • Asterisks * refer to sites in Z that are connected to N atoms.
  • polymer (A) has an average molecular weight M w in the range of from 1,000 to 80,000 g/mol, preferably 5,000 to 50,000 g/mol.
  • the average mo lecular weight may be determined, e.g., by gel permeation chromatography (GPC) in tetrahydro- furan (THF) as mobile phase, with linear polymethyl methacrylate (“PMMA”) as standard.
  • polymer (A) has a molecular weight distribution M w /M n in the range of from 1.1 to 2.5.
  • polymer (A) has a Hazen colour number in the range of from 20 to 500, determined in a 10 % weight aqueous solution.
  • polymer (A) has an OH value, measured according to DIN 53240 (2013), in the range of from 20 to 650, preferably 30 to 100 mg KOH/g polymer (A).
  • polymer (A) has a total amine value in the range of from 10 to 650, preferably 10 to 510 and more preferably 10 to 80 mg KOH/g polymer (A), de termined according to ASTM D2074-07.
  • Polymer (A) furthermore bears
  • polyalkylene oxide chains may be derived from C2-C4- alkylene oxide.
  • C2-C4-alkylene oxides are ethylene oxide difficultyEO“), propylene ox ide (“PO”), butylene oxide (“BuO”), and combinations of at least two of the foregoing, for example ethylene oxide and propylene oxide or ethylene oxide and butylene oxide.
  • Pre ferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.
  • the inventive compositions comprise additionally at least one enzyme (B).
  • Enzymes are identified by polypeptide sequences (also called amino acid sequences herein).
  • the polypeptide sequence specifies the three-dimensional structure including the “active site” of an enzyme which in turn determines the catalytic activity of the same.
  • Polypeptide sequences may be identified by a SEQ ID NO. According to the World Intellectual Property Office (WIPO) Standard ST.25 (1998) the amino acids herein are represented using three-letter code with the first letter as a capital or the corresponding one letter.
  • Any enzyme according to the invention relates to parent enzymes and/or variant enzymes, both having enzymatic activity.
  • Enzymes having enzymatic activity are enzymatically active or exert enzymatic conversion, meaning that enzymes act on substrates and convert these into prod ucts.
  • a “parent” sequence (of a parent protein or enzyme, also called “parent enzyme”) is the starting sequence for introduction of changes (e.g. by introducing one or more amino acid substitutions, insertions, deletions, or a combination thereof) to the sequence, resulting in “variants” of the parent sequences.
  • the term parent enzyme (or parent sequence) includes wild-type enzymes (sequences) and synthetically generated sequences (enzymes) which are used as starting se quences for introduction of (further) changes.
  • enzyme variant or “sequence variant” or “variant enzyme” refers to an enzyme that differs from its parent enzyme in its amino acid sequence to a certain extent. If not indicated otherwise, variant enzyme “having enzymatic activity” means that this variant enzyme has the same type of enzymatic activity as the respective parent enzyme.
  • Amino acid substitutions are described by providing the original amino acid of the parent en zyme followed by the number of the position within the amino acid sequence, followed by the substituted amino acid.
  • Amino acid deletions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by *.
  • Amino acid insertions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by the original amino acid and the additional amino acid. For example, an insertion at position 180 of lysine next to glycine is designated as “Gly180Glyl_ys” or “G180GK”.
  • alterations or optional substitutions may be indicated in brack ets e.g. Arg170[Tyr, Gly] or Arg170 ⁇ Tyr, Gly ⁇ ; or in short R170 [Y,G] or R170 ⁇ Y, G ⁇ ; or in long R170Y, R170G.
  • Enzyme variants may be defined by their sequence identity when compared to a parent en zyme. Sequence identity usually is provided as “% sequence identity” or “% identity”. For calcu lation of sequence identities, in a first step a sequence alignment has to be produced. According to this invention, a pairwise global alignment has to be produced, meaning that two sequences have to be aligned over their complete length, which is usually produced by using a mathemati cal approach, called alignment algorithm. According to the invention, the alignment is generated by using the algorithm of Needleman and Wunsch (J. Mol. Biol. (1979) 48, p. 443-453).
  • EM BOSS European Molecular Biology Open Software Suite
  • %-identity (identical residues / length of the alignment region which is showing the respective sequence of this in vention over its complete length) *100.
  • enzyme variants may be described as an amino acid sequence which is at least n% identical to the amino acid sequence of the respective parent enzyme with “n” being an integer between 10 and 100.
  • variant enzymes are at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical when compared to the full-length amino acid sequence of the parent en zyme, wherein the enzyme variant has enzymatic activity.
  • Enzymatic activity means the catalytic effect exerted by an enzyme, which usually is ex pressed as units per milligram of enzyme (specific activity) which relates to molecules of sub strate transformed per minute per molecule of enzyme (molecular activity).
  • Variant enzymes may have enzymatic activity according to the present invention when said enzyme variants ex hibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the enzymatic activity of the respective parent enzyme.
  • the enzyme is an oxidoreductase (EC 1), a transferase (EC 2), a hydrolase (EC 3), a lyase (EC 4), an isomerase (EC 5), or a ligase (EC 6) (EC-numbering ac cording to Enzyme Nomenclature, Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology including its supplements pub lished 1993-1999).
  • the enzyme is a hydrolase (EC 3), preferably, a glycosidase (EC 3.2) or a peptidase (EC 3.4).
  • enzymes selected from the group consisting of an amylase (in particular an alpha-amylase (EC 3.2.1.1)), a cellulase (EC 3.2.1.4), a lactase (EC 3.2.1.108), a mannanase (EC 3.2.1.25), a lipase (EC 3.1.1.3), a phytase (EC 3.1.3.8), a nuclease (EC 3.1.11 to EC 3.1.31), and a protease (EC 3.4); in particular an enzyme selected from the group consisting of amylase, protease, lipase, mannanase, phytase, xylanase, lactase, phosphatase, glucoamylase, nuclease, and cellulase, preferably, amylase or protease, preferably from protease, amylase, lipase, cellulase, cellulase
  • the protein of interest is an enzyme suitable to be used in detergents.
  • the enzyme is selected from the group consisting of amylase, pro tease, lipase, mannanase, xylanase, nuclease, and cellulase, preferably amylase, protease, lipase, mannanase, and cellulase, most preferably, selected from the group consisting of prote ase, lipase and mannanase.
  • the enzyme is a protease, preferably a subtilisin protease.
  • the enzyme is selected from hydrolases, most preferably from proteases, amylases, lipases, cellulases, nucleases, and mannanases.
  • the inventive compositions comprise at least one lipase.
  • Lipases “Lipases”, “lipolytic enzyme”, “lipid esterase”, all refer to enzymes of EC class 3.1.1 (“carboxylic ester hydrolase”).
  • Such a lipase may have lipase activity (or lipolytic activity; triacyl- glycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74; enzymes having cutinase activity may be called cutinase herein), sterol esterase activity (EC 3.1.1.13) and/or wax-ester hydro lase activity (EC 3.1.1.50).
  • Lipases include those of bacterial or fungal origin.
  • lipase examples include but are not limited to those sold under the trade names LipolaseTM, LipexTM, LipolexTM and LipocleanTM (Novozymes A/S), PreferenzTM L (DuPont), Lumafast (originally from Genencor) and Lipomax (Gist-Brocades/ now DSM).
  • lipase is selected from the following: lipases from Humi- cola (synonym Thermomyces ), e.g. from H. lanuginosa ( T . lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. insolens as described in WO 96/13580; lipases derived from Rhizomucor miehei as described in WO 92/05249; lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. from P. alcali- genes or P. pseudoalcaligenes (EP 218272, WO 94/25578, WO 95/30744, WO 95/35381,
  • WO 96/00292 P. cepacia (EP 331376), P. stutzeri (GB 1372034), P. fluorescens, Pseudomo nas sp. strain SD705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), Pseudomonas mendocina (WO 95/14783), P. glumae (WO 95/35381, WO 96/00292); lipase from Streptomyces griseus (WO 2011/150157) and S.
  • Suitable lipases include also those which are variants of the above described lipases which have lipolytic activity. Such suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105. Suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105.
  • Suitable lipases include also those that are variants of the above described lipases which have lipolytic activity.
  • Suitable lipase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • lipase variants having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • Lipases have “lipolytic activity”.
  • the methods for determining lipolytic activity are well-known in the literature (see e.g. Gupta et al. (2003), Biotechnol. Appl. Biochem. 37, p. 63-71).
  • the lipase activity may be measured by ester bond hydrolysis in the substrate para-nitrophenyl pal- mitate (pNP-Palmitate, C: 16) and releases pNP which is yellow and can be detected at 405 nm.
  • lipase is selected from fungal triacylglycerol lipase (EC class 3.1.1.3).
  • Fun gal triacylglycerol lipase may be selected from lipases of Thermomyces lanuginosa.
  • at least one Thermomyces lanuginosa lipase is selected from triacylglycerol lipase according to amino acids 1-269 of SEQ ID NO: 2 of US5869438 and variants thereof having lipolytic activity.
  • Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity which are at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.
  • Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing conservative mutations only, which do not pertain the functional domain of amino acids 1- 269 of SEQ ID NO: 2 of US 5,869,438.
  • Lipase variants of this embodiment having lipolytic ac tivity may be at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.
  • Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising at least the following amino acid substitutions when compared to amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438: T231R and N233R.
  • Said lipase variants may further comprise one or more of the following amino acid exchanges when compared to amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438: Q4V, V60S, A150G, L227G, P256K.
  • Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising at least the amino acid substitutions T231R, N233R, Q4V, V60S, A150G, L227G, P256K within the polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438and are at least 95%, at least 96%, or at least 97% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.
  • Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising the amino acid substitutions T231R and N233R within amino acids 1-269 of SEQ ID NO: 2 of US5869438 and are at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.
  • Thermomyces lanuginosa lipase may be a variant of amino acids 1-269 of SEQ ID NO: 2 of US5869438 having lipolytic activity, wherein the variant of amino acids 1-269 of SEQ ID NO: 2 of US5869438 is characterized in containing the amino acid substitutions T231R and N233R. Said lipase may be called Lipex herein.
  • a combination of at least two of the foregoing li pases may be used.
  • lipases are included in inventive composition in such an amount that a finished inventive composition has a lipolytic enzyme activity in the range of from 100 to 0.005 LU/mg, preferably 25 to 0.05 LU/mg of the composition.
  • inventive compositions comprise at least one pro tease.
  • At least one protease is selected from the group of serine endopeptidases (EC 3.4.21), most preferably selected from the group of subtilisin type proteases (EC 3.4.21.62).
  • Serine proteases or serine peptidases are characterized by having a serine in the catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction.
  • a ser ine protease in the context of the present invention may be selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21.79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.118, or EC 3.4.21.119,) plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5), and subtilisin.
  • chymotrypsin e.g., EC 3.4.21.1
  • elastase e.g., EC 3.4.21.36
  • subtilisin is also known as subtilopepti- dase, e.g., EC 3.4.21.62, the latter hereinafter also being referred to as “subtilisin”.
  • the subtil isin related class of serine proteases shares a common amino acid sequence defining a catalyt ic triad which distinguishes them from the chymotrypsin related class of serine proteases.
  • Sub- tilisins and chymotrypsin related serine proteases both have a catalytic triad comprising aspar tate, histidine and serine.
  • Proteases are active proteins exerting “protease activity” or “proteolytic activity”.
  • Proteolytic ac tivity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a de fined course of time.
  • proteolytic activity may be determined by using Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF; see e.g. DelMar et al. (1979), Analytical Biochem 99, 316-320) as substrate.
  • Ser-AAPF-pNA Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
  • pNA is cleaved from the substrate molecule by proteolytic cleavage, resulting in release of yellow color of free pNA which can be quantified by measuring OD405.
  • Proteolytic activity may be provided in units per gram enzyme.
  • 1 U protease may correspond to the amount of protease which sets free 1 pmol folin-positive amino acids and peptides (as tyrosine) per minute at pH 8.0 and 37°C (casein as substrate).
  • Proteases of the subtilisin type may be bacterial proteases originating from a microorganism selected from Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. coli, Flavobacterium, Fuso- bacterium, Helicobacter, llyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.
  • At least one protease is selected from Bacillus alcalophilus, Ba cillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus thuringiensis protease.
  • At least one protease is selected from the follow ing: subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bac terid. Volume 159, p. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 11, p. 7911-7925); subtilisin from Bacillus licheniformis (subtilisin Carlsberg; disclosed in EL Smith et al. (1968) in J. Biol Chem, Volume 243, pp. 2184-2191, and Jacobs et al. (1985) in Nucl. Acids Res, Vol 13, p.
  • subtilisin PB92 original sequence of the alkaline prote ase PB92 is described in EP 283075 A2; subtilisin 147 and/or 309 (Esperase®, Savinase®, respectively) as disclosed in WO 89/06279; subtilisin from Bacillus lentus as disclosed in WO 91/02792, such as from Bacillus lentus DSM 5483 or the variants of Bacillus lentus DSM 5483 as described in WO 95/23221; subtilisin from Bacillus alcalophilus (DSM 11233) disclosed in DE 10064983; subtilisin from Bacillus gibsonii (DSM 14391) as disclosed in WO 2003/054184; sub tilisin from Bacillus sp.
  • DSM 11233 subtilisin from Bacillus alcalophilus
  • DSM 14391 subtilisin from Bacillus gibsonii
  • Examples of useful proteases in accordance with the present invention comprise the variants described in: WO 92/19729, WO 95/23221, WO 96/34946, WO 98/20115, WO 98/20116, WO 99/11768, WO 01/44452, WO 02/088340, WO 03/006602, WO 2004/03186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2011/036264, and WO 2011/072099.
  • Suitable exam ples comprise especially variants of subtilisin protease derived from SEQ ID NO:22 as de scribed in EP 1921147 (which is the sequence of mature alkaline protease from Bacillus lentus DSM 5483) with amino acid substitutions in one or more of the following positions: 3, 4, 9, 15,
  • At least one protease has a sequence according to SEQ ID NO:22 as de scribed in EP 1921147, or a protease which is at least 80% identical thereto and has proteolytic activity.
  • said protease is characterized by having amino acid glutamic acid (E), or aspartic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity.
  • At least one protease has a sequence according to SEQ ID NO:22 as de- scribed in EP 1921147, or a protease which is at least 80% identical thereto and comprises a glutamic acid (E) at position 101 (according to BPN’ numbering) and has proteolytic activity.
  • said protease is characterized by having amino acid glutamic acid (E), or as partic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity.
  • said protease comprises one or more further substitutions: (a) threonine at position 3 (3T), (b) isoleucine at position 4 (4I), (c) alanine, threonine or arginine at position 63 (63A, 63T, or 63R), (d) aspartic acid or glutamic acid at position 156 (156D or 156E), (e) proline at position 194 (194P), (f) methionine at position 199 (199M), (g) isoleucine at position 205 (205I), (h) aspartic acid, glutamic acid or glycine at position 217 (217D, 217E or217G), (i) combinations of two or more amino acids according to (a) to (h).
  • At least one protease may be at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and is characterized by comprising one amino acid (according to (a)-(h)) or combina tions according to (i) together with the amino acid 101 E, 101 D, 101 N, 101Q, 101A, 101G, or 101S (according to BPN’ numbering).
  • said protease is characterized by comprising the mutation (according to BPN’ numbering) R101E, or S3T + V4I + V205I, or R101E and S3T, V4I, and V205I, or S3T + V4I + V199M + V205I + L217D, and having proteo lytic activity.
  • protease according to SEQ ID NO:22 as described in EP 1921147 is char acterized by comprising the mutation (according to BPN’ numbering) S3T + V4I + S9R + A15T + V68A + D99S + R101S + A103S + 1104V + N218D, and having proteolytic activity.
  • the inventive composition may comprise a combination of at least two proteases, preferably selected from the group of serine endopeptidases (EC 3.4.21), more preferably selected from the group of subtilisin type proteases (EC 3.4.21.62) - all as disclosed above.
  • inventive compositions comprise at least one man- nanase.
  • the mannanase is an endo-1,4 ⁇ -mannosidase (EC 3.2.1.78).
  • a polypeptide having mannan degrading activity or mannanase activity may be tested for ac cording to standard test procedures known in the art, such as by applying a solution to be tested to 4 mm diameter holes punched out in agar plates containing 0.2% AZCL galactomannan (car- ob), i.e. substrate for the assay of endo-1,4-beta-D-mannanase available as CatNo. I-AZGMA from the company Megazyme (Megazyme's Internet address: http://www. megazyme. com/Purchase/index. html).
  • Mannan degrading activity may be tested in a liquid assay using carob galactomannan dyed with Remazol Brilliant Bue as described in McCleary, B. V.
  • At least one mannanase comprised in the composition of the invention may be selected from alkaline mannanase of Family 5 or 26.
  • alkaline mannanase is meant to encompass mannanases having an enzymatic activity of at least 40% of its maximum activity at a given pH ranging from 7 to 12, preferably 7.5 to10.5.
  • At least one mannanase comprised in the composition of the invention may be selected from mannanases originating from Bacillus organisms, such as described in JP-0304706, JP- 63056289, JP-63036774, JP-08051975, WO 97/11164, WO 91/18974, WO 97/11164,
  • Suitable mannanases are further described in WO 99/064619.
  • the man nanase may be selected from mannanases originating from Trichoderma organisms, such as disclosed in WO 93/24622.
  • At least one mannanase may be selected from a commercially available mannanase such as Mannaway® (Novozymes A/S) (SEQ ID NO: 1 of W02009074685).
  • inventive compositions comprise at least one am ylase.
  • Amylases according to the invention (alpha and/or beta) include those of bacterial or fungal origin (EC 3.2.1.1 and 3.2.1.2, respectively).
  • component (b) comprises at least one enzyme selected from the group of alpha-amylases (EC 3.2.1.1). Chemically modified or protein engineered mutants are included.
  • Amylases according to the invention have “amylolytic activity” or “amylase activity” involving (endo)hydrolysis of glucosidic linkages in polysaccharides alpha-amylase activity may be de termined by assays for measurement of alpha-amylase activity which are known to those skilled in the art. Examples for assays measuring alpha-amylase activity are: alpha-amylase activity can be determined by a method employing Phadebas tablets as sub strate (Phadebas Amylase Test, supplied by Magle Life Science). Starch is hydrolyzed by the alpha-amylase giving soluble blue fragments.
  • the absorbance of the resulting blue solution, measured spectrophotometrically at 620 nm, is a function of the alpha-amylase activity.
  • the measured absorbance is directly proportional to the specific activity (activity/mg of pure alpha- amylase protein) of the alpha-amylase in question under the given set of conditions.
  • Alpha-amylase activity can also be determined by a method employing the Ethyliden-4- nitrophenyl-alpha-D-maltoheptaosid (EPS).
  • EPS Ethyliden-4- nitrophenyl-alpha-D-maltoheptaosid
  • D-maltoheptaoside is a blocked oligosaccharide which can be cleaved by an endo-amylase.
  • kits containing EPS sub strate and alpha-glucosidase is manufactured by Roche Costum Biotech (cat. No. 10880078103).
  • the slope of the time dependent absorption-curve is directly proportional to the specific activity (activity per mg enzyme) of the alpha-amylase in question under the given set of conditions.
  • Amylolytic activity may be provided in units per gram enzyme.
  • 1 unit alpha- amylase may liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20°C.
  • At least one amylase is selected from:
  • Suitable variants of SEQ ID NO:6 include those comprising a deletion in positions 181 and/or 182 and/or a substitution in position 193.
  • Pre ferred variants of SEQ NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216 and K269.
  • amylases from Bacillus sp. comprising amino acids 1 to 485 of SEQ ID NO:2 as described in WO 00/60060.
  • amylases from Bacillus amyloliquefaciens or variants thereof, preferably selected from amylases according to SEQ ID NO: 3 as described in WO 2016/092009.
  • amylases having SEQ ID NO:1 as described in WO 2013/001078 or amylase vari ants comprising an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and
  • amylases having SEQ ID NO:2 as described in WO 2013/001087 or amylase vari ants comprising a deletion of positions 181+182, or 182+183, or 183+184, within said SEQ ID NO:2, optionally comprising one or two or more modifications in any of positions corresponding to WHO, W159, W167, Q169, W189, E194, N260, F262, W284, F289, G304, G305, R320, W347, W439, W469, G476 and G477 within said SEQ ID NO:2.
  • amylases which are hybrid alpha-amylases from above mentioned amylases as for exam ple as described in WO 2006/066594;
  • hybrid amylases according to WO 2014/183920 with A and B domains having at least 90% identity to SEQ ID NO:2 of WO 2014/183920 and a C domain having at least 90% identity to SEQ ID NO:6 of WO 2014/183920, wherein the hybrid amylase has amylolytic activity; preferably the hybrid alpha-amylase is at least 95% identical to SEQ ID NO: 23 of WO 2014/183920 and having amylolytic activity;
  • hybrid amylase has amylolytic activity; preferably, the hybrid alpha-amylase is at least 95% identical to SEQ ID NO: 30 as disclosed in WO 2014/183921 and having amylolytic activity.
  • Suitable amylases include also those, which are variants of the above described amylases which have amylolytic activity.
  • amylase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • amylase variants having amylolytic activity are at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • the invention relates to amylase variants comprising conservative mu tations not pertaining the functional domain of the respective amylase.
  • Amylase variants of this embodiment having amylolytic activity may be at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar to the full length polypeptide sequence of the parent enzyme.
  • amylase variants have amylolytic activity according to the present invention when said amylase variants exhibit increased amylolytic activity when compared to the par ent amylase.
  • amylase variants have amylolytic activity according to the present invention when said amylase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the amylolytic activity of the respective parent amylase.
  • At least one amylase is selected from commercially available amylases which include but are not limited to products sold under the trade names DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, NatalaseTM, Liq uozyme X and BANTM, AmplifyTM, Amplify PrimeTM (from Novozymes A/S), and RapidaseTM, PurastarTM, PoweraseTM, EffectenzTM (M100 from DuPont), PreferenzTM (S1000, S110 and F1000; from DuPont), PrimaGreenTM (ALL; DuPont), OptisizeTM (DuPont).
  • commercially available amylases which include but are not limited to products sold under the trade names DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, NatalaseTM, Liq uozyme X and BANTM, AmplifyTM,
  • At least one enzyme comprised in the composition of the invention may be selected from the group of cellulases.
  • Cellulases according to the invention include those of bacterial or fungal origin.
  • At least one cellulase comprised in the composition of the invention may be selected from cellobiohydrolase (1,4-P-D-glucan cellobiohydrolase, EC 3.2.1.91), endo-ss-1 ,4-glucanase (EC 3.2.1.4) and ss-glucosidase (EC 3.2.1.21).
  • Endoglucanases of EC class 3.2.1.4 may be named endoglucanase, endo-1,4-ss-D-glucan 4-glucano hydrolase, endo-1 ,4-beta-glucanase, carboxymethyl cellulase, and beta-1, 4-glucanase.
  • Endoglucanases may be classified by amino acid sequence similarities (Henrissat, B. Accessed at UniProt 10/26/2011) under family 5 containing more than 20 endoglucanases of EC 3.2.1.4. Reference is also made to T.-M. Enveri, "Microbial Cellulases” in W.M. Fogarty, Microbial En zymes and Biotechnology, Applied Science Publishers, p. 183-224 (1983); Methods in Enzy- mology, (1988) Vol. 160, p. 200-391 (edited by Wood, W.A. and Kellogg, S.T.); Beguin, P., "Mo lecular Biology of Cellulose Degradation", Annu. Rev. Microbiol. (1990), Vol.
  • At least one cellulase comprised in the composition of the invention is selected of the glycosyl hydrolase family 7 (GH7, pfam00840), preferably selected from endoglucanases (EC 3.2.1.4).
  • GH7, pfam00840 glycosyl hydrolase family 7
  • endoglucanases EC 3.2.1.4
  • Cellulases “cellulase enzymes” or “cellulolytic enzymes” according to the invention are en zymes involved in hydrolysis of cellulose. Assays for measurement of “cellulase activity” or “cel lulolytic activity” are known to those skilled in the art. For example, cellulolytic activity may be determined by virtue of the fact that cellulase hydrolyses carboxymethyl cellulose to reducing carbohydrates, the reducing ability of which is determined colorimetrically by means of the ferri- cyanide reaction, according to Hoffman, W. S., J. Biol. Chem. 120, 51 (1937).
  • Cellulolytic activity may be provided in units per gram enzyme. For example, 1 unit may liberate 1.0 pmole of glucose from cellulose in one hour at pH 5.0 at 37°C (2 hour incubation time).
  • At least one cellulase comprised in the composition of the invention is se lected from cellulases comprising a cellulose binding domain. In one embodiment, at least one cellulase is selected from cellulases comprising a catalytic domain only, meaning that the cellu lase lacks cellulose binding domain.
  • composition of the invention comprises at least one endoglucanases of EC class 3.2.1.4 is originating from
  • Bacillus such as Bacillus sp. CBS 670.93 and CBS 669.93
  • Melanocarpus such as Melanocarpus albomyces as disclosed in WO 97/14804
  • Clostridium e.g. Clostridium thermocellum
  • Humicola such as Humicola insolens (DSM1800) as disclosed in EP 0495257, EP 0531315, EP 0531372, US 4435307, US 5648263, US 5776757, WO 89/09259, WO 91/17244, WO 94/07998 (sequence displayed in figure 1 “43kd human variants there of), WO 95/24471, WO 96/11262 and WO 98/12307.
  • Fusarium such as Fusarium oxysporum e.g. strain J79 (DSM2672) as disclosed in EP 0495257, EP 0531315, EP 0531372, US 5648263, US 5776757, WO 89/09259, WO 91/17244, WO 95/24471 and WO 96/11262
  • Thielavia such as Thielavia terrestris or Myceliophthora thermophila strain CBS 11765 as disclosed in EP 0531315, US 5648263, US 5776757, WO 89/09259, WO 91/17244, WO 95/24471, WO 96/11262, WO 96/29397 (SEQ ID NO: 9 and variants thereof), and WO 98/12307.
  • Trichoderma such as Trichoderma reesei, Trichoderma longibrachiatum or Trichoderma harzianum as disclosed in EP 1305432, EP 1240525, WO 92/06165, WO 94/21801, WO 94/26880, WO 95/02043, WO 95/24471 and WO 02/099091.
  • Aspergillus such as Aspergillus aculeatus as disclosed in WO 93/17244
  • Acremonium such as Acremonium sp., Acremonium persicinum, Acremonium acremonium, Acremonium brachypenium, Ac remoni- um dichromosporum, Acremonium obclavatum, Acremonium pinkertoniae, Acremonium roseogriseum, Acremonium incoloratum, and Acremonium furatum as disclosed in WO 96/11262 and WO 96/29397 (SEQ ID NO: 5 and variants thereof).
  • Cellvibrio such as Cellvibrio mixtus DSM 11683, Cellvibrio mixtus DSM 11684, Cellvibrio mixtus DSM 11685, Cellvibrio mixtus ACM
  • Suitable cellulases include also those, which are variants of the above described cellulases which have cellulolytic activity.
  • cellulase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • cellulase variants having cellulolytic activi ty are at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar and/or identical to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • the composition of the invention comprises a Humicola insolens DSM 1800 cellulase complex having endoglucanase, cellobiohydrolase and beta-glucosidase activi ty.
  • the composition of the invention comprises at least one Humicola insolens DSM 1800 endoglucanase (EC 3.2.1.4) having the amino acid se quence disclosed in Fig. 14A-E of WO 91/17244, preferably amino acids 20-434 according said sequence, more preferably having one or more substitutions at positions selected from 182,
  • the endoglucanase is at least 80% similar and/or identical to a polypeptide according to SEQ ID NO: 2 of WO 95/02675.
  • the composition of the invention comprises at least a Bacillus sp. cellulase (EC 3.2.1.4) selected from a polypeptide at least 80% similar and/or identical to the amino acid sequence of position 1 to position 773 of SEQ ID NO: 2 of WO 2004/053039 or a catalytically active fragment thereof.
  • the composition of the invention comprises at least a Thielavia terrestris cellulase (EC 3.2.1.4) having a polypeptide at least 80% similar and/or identical to the amino acid sequence of position 1 to position 299 of SEQ ID NO: 4 of WO 2004/053039 or a catalytically active fragment thereof.
  • cellulase variants have cellulolytic activity according to the present inven tion when said cellulase variants exhibit increased cellulolytic activity when compared to the parent cellulase.
  • cellulase variants have cellulolytic activity according to the present inven tion when said cellulase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the cellulolytic activity of the respective parent cellulase.
  • At least one cellulase may be selected from Renozyme®, Celluzyme®, Celluclean®, Endolase® and Carezyme® (Novozymes A/S), ClazinaseTM, and Puradax HATM (Genencor Int. Inc.), and KAC-500(B)TM (Kao Corporation).
  • At least one peroxidases may be selected from GuardzymeTM (Novozymes A/S).
  • At least one enzyme comprised in the composition of the invention may be a nuclease.
  • the nuclease is selected from the group of DNA degrading enzymes (DNAse). Said en zymes usually catalyzes the hydrolytic cleavage of phosphodiester linkages in DNA.
  • the DNAses are classified e.g. in E.C. 3.1.11, E.C. 3.1.12, E.C. 3.1.15, E.C. 3.1.16, E.C.
  • DNAse activity may be determined on DNAse Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), which should be prepared according to the manual from supplier. Briefly, 21 g of agar is dissolved in 500 ml water and then autoclaved for 15 min at 121 °C. Autoclaved agar is temperated 10 to 48°C in water bath, and 20 ml of agar is to be poured into petridishes with and allowed to solidify by incubation o/n at room temperature. On solidified agar plates, 5 pi of enzyme solution is added and DNAse activity is observed as colorless zones around the spot ted enzyme solutions.
  • DNAse Test Agar with Methyl Green BD, Franklin Lakes, NJ, USA
  • DNAse activity may be determined by using the DNAseAlertTM Kit (11-02-01-04,
  • At least one DNAse comprised in the composition of the invention may be selected from DNAses originating from Bacillus such as from Bacillus cibi, Bacillus horikoshii, Bacillus horneckiae, Bacillus idriensis, Bacillus algicola, B acillus vietnamensis, Bacillus hwajinpoensis, Paenibacillus mucilanginosus, Bacillus indi- cus, Bacillus luciferensis, Bacillus marisflavr, and variants thereof.
  • at least one DNAse comprised in the composition of the invention is selected from polypeptides 80% identical to SEQ ID NO: 1 of WO 2019/081724.
  • Said polypeptide may comprise one or more substitutions at positions selected from T1, G4, S7, K8, S9, S13, N16, T22, S25, S27, D32, L33, S39, G41 , S42, D45, Q48, S57, S59, N61, T65, S66, V76, F78, P91, S101, S106, Q109, A112, S116, T127, S130, T138, Q140, S144, A147, C148, W154, T157, Y159, G162, S167, Q174, G175, L177, S179, and C180 - all as disclosed in WO 2019/081724 and WO 2019/081721.
  • composition of the invention may comprise DNAse variants having DNA degrading activity which are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar and/or identical when compared to the full-length polypeptide sequence of the cor responding parent enzyme as disclosed above.
  • composition of the invention may comprise a combina tion of at least two DNAses.
  • At least one enzyme may be selected from acyltransferases (E.C 2.3.1) or perhydrolases.
  • Perhydrolases catalyze perhydrolysis reaction that results in the production of a peracid from a carboxylic acid ester (acyl) substrate in the presence of a source of peroxygen (e.g., hydrogen peroxide). While many enzymes perform this reaction at low levels, perhydrolases exhibit a high perhydrolysis: hydrolysis ratio, often greater than 1.
  • Suitable perhydrolases may be of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • acyltransferases with homology to Candida antarctica lipase A (WO 2010/111143) and naturally occur ring Mycobacterium perhydrolase enzymes, or variants thereof - e.g. a variant of Mycobacterium smegmatis as described in WO 2005/056782, WO 2008/063400, US 2008145353, and US 2007167344; perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant (WO 2010/100028).
  • oxidore- ductase enzymes may be employed.
  • the catalyzed reaction is the transfer of electrons from the organic substrate, for the glucose oxidase, for example, from the glucose, to the oxygen as the electron acceptor with the formation of the desired hydrogen peroxide.
  • Peroxidase activity may be measured by the ABTS method as described in Childs et al. 1975 (Biochemical J, 145, p. 93-103) and commercial kits are available from different suppliers. Other measuring methods are known to those known in the art.
  • the hydrogen peroxide-producing oxidoreductases herein concern enzymes that produce hy drogen peroxide, using oxygen as an electron acceptor.
  • particularly preferred oxidoreductases include those of the EC classes E.C. 1.1.3 (CH — OH as the electron donor), E.C. 1.2.3 (aldehyde or oxo groups as the electron donor), E.C. 1.4.3 (CH — NH2 as the donor), E.C. 1.7.3 (N-containing groups as the donor) and E.C. 1.8.3 (S-containing groups as the do nor) come into consideration, wherein enzymes of the EC class EC 1.1.3.
  • the hydrogen peroxide-producing oxidoreductase is one in which a sugar is used as the electron donor.
  • the hydrogen peroxide-producing and sugar-oxidizing oxi doreductase is preferably chosen from glucose oxidase (EC 1.1.3.4), hexose oxidase (EC 1.1.3.5), galactose oxidase (EC 1.1.3.9) and pyranose oxidase (EC 1.1.3.10).
  • glucose oxidase EC 1.1.3.4 is particularly preferred.
  • aromatic compounds are added that interact with the enzymes to enhance the activity of the oxidoreduc tases (Enhancer) or to facilitate electron flow (Mediators) between the oxidizing enzymes and the stains over strongly different redox potentials.
  • At least one enzyme may be selected from oxidases such as amino acid oxidase and polyol oxidase (e.g., WO 2008/051491). Oxidases and their corresponding substrates may be used as hydrogen peroxide generating enzyme systems, and thus a source of hydrogen peroxide. Several enzymes, such as peroxidases, haloperoxidases and perhydrolases, require a source of hydrogen peroxide. By studying EC 1.1.3._, EC 1.2.3._, EC 1.4.3._, and EC 1.5.3._ or simi lar classes (under the International Union of Biochemistry), other examples of such combina tions of oxidases and substrates are easily recognized by one skilled in the art.
  • oxidases such as amino acid oxidase and polyol oxidase (e.g., WO 2008/051491).
  • Oxidases and their corresponding substrates may be used as hydrogen peroxide generating enzyme systems, and thus a source
  • At least one oxidoreductase is chosen from enzymes that use peroxides as the electron accepter (EC-Classes 1.11 or 1.11.1), in particular, from catalases (EC 1.11.1.6), peroxidases (EC 1.11.1.7), glutathione peroxidases (EC 1.11.1.9), chloride peroxidases (EC 1.11.1.10), manganese peroxidases (EC 1.11.1.13) and/or lignin peroxidases (EC 1.11.1.14), which can also be generally classified under the term peroxidases.
  • Examples of use ful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, WO 98/10060 and WO 98/15257.
  • a peroxidase for use in the invention also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase is a chloroperoxidase.
  • the haloperoxidase is a vanadium haloperoxidase, i.e. , a vanadate-containing haloperoxidase.
  • the vanadate-containing haloperoxidase is com bined with a source of chloride ion.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • Haloperoxidases h ave also been isolated from bacteria such as Pseudomonas, e.g. P. pyrrocinia, and Streptomyces, e.g. S. aureofaciens.
  • the haloperoxidase is from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartlebii as described in WO 2001/79459, Dendryphiella salina as described in
  • peroxidases include GuardzymeTM (Novozymes A/S), PrimaGreenTM Oxy (DuPont).
  • At least one enzyme may be selected from laccases.
  • laccase activity is defined here in as covered by enzyme classification EC 1.10.3.2, or a similar activity, such as a catechol oxi dase activity (EC 1.10.3.1), o-aminophenol oxidase activity (EC 1.10.3.4), or bilirubin oxidase activity (EC 1.3.3.5), that catalyzes the oxidation of a substrate using molecular oxygen.
  • EC 1.10.3.1 catechol oxi dase activity
  • EC 1.10.3.4 o-aminophenol oxidase activity
  • bilirubin oxidase activity EC 1.3.3.5
  • Preferred laccase enzymes are enzymes of microbial origin.
  • the enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts; e.g. Polyporus radiata (WO 92/01046), Coriolus hirsutus (JP 2238885), Coprinopsis cinerea (WO 97/08325), Myceliophthora thermophila (WO 95/33836)).
  • laccase is selected from those as described in SEQ ID NO: 2, 4, 6, and 8 of WO 2009/127702 and variants thereof.
  • At least one laccase may be selected from commercially available laccase Denilite® 1 and 2 from Novozymes.
  • at least one enzyme is selected from lyases.
  • “Lyase” may be a pectate ly ase derived from Bacillus, particularly B. licheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6,124,127, WO 99/027083, WO 99/027084,
  • pectate lyases are XpectTM, PectawashTM and PectawayTM (Novozymes A/S); PrimaGreenTM, EcoScour (DuPont).
  • At least one enzyme is selected from the group of pectinases (EC 3.2.1.15 gycosidase), and/or arabinases (EC 3.2.1.99), and/or galactanases (EC 3.2.1.89 and EC 3.2.1.181), and/or xylanases (EC 3.2.1.8, EC 3.2.1.32, EC 3.2.1.136, and EC 3.2.1.156).
  • pectinases EC 3.2.1.15 gycosidase
  • arabinases EC 3.2.1.99
  • galactanases EC 3.2.1.89 and EC 3.2.1.181
  • xylanases EC 3.2.1.8, EC 3.2.1.32, EC 3.2.1.136, and EC 3.2.1.156.
  • Combination of different enzymes can also be used. Any combination of the enzymes cited above can be used.
  • the combination of enzymes can include several enzymes of a different class, several different enzymes of the same class, and combinations thereof.
  • the combination of enzymes is selected from the group consisting of amylase, protease, lipase, mannanase, nuclease, and cellulase; protease, lipase, mannanase, and cellulase; protease, lipase, and mannanase; protease and lipase; protease and mannanase, preferably the combi nation of enzymes is protease, lipase, and mannanase.
  • compositions for example 1 to 2% by weight of protease and 0.1 to 0.5% by weight of lipase, both referring to the total weight of the composition.
  • a combination of lipase, protease and a man nanase in the compositions for example 1 to 2% by weight of protease, 0.1 to 0.5% by weight of lipase and 0.1 to 0.5% by weight of mannanase, all referring to the total weight of the compo sition.
  • a protease in the compositions for example 1 to 2% by weight of protease.
  • lipase and/or protease and/or mannanase is deemed called stable when its enzymatic activity “available in application” equals at least 60% when compared to the initial enzymatic activity before storage.
  • An enzyme may be called stable within this invention if its enzymatic activity available in application is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% when compared to the initial enzymatic activity before storage.
  • an enzyme is stable accord- ing to the invention when essentially no loss of enzymatic activity occurs during storage, i.e. loss in enzymatic activity equals 0% when compared to the initial enzymatic activity before stor age.
  • loss in enzymatic activity equals 0% when compared to the initial enzymatic activity before stor age.
  • Essentially no loss of enzymatic activity within this invention may mean that the loss of enzymatic activity is less than 30%, less than 25%, less than 20%, less than 15%, less than 10%, less than 9%, less than 8%, less than 7%, less than 6%, less than 5%.
  • the present invention is directed to a detergent composition
  • a detergent composition comprising (A) at least one polymer comprising
  • X 1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, preferred are methyl and more preferred is hydrogen, n is in the range of from 1 to 4,
  • (B) at least one enzyme preferably selected from the group consisting of amylase, protease, lipase, mannanase, xylanase, nuclease, cellulase, and combinations thereof; preferably at least one protease, and optionally, at least one lipase, and optionally at least one man nanase; preferably at least one protease, and at least one lipase, and optionally at least one mannanase; preferably at least one protease, and at least one lipase, and at least one mannanase.
  • the detergent composition can be solid or liquid.
  • the detergent composition is liquid.
  • inventive compositions can be used in laundry and/or hard surface cleaning, both either in home care or l&l applications, with hard surface cleaning being dish washing (manual (hand) dish washing or automated dish washing), but also meaning cleaning of hard surfaces inside a washing machine (dishwashing or laundry washing machine, preferably laundry washing machine).
  • inventive compositions comprise at least one sur factant (C).
  • the surfactant can be selected from anionic surfactant, cationic surfactant, non ionic surfactant, amphoteric surfactants, amine oxide surfactants, and combinations thereof, preferably, the surfactant is an anionic surfactant.
  • anionic surfactants are alkali metal and ammonium salts of Cs-Cis-alkyl sulfates, of Cs-Ci 8 -fatty alcohol polyether sulfates, of sulfuric acid half-esters of ethoxylated C4-C12- alkylphenols (ethoxylation: 1 to 50 mol of ethylene oxide/mol), C12-C18 sulfo fatty acid alkyl esters, for example of C12-C18 sulfo fatty acid methyl esters, furthermore of Ci2-Ci8-alkylsulfonic acids and of Cio-Ci 8 -alkylarylsulfonic acids.
  • anionic surfactants are soaps, for example the sodium or potassium salts of stearic acid, oleic acid, palmitic acid, ether carboxylates, and alkylether phosphates.
  • anionic surfactant is selected from com pounds according to general formula (II)
  • R 1 n-Cio-Ci 8 -alkyl especially with an even number of carbon atoms, for example n-decyl, n- dodecyl, n-tetradecyl, n-hexadecyl, or n-octadecyl, preferably Cio-Ci4-alkyl, and even more preferably n-Ci2-alkyl, x being a number in the range of from 1 to 5, preferably 2 to 4 and even more preferably 3.
  • M being selected from alkali metals, preferably potassium and even more preferably sodium.
  • x may be an average number and therefore n is not necessarily a whole number, while in individual molecules according to formula (I), x denotes a whole number.
  • inventive compositions may contain 0.1 to 60 % by weight of anionic surfactant, preferably 5 to 50 % by weight.
  • compositions may comprise ingredients other than the aforementioned.
  • examples are non-ionic surfactants, fragrances, dyestuffs, biocides, preservatives, enzymes, hydrotropes, builders, viscosity modifiers, polymers, buffers, defoamers, and anti-corrosion additives.
  • Preferred inventive compositions may contain one or more non-ionic surfactants.
  • Preferred non-ionic surfactants are alkoxylated alcohols, di- and multiblock copolymers of eth ylene oxide and propylene oxide and reaction products of sorbitan with ethylene oxide or pro pylene oxide, alkyl polyglycosides (APG), hydroxyalkyl mixed ethers and amine oxides.
  • alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds of the general formula (III a) in which the variables are defined as follows:
  • R 2 is identical or different and selected from hydrogen and linear Ci-Cio-alkyl, preferably in each case identical and ethyl and particularly preferably hydrogen or methyl,
  • R 3 is selected from Cs-C22-alkyl, branched or linear, for example n-CsH ⁇ , n-CioHbi, n-Ci2H25, n-C 14 H 29 , n-C 16 H 33 or n-CisH37,
  • R 4 is selected from Ci-Cio-alkyl, methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, isopentyl, sec-pentyl, neopentyl, 1,2-dimethylpropyl, isoamyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl or isodecyl,
  • e and f are in the range from zero to 300, where the sum of e and f is at least one, preferably in the range of from 3 to 50.
  • e is in the range from 1 to 100 and f is in the range from 0 to 30.
  • compounds of the general formula (II) may be block copolymers or random copolymers, preference being given to block copolymers.
  • alkoxylated alcohols are, for example, compounds of the general formula (III b) in which the variables are defined as follows:
  • R 2 is identical or different and selected from hydrogen and linear Ci-Co-alkyl, preferably iden tical in each case and ethyl and particularly preferably hydrogen or methyl,
  • R 5 is selected from C6-C2o-alkyl, branched or linear, in particular n-CsH ⁇ , n-CioHbi, n-Ci2H25, n-C 13 H 27 , n-Ci5H3i, n-Ci4H29, n-Ci6H33, n-CisH37, a is a number in the range from zero to 10, preferably from 1 to 6, b is a number in the range from 1 to 80, preferably from 4 to 20, d is a number in the range from zero to 50, preferably 4 to 25.
  • the sum a + b + d is preferably in the range of from 5 to 100, even more preferably in the range of from 9 to 50.
  • Compounds of the general formula (III) may be block copolymers or random copolymers, pref erence being given to block copolymers.
  • nonionic surfactants are selected from di- and multiblock copolymers, com posed of ethylene oxide and propylene oxide. Further suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Amine oxides or alkyl polyglycosides, espe cially linear C4-Ci6-alkyl polyglucosides and branched Cs-Cn-alkyl polyglycosides such as com pounds of general average formula (IV) are likewise suitable. wherein:
  • R 6 is CrC4-alkyl, in particular ethyl, n-propyl or isopropyl,
  • R 7 is -(CH 2 )2-R 6 ,
  • G 1 is selected from monosaccharides with 4 to 6 carbon atoms, especially from glucose and xylose, y in the range of from 1.1 to 4, y being an average number,
  • non-ionic surfactants are compounds of general formula (V) and (VI) AO is selected from ethylene oxide, propylene oxide and butylene oxide,
  • EO is ethylene oxide, CH2CH2-O,
  • R 8 selected from Cs-Cis-alkyl, branched or linear, and R 5 is defined as above.
  • a 3 0 is selected from propylene oxide and butylene oxide
  • w is a number in the range of from 15 to 70, preferably 30 to 50
  • w1 and w3 are numbers in the range of from 1 to 5
  • w2 is a number in the range of from 13 to 35.
  • Mixtures of two or more different nonionic surfactants selected from the foregoing may also be present.
  • surfactants that may be present are selected from amphoteric (zwitterionic) surfactants and anionic surfactants and mixtures thereof.
  • amphoteric surfactants are those that bear a positive and a negative charge in the same molecule under use conditions.
  • Preferred examples of amphoteric surfactants are so- called betaine-surfactants.
  • Many examples of betaine-surfactants bear one quaternized nitrogen atom and one carboxylic acid group per molecule.
  • a particularly preferred example of amphoter ic surfactants is cocamidopropyl betaine (lauramidopropyl betaine).
  • amine oxide surfactants are compounds of the general formula (VII)
  • R 9 is selected from C8-C20- alkyl or C2-C4-alkylene Cio-C2o-alkylamido and R 10 and R 11 are both methyl.
  • a particularly preferred example is lauryl dimethyl aminoxide, sometimes also called lauramine oxide.
  • a further particularly preferred example is cocamidylpropyl dimethylaminoxide, some times also called cocamidopropylamine oxide.
  • inventive compositions may contain 0.1 to 60 % by weight of at least one surfactant, selected from non-ionic surfactants, amphoteric surfactants and amine oxide surfactants.
  • inventive solid detergent compositions for cleaners and especially those for automatic dishwashing do not contain any anionic surfactant.
  • compositions may contain at least one bleaching agent, also referred to as bleach.
  • Bleaching agents may be selected from chlorine bleach and peroxide bleach, and peroxide bleach may be selected from inorganic peroxide bleach and organic peroxide bleach.
  • Preferred are inorganic peroxide bleaches, selected from alkali metal percarbonate, alkali metal perborate and alkali metal persulfate.
  • organic peroxide bleaches are organic percarboxylic acids, especially organic per- carboxylic acids.
  • alkali metal percarbonates especially sodium percarbonates
  • Such coatings may be of organic or inorganic nature. Examples are glycerol, sodium sulfate, silicate, sodium carbonate, and combinations of at least two of the foregoing, for example combinations of sodium carbonate and sodium sulfate.
  • Suitable chlorine-containing bleaches are, for example, 1,3-dichloro-5,5-dimethylhydantoin, N-chlorosulfamide, chloramine T, chloramine B, sodium hypochlorite, calcium hypochlorite, magnesium hypochlorite, potassium hypochlorite, potassium dichloroisocyanurate and sodium dichloroisocyanurate.
  • compositions may comprise, for example, in the range from 3 to 10% by weight of chlorine-containing bleach.
  • Inventive compositions may comprise one or more bleach catalysts.
  • Bleach catalysts can be selected from bleach-boosting transition metal salts or transition metal complexes such as, for example, manganese-, iron-, cobalt-, ruthenium- or molybdenum-salen complexes or carbonyl complexes.
  • Manganese, iron, cobalt, ruthenium, molybdenum, titanium, vanadium and copper complexes with nitrogen-containing tripod ligands and also cobalt-, iron-, copper- and rutheni um-amine complexes can also be used as bleach catalysts.
  • compositions may comprise one or more bleach activators, for example N- methylmorpholinium-acetonitrile salts (“MMA salts”), trimethylammonium acetonitrile salts, N- acylimides such as, for example, N-nonanoylsuccinimide, 1,5-diacetyl-2,2-dioxohexahydro- 1,3,5-triazine (“DADHT”) or nitrile quats (trimethylammonium acetonitrile salts).
  • MMA salts N- methylmorpholinium-acetonitrile salts
  • DADHT 1,5-diacetyl-2,2-dioxohexahydro- 1,3,5-triazine
  • DADHT 1,5-diacetyl-2,2-dioxohexahydro- 1,3,5-triazine
  • nitrile quats trimethylammonium acetonitrile salts
  • TAED tetraacetylethylenediamine
  • TAED tetraacetylhexylenediamine
  • fragrances are benzyl salicylate, 2-(4-tert.-butylphenyl) 2-methylpropional, com suddenly available as Lilial®, and hexyl cinnamaldehyde.
  • dyestuffs are Acid Blue 9, Acid Yellow 3, Acid Yellow 23, Acid Yellow 73, Pigment Yellow 101, Acid Green 1, Solvent Green 7, and Acid Green 25.
  • Inventive compositions may contain one or more preservatives or biocides.
  • Biocides and pre servatives prevent alterations of inventive liquid detergent compositions due to attacks from microorganisms.
  • some biocides, as part of the laundry detergent compositions may help to kill or deactivate or prevent growth or prevent biofilm formation of microorganisms on the textiles and clothes that are washed or on surfaces inside the washing machine.
  • biocides and preservatives examples include BTA (1,2,3- benzotriazole), benzalkonium chlorides, 1,2-benzisothiazolin-3-one (“BIT”), 2-methyl-2H- isothiazol-3-one StammMIT“) and 5-chloro-2-methyl-2H-isothiazol-3-one facedCIT“), benzoic acid, sorbic acid, iodopropynyl butylcarbamate (“IPBC”), dichlorodimethylhydantoine (“DCDMH”), bromo- chlorodimethylhydantoine (“BCDMH”), and dibromodimethylhydantoine (“DBDMH”).
  • BTA 1,2,3- benzotriazole
  • benzalkonium chlorides 1,2-benzisothiazolin-3-one
  • BIT 1,2-benzisothiazolin-3-one
  • 2-methyl-2H- isothiazol-3-one such as 2-methyl-2H- isothiazol-3-one
  • the preservative or biocide is selected from the group consisting of 2- phenoxyethanol, glutaraldehyde, 2-bromo-2-nitropropane-1,3-diol, formic acid in acid form or as its salt, 4,4’-dichloro 2-hydroxydiphenyl ether, and combinations thereof.
  • the preservative or biocide is added to the composition in a concentration of 0.0001 to 10% relative to the total weight of the composition.
  • the preservative or biocide is selected from the group consisting of
  • DBNPA 2.2-dibromo-2-cyanoacetamide
  • DTBMA 2,2'-dithiobis[N-methylbenzamide]
  • DTBMA 2-bromo-2-(bromomethyl)pentanedinitrile
  • BBIT 2-butyl-benzo[d]isothiazol-3-one
  • Biphenyl -2-ol, and its salts o-phenylphenol, MEA-o-phenylphenate, potassium phenylphenate, sodium phenylphenate;
  • Didecyldimethylammonium chloride (DDAC, CAS No. 68424-95-3 and CAS No. 7173-51-5); Dodecylguanidine monohydrochloride (CAS No 13590-97-1); Ethanol (CAS. No 64-17-5); n-propanol (1 -propanol, CAS No. 71-23-8)
  • Hexa-2,4-dienoic acid (Sorbic acid, CAS No. 110-44-1) and its salts, e.g. calcium sorbate, sodi um sorbate
  • Peracetic acid (CAS No. 79-21-0); polyhexamethylene biguanide hydrochloride (PHMB, CAS No 1802181-67-4), polyhexameth- ylene biguanide hydrochloride (PHMB, CAS No. 27083-27-8), e.g. poly(iminoimidocarbonyl)iminohexamethylene hydrochloride, poly(iminocarbonimidoyliminocarbonimidoylimino -1,6-hexanediyl), polyaminopropyl biguanide; Pyridine-2-thiol 1-oxide, sodium salt (Sodium pyrithione, CAS No. 3811-73-2);
  • Salts of benzoic acid e.g. ammonium benzoate, calcium benzoate, magnesium benzoate, MEA- benzoate, potassium benzoate;
  • Benzoic acid and its sodium salt (CAS No 65-85-0, CAS No. 532-32-1);
  • Salicylic acid and its salts e.g. calcium salicylate, magnesium salicylate, MEA salicylate, sodi um salicylate, potassium salicylate, TEA salicylate;
  • Undec -10-enoic acid and its salts e.g. undecylenic acid, potassium undecylenic acid, sodium undecylenic acid, calcium undecylenic acid, MEA-undecylenic acid, TEA-undecylenic acid;
  • N,N' -bis(4-chlorophenyl)-3,12-diimino-2,4,11,13-tetraazatetradecanediamidine and its diglu conate, diacetate and dihydrochloride e.g. chlorohexidine, chlorhexidine digluconate, chloro- hexidine diacetate, chlorhexidine dihydrochloride (CAS Nos 55-56-1, 56-95-1, 18472-51-0, 3697-42-5);
  • Benzenemethanaminium N,N -dimethyl-N-[2-[2-[4-(1, 1,3,3, - tetramethylbutyl)phenoxy]ethoxy]ethyl]-, chloride, synonym: benzethonium chloride CAS No 121-54-0);
  • Benzalkonium chloride, bromide and saccharinate e.g. benzalkonium chloride, benzalkonium bromide, benzalkonium saccharinate (CAS Nos 8001-54-5, 63449-41-2, 91080-29-4, 68989-01- 5, 68424-85-1 , 68391-01-5, 61789-71-7, 85409-22-9);
  • IPBC 3 -lodo-2-propynylbutylcarbamate
  • 2,4-dichlorobenzyl alcohol (CAS-No. 1777-82-8, further names: dichlorobenzyl alcohol, 2,4- dichloro-benzenemethanol, (2,4-dichloro-phenyl)-methanol, DCBA, Protectol® DA);
  • 1-propanol (CAS-No. 71-23-8, further names: n-propanol, propan-1-ol, n-propyl alcohol, Protec tol® NP S);
  • 5-bromo-5-nitro-1,3-dioxane (CAS-No. 30007-47-7, further names: 5-bromo-5-nitro-m-dioxane, Bronidox ®);
  • 2-bromo-2-nitropropane-1,3-diol (CAS-No. 52-51-7, further names: 2-bromo-2-nitro-1,3- propanediol, Bronopol®, Protectol® BN, Myacide AS);
  • Glutaraldehyde (CAS-No. 111-30-8, further names: 1-5-pentandial, pentane-1, 5-dial, glutaral, glutardialdehyde, Protectol® GA, Protectol® GA 50, Myacide® GA);
  • 2,4,4'-trichloro-2'-hydroxydiphenyl ether (CAS No. 3380-34-5, further names: triclosan, Irgasan® DP 300, Irgacare® MP, TCS);
  • 4,4’-dichloro 2-hydroxydi phenyl ether (CAS-No. 3380-30-1), further names: 5-chloro-2-(4- chlorophenoxy) phenol, Diclosan, DCPP, which is commercially available as a solution of 30 wt% of 4,4’-dichloro 2-hydroxydiphenyl ether in 1 ,2 propyleneglycol under the trade name Tino- san® HP 100 (BASF);
  • 2-Phenoxyethanol (CAS-no. 122-99-6, further names: Phenoxyethanol, Methylphenylglycol, Phenoxetol, ethylene glycol phenyl ether, Ethylene glycol monophenyl ether, Protectol® PE); Phenoxypropanol (CAS-No. 770-35-4, CAS No 4169-04-4, propylene glycol phenyl ether, phe- noxyisopropanol 1-phenoxy-2-propanol, 2-phenoxy-1 -propanol);
  • Glucoprotamine (CAS-No. 164907-72-6, chemical description: reaction product of glutamic acid and alkylpropylenediamine, further names: Glucoprotamine 50);
  • Cyclohexyl hydroxyl diazenium-1 -oxide, potassium salt (CAS No. 66603-10-9, further names: N- cyclohexyl-diazenium dioxide, Potassium HDO, Xyligene, Protectol® KD);
  • Formic acid (CAS-No. 64-18-6, further names: methanoic acid, Protectol® FM, Protectol® FM 75, Protectol® FM 85, Protectol® FM 99, Lutensol® FM) and its salts, e.g. sodium formiate (CAS No 141-53-7); and performic acid and its salts.
  • the composition comprises 2-phenoxyethanol in a concentration of 0.01% to 5%, more preferably 0.1% to 2%, and/or bronopol in a concentration of 5ppm to 5000ppm, more preferably 20ppm to lOOOppm, and/or glutaraldehyde in a concentration of 2ppm to 5000ppm, more preferably 10ppm to 2000ppm, and/or formic acid (as an acid or its salt) in a concentration of 0.01% to 3%, more preferably 0.05% to 0.5%, and/or 4,4’-dichloro 2-hydroxydiphenyl ether in a concentration of 0.001% to 1%, more preferably 0.002% to 0.6% (in all cases relative to the total weight of the composition).
  • the composition comprises 2-phenoxyethanol in a concentration from 0.01% to 5%, preferably 0.1% to 2%, and/or 4,4’-dichloro 2- hydroxydiphenylether in a concentration from 0.001 to 3%, preferably 0.002 to 1%, more prefer ably 0.01 to 0.6%, each by weight of the composition:
  • the composition is an aqueous composition comprising 2- phenoxyethanol, bronopol, glutaraldehyde and/or formic acid (as an acid or its salt), especially in the amount indicated above.
  • the invention thus further pertains to a method of preserving an aqueous composition accord ing to the invention against microbial contamination or growth, which method comprises addition of an preservative or biocide selected from the group consisting of 2-phenoxyethanol, glutaral dehyde, 2-bromo-2-nitropropane-1,3-diol, and formic acid in acid form or as its salt.
  • an preservative or biocide selected from the group consisting of 2-phenoxyethanol, glutaral dehyde, 2-bromo-2-nitropropane-1,3-diol, and formic acid in acid form or as its salt.
  • the composition contains a surfactant and 4,4’-dichloro 2- hydroxydiphenyl ether, typically formulated as a cleansing product or laundry detergent; the amount of 4,4’-dichloro 2-hydroxydiphenyl ether therein is preferably as noted above, and the amount of surfactant in the cleansing product or laundry detergent is typically from the range 1% to 95%, each relative to the total weight of the composition.
  • the invention thus further pertains to the use of present composition further comprising a sur factant and 4,4’-dichloro 2-hydroxydiphenyl ether, as a cleansing composition especially for hard surfaces, or as a laundry detergent or as a softener composition, and to a corresponding method of laundering fabric or of cleaning hard surfaces.
  • viscosity modifiers examples include agar-agar, carragene, tragacanth, gum arabic, alginates, pectins, hydroxyethyl cellulose, hydroxypropyl cellulose, starch, gelatin, locust bean gum, cross- linked poly(meth)acrlyates, for example polyacrlyic acid cross-linked with bis-(meth)acrylamide, furthermore silicic acid, clay such as - but not limited to - montmorrilionite, zeolite, dextrin, and casein.
  • cross- linked poly(meth)acrlyates for example polyacrlyic acid cross-linked with bis-(meth)acrylamide, furthermore silicic acid, clay such as - but not limited to - montmorrilionite, zeolite, dextrin, and casein.
  • Hydrotropes in the context with the present invention are compounds that facilitate the dissolu tion of compounds that exhibit limited solubility in water.
  • hydrotropes are organic solvents such as ethanol, isopropanol, ethylene glycol, 1,2-propylene glycol, and further organic solvents that are water-miscible under normal conditions without limitation.
  • suitable hydrotropes are the sodium salts of toluene sulfonic acid, of xylene sulfonic acid, and of cumene sulfonic acid.
  • polymers other than polymer (A) are especially polyacrylic acid and its respective alkali metal salts, especially its sodium salt.
  • a suitable polymer is in particular polyacrylic acid, preferably with an average molecular weight M w in the range from 2,000 to 40,000 g/mol. pref erably 2,000 to 10,000 g/mol, in particular 3,000 to 8,000 g/mol, each partially or fully neutral ized with alkali, especially with sodium.
  • Suitable as well are copolymeric polycarboxylates, in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid and/or fumaric acid.
  • Polyacrylic acid and its respective alkali metal salts may serve as soil anti-redeposition agents.
  • polymers are polyvinylpyrrolidones (PVP).
  • PVP polyvinylpyrrolidones
  • Polyvinylpyrrolidones may serve as dye transfer inhibitors.
  • polymers are polyethylene terephthalates, polyoxyethylene terephthalates, and polyethylene terephthalates that are end-capped with one or two hydrophilic groups per molecule, hydrophilic groups being selected from CFhCFhCFh-SOsNa, CH 2 CH(CH 2 -SC> 3 Na) 2 , and CH 2 CH(CH 2 S0 2 Na)CH 2 -S0 3 Na.
  • buffers are monoethanolamine and N,N,N-triethanolamine.
  • defoamers are silicones.
  • compositions are not only good in cleaning soiled laundry and/or hard surfaces, pref erably laundry, with respect to organic fatty soil such as oil.
  • Inventive liquid detergent composi tions are very useful for removing non-bleachable stains such as, but not limited to stains from red wine, tea, coffee, vegetables, and various fruit juices like berry juices from laundry and/or hard surfaces, preferably laundry. They still do not leave residues on the clothes or hard surfac es.
  • inventive compositions may be in bulk form or as unit doses, for example in the form of sachets or pouches.
  • Suitable materials for pouches are water-soluble polymers such as polyvinyl alco hol.
  • inventive compositions are liquid or gel- type.
  • inventive compositions are liquid or gel-type and have a pH value in the range of from 7 to 9, preferably 7.5 to 8.5. In one embodiment of the present invention, inventive compositions are liquid or gel-type and have a total solids content in the range of from 8 to 80%, preferably 10 to 50%, determined by drying under vacuum at 80°C.
  • the invention is directed to a method of improving the cleaning performance of a detergent composition, preferably a liquid detergent composition, by adding a polymer (A) ac cording to the invention to a detergent composition preferably comprising at least one lipase and/or at least one protease.
  • improved cleaning performance herein may indicate that the polymer (A) provides better, i.e. improved, properties in stain removal under relevant cleaning conditions, when com pared to the cleaning performance of a detergent composition lacking polymer (A).
  • “improved cleaning performance” means that the cleaning performance of a deter gent comprising polymer (A) and at least one enzyme (B), preferably at least one lipase and/or at least one protease and/or a mannanase, is improved when compared to the cleaning perfor mance of a detergent comprising polymer (A) and no enzyme (B).
  • “im proved cleaning performance” means that the cleaning performance of a detergent comprising polymer (A) and an enzyme (B), preferably lipase and/or protease and/or mannanase, is im proved when compared to the cleaning performance of a detergent comprising at least one en zyme (B), preferably at least one lipase and/or at least one protease and/or mannanase, and no polymer (A).
  • relevant cleaning conditions refers to the conditions, particularly cleaning temperature, time, cleaning mechanics, suds concentration, type of detergent and water hard ness, actually used in laundry machines, automatic dish washers or in manual cleaning provics.
  • the present invention is also directed to the use of a composition as described herein for laundry or hard surface care.
  • the present invention is also directed to the use of a composition as described herein for improved cleaning performance, in particular in laundry or hard surface care.
  • the present invention is also directed to the use of a composition described herein for biofilm and/or sebum stain removal and/or for malodour reduction on a textile or hard surface, with hard surface cleaning preferably being dish washing (manual (hand) dish washing or auto mated dish washing) or cleaning of hard surfaces inside a washing machine, but in this embod iment preferably being cleaning of hard surfaces inside a washing machine (dishwashing or laundry washing machine, preferably laundry washing machine).
  • the present invention is also directed to a method of biofilm removal and/or biofilm pre vention and/or sebum stain removal and/or for malodour reduction on a textile or hard surface comprising the steps of
  • a liquid composition preferably a detergent composition, preferably comprising a surfactant as described herein, comprising (A) at least one polymer comprising
  • X 1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, n is in the range of from 1 to 4,
  • step (ii) contacting a textile or a hard surface with the liquid composition of step (i) for a time and under conditions suitable to allow biofilm removal and/or biofilm prevention and/or sebum stain removal and/or malodour reduction.
  • the enzyme used in the method of biofilm removal and/or biofilm prevention and/or sebum stain removal and/or for malodour reduction on a textile or hard surface described above is selected from the group consisting of amylase, protease, lipase, mannanase, xylanase, nu clease, cellulase, and combinations thereof, preferably selected from the group consisting of protease, lipase, mannanase, and combinations thereof.
  • the enzyme is a pro tease, preferably a subtilisin protease.
  • the method biofilm and/or sebum stain removal and/or for malodour reduction on a textile or hard surface described herein comprises the use of several enzymes.
  • the combination of enzymes is prote ase and/or lipase and/or mannanse, preferably protease and lipase, further preferred protease, lipase and mannanase.
  • the enzyme used in the method of biofilm removal described herein is a protease, preferably a subtilisin.
  • the enzyme used in the method of sebum stain removal described herein is selected from the group consisting of protease, lipase, mannanase, and combinations thereof, preferably a protease; more preferably, the at least one enzyme is a combination of enzymes selected from the group consisting of a protease and a lipase; and a protease, a lipase, and a man nanase, preferably the combination of enzymes in the method of sebum stain removal de scribed herein is a protease, a lipase, and a mannanase.
  • inventive process comprises steps (a), (b) and (y):
  • step (b) subjecting the intermediate from step (a) to polycondensation under catalysis of at least one acidic catalyst, thereby obtaining a polycondensate
  • step (g) reacting the polycondensate from step (b) with at least one C2-C4-alkylene oxide in one or more steps.
  • step (a) a diamine according to general formula H2-N-Z-NH2 is reacted with an alkylene ox ide.
  • the variable Z has been defined above.
  • mixtures of isomeric diamines are considered “a diamine”.
  • diamino-methylcyclohexane is usually generated as a mixture of various isomers
  • Alkylene oxides reacted in step (a) are selected from ethylene oxide experiencingEO“), propylene oxide (“PO”), and mixtures of the foregoing. Preferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.
  • step (a) the molar ratio alkylene oxide: diamine is in the range of from 4:1 to 1:1, preferably 2.5:1 to 1 :0.7.
  • Step (a) may be performed with or without a solvent.
  • diamine accord ing to general formula H2-N-Z-NH2 is liquid at reaction temperature it is preferred to use said diamine in bulk.
  • diamine according to general formula H2-N-Z-NH2 is solid at reaction temperature it is preferred to use a solvent.
  • Suitable solvents are aprotic sol vents, for example hydrocarbons such as toluene and ethers, e.g. di-n-butyl ether.
  • step (a) may include dilution of diamine according to general formula H2-N-Z-NH2 with water before alkoxylation, for example in a ratio diamine : water of 100 : 1 to 1 :1 , especially from 20 : 1 to 5 :1 by weight.
  • step (a) is carried out in the absence of a catalyst.
  • step (a) is performed at a reaction temperature from 90 to 150°C, preferably from 100 to 135°C.
  • step (a) may be carried out at a pressure of up to 15 bar, preferably up to 10 bar, for example 1 to 8 bar.
  • Preferred vessels for carrying out step (a) are autoclaves and tubular reactors.
  • step (a) has a duration in the range of from 30 minutes to 10 hours, preferably 1 hour to 7 hours.
  • Step (a) may be carried out under an inert gas atmosphere, for example nitrogen or a noble gas.
  • step (a) is carried out under an atmosphere of alkylene oxide. Inert gas atmosphere is preferred.
  • an intermediate is formed. It is possible to work up the intermediate, for example by removal of unreacted alkylene oxide and of water, if present, or to use the intermediate from step (a) without further work-up.
  • Said removal of unreacted al kylene oxide and of water, if present, may be performed by evaporation at a pressure in the range of from 500 mbar to 0 mbar, preferred: 100 mbar to 20 mbar and at a temperature in the range of from 20 to 120 °C, preferred are 60 to 100 °C.
  • the intermediate from step (a) is usually a mixture of compounds, a main component being H-AO-NH-Z-NH-AO-H, with AO being CH2CH2-O or CH 2 CH(CH 3 )-0, and the degree of alkoxylation is usually an average number.
  • step (b) the intermediate from step (a) is subjected to polycondensation under catalysis of at least one acidic catalyst.
  • Suitable acidic catalysts for step (b) are selected from organic sulfonic acids such as para- toluene sulfonic acid, sulfuric acid and phosphorus-bearing acids, preferred are H 3 PO 3 , H 3 PO 4 , and phosphinic acid (H 3 PO 2 ), even more preferred are H 3 PO 4 and H 3 PO 2 .
  • Lewis acids such as, but not limited to AICI 3 , FeC , diethyl tin dilaurate, and Ti(0-te/tbutyl) 4 may serve as catalyst as well.
  • the acidic catalyst can be applied in bulk or as aqueous solution.
  • the catalyst is added generally in an amount of 0.001 to 10 mole-%, preferably of 0.005 to 7, more preferably 0.01 to 5 mol-%, based on the amount of intermediate from step (a).
  • Step (b) may be carried out by using a solvent.
  • solvents that can be used to per form the inventive process are aromatic and/or (cyclo)aliphatic hydrocarbons and their mixtures, and halogenated hydrocarbons. Preference is given monoalkylated or polyalkylated benzenes and naphthalenes and mixtures thereof.
  • Preferred aromatic hydrocarbon mixtures are those predominantly comprising aromatic C 7 to C M hydrocarbons and possibly encompassing a boiling range from 110 to 300 °C, particular preference being given to toluene, 0-, m- or p-xylene, trimethylbenzene isomers, tetra- methylbenzene isomers, ethylbenzene, cumene, tetrahydronaphthalene, and mixtures compris ing them.
  • Examples thereof are the Solvesso® grades from ExxonMobil Chemical, especially Solvesso® 100 (CAS No.
  • Halogenated hydrocarbons are, for example, chlorobenzene and dichlorobenzene or its isomer mixtures.
  • esters are n-butyl acetate, ethyl acetate, 1-methoxyprop-2-yl acetate, and 2-methoxyethyl acetate.
  • ethers are THF, dioxane, and the dimethyl, diethyl or di-n-butyl ethers of ethylene glycol.
  • Examples of (cyclo)aliphatic hydrocarbons are decalin, alkylated decalin, and isomer mixtures of linear or branched alkanes and/or cycloalkanes.
  • Preferred solvents are those that form low-boiling azeotropic mixtures with water and thus facili tate removal of water.
  • step (b) is carried out in a way that the temperature during polycon densation does not exceed 240 °C.
  • the polycondensation is carried out at temper atures in the range of from 100 to 230 °C, preferably 150 to 210 °C. Even more preferably, the temperature during polycondensation does not exceed 210 °C.
  • step (b) is carried out in a way that the duration of the polycondensation is one to 25 hours, preferably 1 to 15 hours, more preferably 2 to 10 hours.
  • step (b) can be carried out at a pressure in the range of from 0.5 bar to 20 bar, while normal pressure being preferred. In a preferred embodi ment, the inventive process is being performed at normal pressure. In an alternative embodi ment, step (b) is carried out in vacuo or at a pressure in the range of from 1 mbar to 0.5 bar. Step (b) is preferably followed by removal or blow-off of residual monomers, for example, by distilling them off at normal pressure or at reduced pressure, e. g., in the range of from 0.1 to 0.75 bar.
  • step (b) water or other volatile products released during the polyconden sation can be removed from the reaction mixture in order to accelerate the reaction, such re moval being accomplished by distillation, for example, and optionally under reduced pressure.
  • the removal of water or of other low molecular mass reaction by-products can also be assisted by passing through the reaction mixture a stream of gas which is substantially inert under the reaction conditions (stripping), such as nitrogen, for example, or a noble gas such as helium, neon or argon, for example.
  • step (b) 0.4 to 1.0 and preferably 0.4 to 0.7 mol H2O moles of water per mole of intermediate from step (a) are removed in step (b).
  • a polycondensate is obtained.
  • Said polycondensate is usually a mixture of compounds, e.g., with a different value of the variable n, or with branching or cross-linking.
  • H2N-Z-NH2 is selected from 2,4-diamino- methylcyclohexane and alkylene oxide is ethylene oxide and 0.5 mole of water are removed from the intermediate, a mixture containing the below compounds is made.
  • An - optional - step of work-up may include the deactivation of catalyst used in step (b).
  • step (y) polycondensate from step (b) is reacted with at least one C2-C4-alkylene oxide.
  • C2-C4-alkylene oxides are ethylene oxide deficitEO“), propylene oxide (“PO”), butylene oxide (“BuO”), and mixtures of at least two of the foregoing.
  • Preferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.
  • Step (g) is preferably carried out in the presence of a catalyst, for example a base or a double metal cyanide.
  • a catalyst for example a base or a double metal cyanide.
  • step (g) is carried out in the presence of a base.
  • bases such as potassium hydroxide, sodium hydroxide, sodium or potassium alkoxides such as potassium methylate (KOCH 3 ), potassium tert-butoxide, sodium ethoxide and sodium methylate (NaOCHs), preferably from potassium hydroxide and sodium hydroxide.
  • Suitable bases such as potassium hydroxide, sodium hydroxide, sodium or potassium alkoxides such as potassium methylate (KOCH 3 ), potassium tert-butoxide, sodium ethoxide and sodium methylate (NaOCHs), preferably from potassium hydroxide and sodium hydroxide.
  • alkali metal hydrides and alkaline earth metal hydrides such as sodium hydride and calcium hydride
  • alkali metal hydroxides preference being given to potassium hydroxide and sodium hydroxide
  • alkali metal alkoxides particular preference being given to potassium t-butoxide in t-butanol, sodium n-hexanolate in n-hexanol, and to so dium methanolate in n-nonanol.
  • Typical use amounts for the base are from 0.05 to 10% by weight, in particular from 0.5 to 2% by weight, based on the total amount of polycondensate from step (b) and C 2 -C4-alkylene oxide.
  • step (g) is carried out in the presence of a double metal cyanide.
  • Double-metal cyanides hereinafter also referred to as double metal cyanide compounds or DMC compounds, usually comprise at least two different metals, at least one of them being selected from transition metals and the other one being selected from transition metals and alkali earth metals, and furthermore cyanide counterions.
  • Particularly suitable cata lysts for the alkoxylation are double-metal cyanide compounds which contain zinc, cobalt or iron or two thereof. Berlin blue, for example, is particularly suitable.
  • crystalline DMC compounds Preference is given to using crystalline DMC compounds.
  • a crystal line DMC compound of the Zn-Co type which comprises zinc acetate as further metal salt com ponent is used as catalyst. Such compounds crystallize in monoclinic structure and have a platelet-like habit.
  • the inventive synthesis is carried out in the pres ence of at least one double-metal cyanide selected from hexacyano cobaltates.
  • the inventive synthesis is carried out in the pres ence of at least one double-metal cyanide selected from compounds according to general for mula (VIII)
  • M 2 is at least one metal ion chosen from the group consisting of Fe 2+ , Fe 3+ , Co 2+ , Co 3+ , Mn 2+ , Mn 3+ , V 4+ , V 5+ , Cr 2+ , Cr 3 *, Rh 3+ , Ru 2+ , Ir 3 *, and in a way that M 1 and M 2 are not identical,
  • a and X 2 are anions selected from the group consisting of halide, hydroxide, sulfate, carbonate, cyanide, thiocyanate, isocyanate, cyanate, carboxylate, oxalate, nitrate, nitrosyl, hydrogensulfate, phosphate, dihydrogenphosphate, hydrogenphosphate or hy- drogencarbonate,
  • L is a ligand chosen from the group consisting of alcohols, aldehydes, ketones, ethers, polyeth ers, esters, polyesters, polycarbonate, ureas, amides, primary, secondary and tertiary amines, ligands with pyridine nitrogen, nitriles, sulfides, phosphides, phosphites, phosphanes, phospho- nates and phosphates, k is greater than or equal to zero, and up to 6.
  • the variable k can be a whole number or a frac tion.
  • P is an organic additive, selected for example from polyethers, polyesters, polycarbonates, poly- alkylene glycol sorbitan esters, polyalkylene glycol glycidyl ethers, polyacrylamides, poly(acrylamide-co-acrylic acid), polyacrylic acids, poly(acrylamide-co-maleic acid), polyacrylo nitriles, polyalkyl acrylates, polyalkyl methacrylates, polyvinyl methyl ethers, polyvinyl ethyl ethers, polyvinyl acetates, polyvinyl alcohol, poly-N-vinylpyrrolidone, poly(N-vinylpyrrolidone-co- acrylic acid), polyvinyl methyl ketone, poly(4-vinylphenol), poly(acrylic acid-co-styrene), oxazo- line polymer, maleic acid and maleic anhydride copolymers, hydroxyethylcellulose, polyace tates, ionic surface-active
  • r1 , r2, r3, r4, r 7 and ml are chosen such that the electroneutrality of the compound (I) is en sured, where each f and r 3 may be 0, r 5 is the number of ligand molecules, for example a fraction or an integer greater than zero, or zero, r6 and r6, independently of one another, are fractions or integers greater than zero, or zero.
  • the upper limits of r 5 , r 6 , and r 8 are each 6.
  • Double-metal cyanide compounds can be used as powder, paste or suspension or be moulded to give a moulding, be introduced into mouldings, foams or the like or be applied to mouldings, foams or the like.
  • the DMC catalyst used for step (y), based on polycondensate obtained in step (b), is from 5 to 2000 ppm (i.e. mg of catalyst per kg of product), preferably less than 1000 ppm, in particular less than 500 ppm, particularly preferably less than 100 ppm, for example less than 50 ppm or 35 ppm, particularly preferably less than 25 ppm; ppm referring to mass-ppm (parts per million) of polycondensate obtained in step (b).
  • Step (g) may be carried out in bulk, embodiment (i), or in an organic solvent, embodiment (ii).
  • water can be removed from the polycondensate obtained in step (b).
  • Such wa ter removal can be done by heating to a temperature in the range of from 80 to 150°C under a reduced pressure in the range of from 0.01 to 0.5 bar and distilling off the water.
  • step (g) is carried out at a reaction temperature in the range of from 70 to 200°C and preferably from 100 to 180°C.
  • step (g) is carried out once per synthesis of in ventive polymer (A).
  • step (g) is carried out several time, for ex ample up to four times per synthesis of an inventive polymer (A), for example with the same or preferably with different C2-C4-alkylene oxides. It is, for example, possible to subject a polycon densate obtained in step (b) to a first alkoxylation (g1) with ethylene oxide and to subject the product from step (g1) to a second alkoxylation (g2), for example with propylene oxide.
  • step (g) is carried out at a pressure of up to 10 bar and in particular up to 8 bar, for example 1 to 8 bar.
  • reaction time of step (g) is generally in the range of from 0.5 to 12 hours.
  • suitable organic solvents for embodiment (ii) of step (g) are nonpolar and polar aprotic organic solvents.
  • suitable nonpolar aprotic solvents include ali- phatic and aromatic hydrocarbons such as hexane, cyclohexane, toluene and xylene.
  • particularly suitable polar aprotic solvents are ethers, in particular cyclic ethers such as tetra- hydrofuran and 1 ,4-dioxane, furthermore N,N-dialkylamides such as dimethylformamide and dimethylacetamide, and N-alkyllactams such as N-methylpyrrolidone. It is as well possible to use mixtures of at least two of the above organic solvents.
  • Preferred organic solvents are xy lene and toluene.
  • the solution obtained in the first step, before or after addition of catalyst and solvent is dewatered before being subjected to alkylene oxide, said water removal advanta geously being done by removing the water at a temperature in the range of from 120 to 180°C, preferably supported by a stream of nitrogen.
  • the subsequent reaction with the alkylene oxide may be effected as in embodiment (i).
  • alkoxylated polyalkylenimines accord ing to the invention is obtained directly in bulk and may be dissolved in water, if desired.
  • organic solvent is typically replaced by water.
  • Alkoxylated polyalkylen imines according to the invention may alternatively be isolated in bulk.
  • An - optional - step of work-up may include the deactivation of catalyst used in step (y), in the case of basic catalysts by neutralization.
  • the inventive process does not require bleaching steps or reductive removal of impurities.
  • the invention is also directed to a method of making a composition comprising a polymer (A) and at least one enzyme (B) and optionally one surfactant (C) comprising the steps of
  • step (b) subjecting the intermediate from step (a) to polycondensation under catalysis of at least one acidic catalyst, thereby obtaining a polycondensate
  • step (g) reacting the polycondensate from step (b) with at least one C 2 -C 4 -alkylene oxide in one or more steps,
  • step (ii) obtaining a composition comprising the polymer obtained in step (i), and
  • step (iii) adding at least one enzyme (B) to the composition obtained in step (ii); and optionally
  • step (iv) adding at least one surfactant (C) to the composition obtained in step (iii).
  • composition can also obtained in a differ ent order, e.g., step (iii) prior step (ii) and step (iv) prior step (iii) or (ii), etc..
  • step (iii) prior step (ii) and step (iv) prior step (iii) or (ii), etc. The present invention is further illustrated by working examples.
  • the Hazen colour number was determined according to DIN ISO 6271, ASTM D 1209, with spectrophotometric detection. (2° norm observer, normal light, layer thickness 11 mm, against distilled water).
  • a 2-L steel autoclave was charged with 256 g methylcyclohexyldiamine (MCDA) as 4:1 mixture of 2,4-diamines and 2,6-diamines: and 43 g water and then heated to 100 °C. Then, 30 g of ethylene oxide were dosed into the autoclave. The start of an exothermic reaction was observed. Subsequently, 146 g of ethylene oxide were dosed into the autoclave within 4 hours. The system was kept at 100 °C for further 6 hours. After hat, the mixture is removed from the autoclave and residual EO and water were stripped under reduced pressure (20 mbar) at 80 °C for two hours. 430 g of intermediate were obtained as a yellow viscous liquid.
  • MCDA methylcyclohexyldiamine
  • a 500 ml_ four-neck flask equipped with stirrer, distillation bridge, N2 inlet, and internal ther mometer was charged with 315 g of the intermediate from step (a.1) and 1.6 g of a 50% aque ous solution of phosphinic acid (H 3 PO2).
  • the resulting reaction mixture was heated to 200 °C and then stirred at 200 °C under nitrogen for 2 hours while the distillate was collected. Then the temperature was reduced to 80 °C and the resulting polycondensate was collected as a viscous liquid.
  • a 2-liter steel autoclave was charged with 92 g of polycondensate from step (b.1) and 3.9 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under reumbled pressure. Then the residue was heated to 120 °C and 30 g of ethylene oxide were added within 10 minutes. After start of the exothermic reaction, 851 g of ethylene oxide were added within 12 hours. The resultant reaction mixture was maintained at 120 °C for 6 hours and then cooled to 80 °C. The autoclave was vented and discharged. Residual EO was stripped from the residue under reduced pressure at 80 °C. An amount of 987 g of inventive polymer (A.1) was obtained.
  • a 2-liter steel autoclave was charged with 292 g of inventive polymer (A.1) and 2.3 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under reduced pres sure. Then the residue was heated to 130 °C and 50 g of propylene oxide were added within 10 minutes. After start of the exothermic reaction, 229 g of propylene oxide were added within 6 hours. The resultant reaction mixture was maintained at 130 °C for 6 hours and then cooled to 100 °C. The autoclave was vented and discharged. Residual PO was stripped under reduced pressure at 80 °C. An amount of 575 g of inventive polymer (A.2) as a brown solid material were obtained. Analytics:
  • a 2-liter steel autoclave was charged with 641 g methylcyclohexyldiamine (MCDA) as 4:1 mix ture of 2,4-diamines and 2,6-diamines and 64 g water and then heated to 100 °C. Then, 30 g of ethylene oxide were dosed into the autoclave. The start of an exothermic reaction was ob served. Subsequently, 322 g of ethylene oxide were dosed into the autoclave within 6 hours. The system was kept at 100 °C for further 6 hours. After hat, the mixture is removed from the autoclave and residual EO and water were stripped under reduced pressure (20 mbar) at 80 °C for two hours 991 g of intermediate of stepl were obtained as a yellow viscous liquid.
  • MCDA methylcyclohexyldiamine
  • a 500 ml_ four-neck flask equipped with stirrer, distillation bridge, N2 inlet, and internal ther mometer was charged with 180.5 g of the intermediate from step a.3 and 0.94 g of a 50% aqueous solution of phosphinic acid (H 3 PO2).
  • the reaction mixture was stirred under nitrogen and heated up to 200 °C under stirring.
  • the reaction was kept at 200 °C under nitrogen and stirring for 14 hours while the distillate was collected. Then the temperature was reduced to 130 °C and the product was collected as a viscous liquid.
  • the resulting product was characterized via gel permeation chromatography (GPC) in HFIP and OH value.
  • a 2-liter steel autoclave was charged with 70 g of polycondensate from step (b.3) and 2.8 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under reumbled pressure. The resulting residue was then heated to 120 °C and 30 g of ethylene oxide were added within 10 minutes. After start of the exothermic reaction, 587 g of ethylene oxide were added within 12 hours. The resultant reaction mixture was maintained at 120 °C for 6 hours and then cooled to 100 °C. The autoclave was vented and discharged. Residual EO was stripped from the residue under reduced pressure at 80 °C. An amount of 689 g of inventive polymer (of step3) was obtained.
  • a 2-liter steel autoclave was charged with 197 g of inventive polymer A.3 and 1.5 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under reduced pres sure. The resultant residue was then heated to 130 °C and 30 g of propylene oxide was added within 10 minutes. After start of the exothermic reaction, 156 g of propylene oxide were added within 20 hours. The resultant reaction mixture was maintained at 130 °C for 4 hours and then cooled to 100 °C. The autoclave was vented and discharged. Residual PO was stripped under reduced pressure at 80 °C. An amount of 383 g of inventive polymer (A.4) as a brown solid ma terial were obtained.
  • Lipase (B.1) Lipex® 100 L, a lipase commercially available from Novozymes (lipase variant of amino acids 1-269 of SEQ ID NO: 2 of US5869438 with T231R and N233R substitutions) Quantities of the respective enzyme are tel quel.
  • inventive polymer (A.2) The primary wash performance of the inventive polymer (A.2) was tested in the washing ma chine preparing wash solutions using water of 14°dH hardness (2.5 mmol/L; Ca:Mg:HCC>34:1 :8) containing 3.0-4.0 g/L of the liquid test detergent L.1, see composition in Table 1, and 0.7-1.0% of inventive polymer (A.2) and/or in combination with 0.1% by weight (B.1) and 0.5% by weight (C.1).
  • the multi-stain monitors MS1 and MS2 (Table 2) contain respectively 8 and 4, standardized soiled fabrics, of respectively 5.0 x 5.0 cm and 4.5x4.5 cm size, all of them stitched on two sides to a polyester carrier.
  • CFT C-S-10 butterfat with colorant on cotton
  • CFT C-S-62 lard, colored on cotton
  • CFT C-S-78 soybean oil with pigment on cotton EM
  • PA 112 cocoa on cotton EM
  • PA 141/1 lipstick on cotton
  • EMPA 125 soiling on cotton fabric, sensitive to surfactants as well as to lipases wfk20D: pigment and sebum-type fat on polyester/cotton mixed fabric CFT C-S-70: chocolate/mousse cream on cotton MS2:
  • CFT C-S-10 butterfat with colorant on cotton CFT C-S-62: lard, colored on cotton CFT C-S-61: beef fat, colored on cotton CFT PC-S-04: Saturated with colored olive oil on Polyester/Cotton (65/35)
  • the total level of cleaning was evaluated using color measurements. Reflectance values of the stains on the monitors were measured using a sphere reflectance spectrometer (SF 500 type from Datacolor, USA, wavelength range 360-700 nm, optical geometry d/8°) with a UV cutoff filter at 460 nm. In this case, with the aid of the CIE-Lab color space classification, the bright ness L *, the value a * on the red - green color axis and the b * value on the yellow - blue color axis, were measured before and after washing and averaged for the respective stains of the monitor. The change of the color value (Delta E, DE) value, defined and calculated automatical- ly by the evaluation color tools on the following formula is a measure of the achieved cleaning effect. All experiments were repeated three times to fur nish an average number.
  • Lipase activity was determined by employing para-nitrophenol-valerate (2.4 mM pNP-C5 in 100 mM Tris pH 8.0, 0.01% Triton X100) as a substrate.
  • the absorption at 405 nm was measured at 20°C every 30 seconds over 5 minutes.
  • the slope (absorbance increase at 405 nm per minute) of the time dependent absorption-curve is directly proportional to the activity of the lipase.
  • Lipase (B.1) Lipex® 100L, a lipase commercially available from Novozymes (amino acids 1-269 of SEQ ID NO: 2 of US5869438 with T231R and N233R substitutions);
  • BLAP protease formulation formulation comprising 4.6% Bacillus lentus alka line protease (BLAP) with R99E substitution (W09523221));
  • Mannanase (B.3): Mannaway® 4.0 L, a mannanase commercially available from Novozymes (amino acids of SEQ ID NO: 1 of W02009074685).
  • Quantities mentioned in this example refer to the enzyme products used as such.
  • the primary wash performance of the inventive compositions was tested in the washing ma chine (Miele SOFTTRONIC W 1935 WTL, 30°C, short program, 1200 rpm, 3.5 kg ballast load), in which wash solutions using water of 14°dH hardness (2.5 mmol/L; Ca:Mg:HC034:1:8) were prepared. In all cases 45 g of the liquid test detergent L.1 (see composition in Table 1 above) was added. This corresponds to about 3 g/L in the wash liquor.
  • the brightness L *, the value a * on the red - green color axis and the b * value on the yellow - blue color axis were meas ured before and after washing and averaged for the respective stains of the monitor.
  • the change of the color value (Delta E, DE) is a measure of the achieved cleaning effect.
  • Table 5b Results of washing machine test fabrics. Numbers are the average over 2 washing experiments per detergent formulation.
  • Biofilms were cultivated in a nutrient medium in microtiter plates in the presence of potentially inhibiting additives or mixtures of additives. After culturing, the biofilm was stained with a dye (safranin), the dye was then re-dissolved in a solvent. The absorption of the dye solution at 540 nm is a measure of the amount of biofilm that was grown in the well.
  • a dye safranin
  • Test organism Pseudomonas aeruginosa DSM 1117 (P. aeruginosa) was cultured on tryptic soy agar at 35°C for 24 h. The first passage was stored at +4°C for 9 days.
  • the inoculum was prepared by suspending 5 single colonies of the first passage in 200 ml 30% TSB + 2.5g/L glucose in a 200 ml_ shake flask at 35°C, on a shaker with agitation speed of -160 rpm for 24 h.
  • TSB + 2.5 g/L glucose The plate was incubated in a humid chamber at 33°C and 40 rpm for 24 h.
  • the absorption of the safranin solutions was determined using a plate reader at 540 nm.
  • composition was tested in parallel in 10 wells. The average over 10 results was taken. From each of these average absorption values a blank background value (average of at least 3 wells with growth medium, but without bacteria) was subtracted. A relative biofilm formation (in %) is calculated relative to the formation in the blank experiment (100% by definition). A biofilm inhibition effect (in %) is calculated by taking 100% - relative biofilm formation (%).
  • Protease only appears not to inhibit, but slightly promote biofilm growth (negative number).
  • Polymer A.2 shows a significant biofilm inhibition of 36%.
  • Surfactant Lutensol A07 shows a very slight biofilm inhibition of 9%.
  • the combination of all 3 shows a very pronounced biofilm inhibi- tion of 72%.
  • liquid laundry detergent formulations are illustrative examples of typical detergent formulations according to the present invention.
  • AEO C12/C14 fatty alcohol (7EO) Lutensol A07 (BASF)
  • AES Alcohol Ethoxysulfate: Texapon N 70 (BASF).
  • Tinosan HP 100 is a solution of 30% w/w of 4,4’-dichloro-2-hydroxydiphenylether (CAS: 3380- 30-1) in 1,2-propyleneglycol.

Landscapes

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

Abstract

The present invention is directed towards compositions comprising (A) at least one polymer comprising (a) a core that bears one to 3 moieties of the general formula (I) wherein Z are different or the same and selected from C2-C12-alkylene and C3-C12-cycloalkylene wherein C2-C12-alkylene and C3-C12-cycloalkylene may be non-substituted or substituted with one or more O-C1-C4-alkyl groups and wherein C3-C12-cycloalkylene may be non-substituted or bear one to three methyl groups. X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, n is in the range of from 1 to 4, (b) polyalkylene oxide chains; and (B) at least one enzyme.

Description

Compositions comprising polymer and enzyme
Description
The present invention is directed towards compositions comprising (A) at least one polymer comprising
(a) a core that bears one to 3 moieties of the general formula (I)
Figure imgf000002_0001
wherein Z are different or the same and selected from C2-Ci2-alkylene and C3-Ci2-cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-CrC4-alkyl groups and wherein C3-Ci2-cycloalkylene may bear one to three me thyl groups,
X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the fore going, preferred are methyl and more preferred is hydrogen, n is in the range of from 1 to 4,
(b) polyalkylene oxide chains; and
(B) at least one enzyme.
Furthermore, the present invention is directed to polymers useful for such compositions, and to a process for making such polymers.
Moreover, the present invention is directed to the use of the compositions comprising the poly mer and the at least one enzyme described herein for cleaning of textiles or hard surfaces. In particular, the compositions described herein are suitable for biofilm and/or sebum stain remov al and/or malodour reduction.
Laundry detergents and detergents for dish washing (including manual or automated dish wash ing) - both in home care and industrial and institutional (l&l) cleaning - have to fulfil several re- quirements. They need to remove all sorts of soiling from laundry or hard surfaces, for example all sorts of pigments, clay, fatty soil, sebum and body soils and dyestuffs including dyestuff from food and drinks such as red wine, tea, coffee, and fruit including berry juices. Laundry deter gents and dish wash detergents also need to exhibit a certain storage stability. Especially laun dry detergents and dish washing detergents that are liquid or that contain hygroscopic ingredi ents often lack a good storage stability, e.g. enzymes tend to be deactivated.
Fatty soilings, including sebum, are still a challenge, in particular in laundering. Although nu merous suggestions for removal have been made - polymers, enzymes, surfactants - solutions that work well are still of interest.
Furthermore, it is a challenge to prevent the formation of malodor on clothes. Malodor on clothes may be formed when body soils, like sebum are not well removed from clothes during washing. Bacteria can transform residual sebum on clothes into malodorous substances. More over, bacterial biofilms sometimes are formed in washing machines, especially when the wash ing temperatures are too low to kill all microorganisms. Also such biofilms can contribute to mal odor formation on clothes washed in that machine. Hence, it would be desirable when a laundry detergent, in particular a liquid laundry detergent, can remove sebum soils well from clothes and if it could prevent and/or remove the formation of bacterial biofilms in washing machines.
It was therefore an objective to provide a detergent composition that fulfils the requirements discussed above. It was further an objective to provide ingredients that fulfil the above require ments, and it was an objective to provide a process to make such ingredients and detergent compositions.
Accordingly, the compositions defined at the outset have been found, hereinafter also referred to as inventive compositions or compositions according to the present invention.
The inventive compositions comprise (A) least one polymer comprising
(a) a core that bears one to 3 moieties of the general formula (I)
Figure imgf000003_0001
wherein Z are different or the same and selected from
C2-Ci2-alkylene, for example -CH2CH2-, -(CH2)3-, -(CH2)4-, -(CH2)5-, -(CH2)6-, -(CH2)8-, -(CH2)10-, -(CH2)i2-, wherein C2-Ci2-alkylene may be straight-chain or branched, non-substituted or substi tuted with one or more 0-CrC4-alkyl groups and
C3-Ci2-cycloalkylene, wherein C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-CrC4-alkyl groups, and where C3-Ci2-cycloalkylene may bear one to three me thyl groups, preferably Cs-Cio-cycloalkylene such as 1,3-cyclopentylene, 1,2-cyclopentylidene, 1,2-cyclohexylene, 1,3-cyclohexylene, 1,4-cyclohexylene, 1 -methyl-2, 4-cyclohexylene, 1- methyl-2, 6-cyclohexylene, 1,3-cycloheptylene, 1,4-cylooctylene, 1,5-cyclooctylene, wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-CrC4-alkyl groups and wherein C3-Ci2-cycloalkylene may be non-substituted or bear one to three methyl groups,
X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the fore going, preferred are methyl and more preferred is hydrogen, preferred is hydrogen, n is in the range of from 1 to 4, preferably 1 to 3 and more preferably 1 to 2,
The free valences on the nitrogen atoms in formula (I) bear polyalkylene chains (b) or -CH2-CH(X1)-0-CHX1-CH2-N-Z-N units, or hydrogen atoms. In embodiments with molecular weights Mw of 10,000 g/mol or more, the free valences on the nitrogen atoms in formula (I) bear polyalkylene chains (b) or-CH2-CH(X1)-0-CHX1-CH2-N-Z-N units.
In one embodiment of the present invention, all Z in polymer (A) are selected from cyclo hexylene and cyclopentylene, each non-substituted or substituted with one to two methyl or methoxy groups.
Preferably, Z are isomers to each other and/or differ in the variable n. Even more preferably, Z are isomers.
A preferred example of Z is a combination - thus a mixture of isomers - according to the formu lae
Figure imgf000005_0001
Asterisks * refer to sites in Z that are connected to N atoms.
In one embodiment of the present invention, polymer (A) has an average molecular weight Mw in the range of from 1,000 to 80,000 g/mol, preferably 5,000 to 50,000 g/mol. The average mo lecular weight may be determined, e.g., by gel permeation chromatography (GPC) in tetrahydro- furan (THF) as mobile phase, with linear polymethyl methacrylate (“PMMA”) as standard.
In one embodiment of the present invention, polymer (A) has a molecular weight distribution Mw/Mn in the range of from 1.1 to 2.5.
In one embodiment of the present invention, polymer (A) has a Hazen colour number in the range of from 20 to 500, determined in a 10 % weight aqueous solution.
In one embodiment of the present invention, polymer (A) has an OH value, measured according to DIN 53240 (2013), in the range of from 20 to 650, preferably 30 to 100 mg KOH/g polymer (A).
In one embodiment of the present invention, polymer (A) has a total amine value in the range of from 10 to 650, preferably 10 to 510 and more preferably 10 to 80 mg KOH/g polymer (A), de termined according to ASTM D2074-07.
Polymer (A) furthermore bears
(b) polyalkylene oxide chains. Said polyalkylene oxide chains may be derived from C2-C4- alkylene oxide. Examples of C2-C4-alkylene oxides are ethylene oxide („EO“), propylene ox ide (“PO”), butylene oxide (“BuO”), and combinations of at least two of the foregoing, for example ethylene oxide and propylene oxide or ethylene oxide and butylene oxide. Pre ferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.
The inventive compositions comprise additionally at least one enzyme (B). Enzymes are identified by polypeptide sequences (also called amino acid sequences herein). The polypeptide sequence specifies the three-dimensional structure including the “active site” of an enzyme which in turn determines the catalytic activity of the same. Polypeptide sequences may be identified by a SEQ ID NO. According to the World Intellectual Property Office (WIPO) Standard ST.25 (1998) the amino acids herein are represented using three-letter code with the first letter as a capital or the corresponding one letter.
Any enzyme according to the invention relates to parent enzymes and/or variant enzymes, both having enzymatic activity. Enzymes having enzymatic activity are enzymatically active or exert enzymatic conversion, meaning that enzymes act on substrates and convert these into prod ucts. The term “enzyme” herein excludes inactive variants of an enzyme.
A “parent” sequence (of a parent protein or enzyme, also called “parent enzyme”) is the starting sequence for introduction of changes (e.g. by introducing one or more amino acid substitutions, insertions, deletions, or a combination thereof) to the sequence, resulting in “variants” of the parent sequences. The term parent enzyme (or parent sequence) includes wild-type enzymes (sequences) and synthetically generated sequences (enzymes) which are used as starting se quences for introduction of (further) changes.
The term “enzyme variant” or “sequence variant” or “variant enzyme” refers to an enzyme that differs from its parent enzyme in its amino acid sequence to a certain extent. If not indicated otherwise, variant enzyme “having enzymatic activity” means that this variant enzyme has the same type of enzymatic activity as the respective parent enzyme.
In describing the variants of the present invention, the nomenclature described as follows is used:
Amino acid substitutions are described by providing the original amino acid of the parent en zyme followed by the number of the position within the amino acid sequence, followed by the substituted amino acid. Amino acid deletions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by *. Amino acid insertions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by the original amino acid and the additional amino acid. For example, an insertion at position 180 of lysine next to glycine is designated as “Gly180Glyl_ys” or “G180GK”. In cases where a substitution and an insertion occur at the same position, this may be indicated as S99SD+S99A or in short S99AD. In cases where an amino acid residue identical to the existing amino acid residue is inserted, degeneracy in the nomenclature arises. If for example a glycine is inserted after the glycine in the above example this would be indicated by G180GG. Where different al terations can be introduced at a position, the different alterations are separated by a comma, e.g. “Arg170Tyr, Glu” represents a substitution of arginine at position 170 with tyrosine or glu tamic acid. Alternatively different alterations or optional substitutions may be indicated in brack ets e.g. Arg170[Tyr, Gly] or Arg170{Tyr, Gly}; or in short R170 [Y,G] or R170 {Y, G}; or in long R170Y, R170G.
Enzyme variants may be defined by their sequence identity when compared to a parent en zyme. Sequence identity usually is provided as “% sequence identity” or “% identity”. For calcu lation of sequence identities, in a first step a sequence alignment has to be produced. According to this invention, a pairwise global alignment has to be produced, meaning that two sequences have to be aligned over their complete length, which is usually produced by using a mathemati cal approach, called alignment algorithm. According to the invention, the alignment is generated by using the algorithm of Needleman and Wunsch (J. Mol. Biol. (1979) 48, p. 443-453). Prefer ably, the program “NEEDLE” (The European Molecular Biology Open Software Suite (EM BOSS)) is used for the purposes of the current invention, with using the programs default pa rameter (gap open=10.0, gap extend=0.5 and matrix=EBLOSUM62).
According to this invention, the following calculation of %-identity applies: %-identity = (identical residues / length of the alignment region which is showing the respective sequence of this in vention over its complete length) *100.
According to this invention, enzyme variants may be described as an amino acid sequence which is at least n% identical to the amino acid sequence of the respective parent enzyme with “n” being an integer between 10 and 100. In one embodiment, variant enzymes are at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical when compared to the full-length amino acid sequence of the parent en zyme, wherein the enzyme variant has enzymatic activity.
“Enzymatic activity” means the catalytic effect exerted by an enzyme, which usually is ex pressed as units per milligram of enzyme (specific activity) which relates to molecules of sub strate transformed per minute per molecule of enzyme (molecular activity). Variant enzymes may have enzymatic activity according to the present invention when said enzyme variants ex hibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the enzymatic activity of the respective parent enzyme.
In a particular embodiment, the enzyme is an oxidoreductase (EC 1), a transferase (EC 2), a hydrolase (EC 3), a lyase (EC 4), an isomerase (EC 5), or a ligase (EC 6) (EC-numbering ac cording to Enzyme Nomenclature, Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology including its supplements pub lished 1993-1999). Preferably, the enzyme is a hydrolase (EC 3), preferably, a glycosidase (EC 3.2) or a peptidase (EC 3.4). Especially preferred enzymes are enzymes selected from the group consisting of an amylase (in particular an alpha-amylase (EC 3.2.1.1)), a cellulase (EC 3.2.1.4), a lactase (EC 3.2.1.108), a mannanase (EC 3.2.1.25), a lipase (EC 3.1.1.3), a phytase (EC 3.1.3.8), a nuclease (EC 3.1.11 to EC 3.1.31), and a protease (EC 3.4); in particular an enzyme selected from the group consisting of amylase, protease, lipase, mannanase, phytase, xylanase, lactase, phosphatase, glucoamylase, nuclease, and cellulase, preferably, amylase or protease, preferably from protease, amylase, lipase, cellulase, and mannanase, most prefera bly, a protease. Particularly preferred is a serine protease (EC 3.4.21), preferably a subtilisin protease. In a preferred embodiment, the protein of interest is an enzyme suitable to be used in detergents. Thus, preferably, the enzyme is selected from the group consisting of amylase, pro tease, lipase, mannanase, xylanase, nuclease, and cellulase, preferably amylase, protease, lipase, mannanase, and cellulase, most preferably, selected from the group consisting of prote ase, lipase and mannanase. Most preferably, the enzyme is a protease, preferably a subtilisin protease.
In one embodiment, the enzyme is selected from hydrolases, most preferably from proteases, amylases, lipases, cellulases, nucleases, and mannanases.
In one embodiment of the present invention, the inventive compositions comprise at least one lipase. “Lipases”, “lipolytic enzyme”, “lipid esterase”, all refer to enzymes of EC class 3.1.1 (“carboxylic ester hydrolase”). Such a lipase may have lipase activity (or lipolytic activity; triacyl- glycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74; enzymes having cutinase activity may be called cutinase herein), sterol esterase activity (EC 3.1.1.13) and/or wax-ester hydro lase activity (EC 3.1.1.50). Lipases include those of bacterial or fungal origin.
Commercially available lipase include but are not limited to those sold under the trade names Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A/S), Preferenz™ L (DuPont), Lumafast (originally from Genencor) and Lipomax (Gist-Brocades/ now DSM).
In one aspect of the present invention, lipase is selected from the following: lipases from Humi- cola (synonym Thermomyces ), e.g. from H. lanuginosa ( T . lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. insolens as described in WO 96/13580; lipases derived from Rhizomucor miehei as described in WO 92/05249; lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. from P. alcali- genes or P. pseudoalcaligenes (EP 218272, WO 94/25578, WO 95/30744, WO 95/35381,
WO 96/00292), P. cepacia (EP 331376), P. stutzeri (GB 1372034), P. fluorescens, Pseudomo nas sp. strain SD705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), Pseudomonas mendocina (WO 95/14783), P. glumae (WO 95/35381, WO 96/00292); lipase from Streptomyces griseus (WO 2011/150157) and S. pristinaespiralis (WO 2012/137147), GDSL-type Streptomyces lipases (WO 2010/065455); lipase from Thermobifida fusca as dis closed in WO 2011/084412; lipase from Geobacillus stearothermophilus as disclosed in WO 2011/084417; Bacillus lipases, e.g. as disclosed in WO 00/60063, lipases from B. subtilis as disclosed in Dartois et al. (1992), Biochemica et Biophysica Acta, 1131, 253-360 or WO 2011/084599, B. stearothermophilus (JP S64-074992) or B. pumilus (WO 91/16422); lipase from Candida antarctica as disclosed in WO 94/01541. Suitable lipases include also those which are variants of the above described lipases which have lipolytic activity. Such suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105. Suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105.
Suitable lipases include also those that are variants of the above described lipases which have lipolytic activity. Suitable lipase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment lipase variants having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
Lipases have “lipolytic activity”. The methods for determining lipolytic activity are well-known in the literature (see e.g. Gupta et al. (2003), Biotechnol. Appl. Biochem. 37, p. 63-71). E.g. the lipase activity may be measured by ester bond hydrolysis in the substrate para-nitrophenyl pal- mitate (pNP-Palmitate, C: 16) and releases pNP which is yellow and can be detected at 405 nm. In one embodiment, lipase is selected from fungal triacylglycerol lipase (EC class 3.1.1.3). Fun gal triacylglycerol lipase may be selected from lipases of Thermomyces lanuginosa. In one em bodiment, at least one Thermomyces lanuginosa lipase is selected from triacylglycerol lipase according to amino acids 1-269 of SEQ ID NO: 2 of US5869438 and variants thereof having lipolytic activity. Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity which are at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438. Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing conservative mutations only, which do not pertain the functional domain of amino acids 1- 269 of SEQ ID NO: 2 of US 5,869,438. Lipase variants of this embodiment having lipolytic ac tivity may be at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.
Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing at least the following amino acid substitutions when compared to amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438: T231R and N233R. Said lipase variants may further comprise one or more of the following amino acid exchanges when compared to amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438: Q4V, V60S, A150G, L227G, P256K.
Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing at least the amino acid substitutions T231R, N233R, Q4V, V60S, A150G, L227G, P256K within the polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438and are at least 95%, at least 96%, or at least 97% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.
Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing the amino acid substitutions T231R and N233R within amino acids 1-269 of SEQ ID NO: 2 of US5869438 and are at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.
Thermomyces lanuginosa lipase may be a variant of amino acids 1-269 of SEQ ID NO: 2 of US5869438 having lipolytic activity, wherein the variant of amino acids 1-269 of SEQ ID NO: 2 of US5869438 is characterized in containing the amino acid substitutions T231R and N233R. Said lipase may be called Lipex herein.
In one embodiment of the present invention, a combination of at least two of the foregoing li pases may be used.
In one embodiment of the present invention, lipases are included in inventive composition in such an amount that a finished inventive composition has a lipolytic enzyme activity in the range of from 100 to 0.005 LU/mg, preferably 25 to 0.05 LU/mg of the composition. A Lipase Unit (LU) is that amount of lipase which produces 1 pmol of titratable fatty acid per minute in a pH stat. under the following conditions: temperature 30° C.; pH=9.0; substrate is an emulsion of 3.3 wt.
% of olive oil and 3.3% gum arabic, in the presence of 13 mmol/l Ca2+ and 20 mmol/l NaCI in 5 mmol/l Tris-buffer. In one embodiment of the present invention, inventive compositions comprise at least one pro tease.
In one embodiment, at least one protease is selected from the group of serine endopeptidases (EC 3.4.21), most preferably selected from the group of subtilisin type proteases (EC 3.4.21.62). Serine proteases or serine peptidases are characterized by having a serine in the catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction. A ser ine protease in the context of the present invention may be selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21.79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.118, or EC 3.4.21.119,) plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5), and subtilisin. Subtilisin is also known as subtilopepti- dase, e.g., EC 3.4.21.62, the latter hereinafter also being referred to as “subtilisin”. The subtil isin related class of serine proteases shares a common amino acid sequence defining a catalyt ic triad which distinguishes them from the chymotrypsin related class of serine proteases. Sub- tilisins and chymotrypsin related serine proteases both have a catalytic triad comprising aspar tate, histidine and serine.
Proteases are active proteins exerting “protease activity” or “proteolytic activity”. Proteolytic ac tivity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a de fined course of time.
The methods for analyzing proteolytic activity are well-known in the literature (see e.g. Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60: 381-395). Proteolytic activity may be determined by using Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF; see e.g. DelMar et al. (1979), Analytical Biochem 99, 316-320) as substrate. pNA is cleaved from the substrate molecule by proteolytic cleavage, resulting in release of yellow color of free pNA which can be quantified by measuring OD405.
Proteolytic activity may be provided in units per gram enzyme. For example, 1 U protease may correspond to the amount of protease which sets free 1 pmol folin-positive amino acids and peptides (as tyrosine) per minute at pH 8.0 and 37°C (casein as substrate).
Proteases of the subtilisin type (EC 3.4.21.62) may be bacterial proteases originating from a microorganism selected from Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. coli, Flavobacterium, Fuso- bacterium, Helicobacter, llyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.
In one aspect of the invention, at least one protease is selected from Bacillus alcalophilus, Ba cillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus thuringiensis protease.
In one embodiment of the present invention, at least one protease is selected from the follow ing: subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bac terid. Volume 159, p. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 11, p. 7911-7925); subtilisin from Bacillus licheniformis (subtilisin Carlsberg; disclosed in EL Smith et al. (1968) in J. Biol Chem, Volume 243, pp. 2184-2191, and Jacobs et al. (1985) in Nucl. Acids Res, Vol 13, p. 8913-8926); subtilisin PB92 (original sequence of the alkaline prote ase PB92 is described in EP 283075 A2); subtilisin 147 and/or 309 (Esperase®, Savinase®, respectively) as disclosed in WO 89/06279; subtilisin from Bacillus lentus as disclosed in WO 91/02792, such as from Bacillus lentus DSM 5483 or the variants of Bacillus lentus DSM 5483 as described in WO 95/23221; subtilisin from Bacillus alcalophilus (DSM 11233) disclosed in DE 10064983; subtilisin from Bacillus gibsonii (DSM 14391) as disclosed in WO 2003/054184; sub tilisin from Bacillus sp. (DSM 14390) disclosed in WO 2003/056017; subtilisin from Bacillus sp. (DSM 14392) disclosed in WO 2003/055974; subtilisin from Bacillus gibsonii (DSM 14393) dis closed in WO 2003/054184; subtilisin having SEQ ID NO: 4 as described in WO 2005/063974; subtilisin having SEQ ID NO: 4 as described in WO 2005/103244; subtilisin having SEQ ID NO: 7 as described in WO 2005/103244; and subtilisin having SEQ ID NO: 2 as described in appli cation DE 102005028295.4.
Examples of useful proteases in accordance with the present invention comprise the variants described in: WO 92/19729, WO 95/23221, WO 96/34946, WO 98/20115, WO 98/20116, WO 99/11768, WO 01/44452, WO 02/088340, WO 03/006602, WO 2004/03186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2011/036264, and WO 2011/072099. Suitable exam ples comprise especially variants of subtilisin protease derived from SEQ ID NO:22 as de scribed in EP 1921147 (which is the sequence of mature alkaline protease from Bacillus lentus DSM 5483) with amino acid substitutions in one or more of the following positions: 3, 4, 9, 15,
24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 131, 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and 274 (according to the BPN' numbering), which have proteolytic activity. In one embodiment, such a protease is not mutated at positions Asp32, His64 and Ser221 (according to BPN’ numbering).
In one embodiment, at least one protease has a sequence according to SEQ ID NO:22 as de scribed in EP 1921147, or a protease which is at least 80% identical thereto and has proteolytic activity. In one embodiment, said protease is characterized by having amino acid glutamic acid (E), or aspartic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity. In a pre ferred embodiment, at least one protease has a sequence according to SEQ ID NO:22 as de- scribed in EP 1921147, or a protease which is at least 80% identical thereto and comprises a glutamic acid (E) at position 101 (according to BPN’ numbering) and has proteolytic activity. In one embodiment, said protease is characterized by having amino acid glutamic acid (E), or as partic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity. In one embodiment, said protease comprises one or more further substitutions: (a) threonine at position 3 (3T), (b) isoleucine at position 4 (4I), (c) alanine, threonine or arginine at position 63 (63A, 63T, or 63R), (d) aspartic acid or glutamic acid at position 156 (156D or 156E), (e) proline at position 194 (194P), (f) methionine at position 199 (199M), (g) isoleucine at position 205 (205I), (h) aspartic acid, glutamic acid or glycine at position 217 (217D, 217E or217G), (i) combinations of two or more amino acids according to (a) to (h).
At least one protease may be at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and is characterized by comprising one amino acid (according to (a)-(h)) or combina tions according to (i) together with the amino acid 101 E, 101 D, 101 N, 101Q, 101A, 101G, or 101S (according to BPN’ numbering). In one embodiment, said protease is characterized by comprising the mutation (according to BPN’ numbering) R101E, or S3T + V4I + V205I, or R101E and S3T, V4I, and V205I, or S3T + V4I + V199M + V205I + L217D, and having proteo lytic activity.
In one embodiment, protease according to SEQ ID NO:22 as described in EP 1921147 is char acterized by comprising the mutation (according to BPN’ numbering) S3T + V4I + S9R + A15T + V68A + D99S + R101S + A103S + 1104V + N218D, and having proteolytic activity.
The inventive composition may comprise a combination of at least two proteases, preferably selected from the group of serine endopeptidases (EC 3.4.21), more preferably selected from the group of subtilisin type proteases (EC 3.4.21.62) - all as disclosed above.
In one embodiment of the present invention, inventive compositions comprise at least one man- nanase. Preferably, the mannanase is an endo-1,4^-mannosidase (EC 3.2.1.78).
A polypeptide having mannan degrading activity or mannanase activity may be tested for ac cording to standard test procedures known in the art, such as by applying a solution to be tested to 4 mm diameter holes punched out in agar plates containing 0.2% AZCL galactomannan (car- ob), i.e. substrate for the assay of endo-1,4-beta-D-mannanase available as CatNo. I-AZGMA from the company Megazyme (Megazyme's Internet address: http://www. megazyme. com/Purchase/index. html). Mannan degrading activity may be tested in a liquid assay using carob galactomannan dyed with Remazol Brilliant Bue as described in McCleary, B. V.
(1978). Carbohydrate Research, 67(1), 213-221. Another method for testing mannan degrading activity uses detection of reducing sugars when incubated with substrate such as guar gum or locust bean gut - for reference see Miller, G. L.Use of Dinitrosalicylic Acid Reagent for Determi nation of Reducing Sugars. Analytical Chemistry 1959; 31: 426-428.
At least one mannanase comprised in the composition of the invention may be selected from alkaline mannanase of Family 5 or 26. The term “alkaline mannanase” is meant to encompass mannanases having an enzymatic activity of at least 40% of its maximum activity at a given pH ranging from 7 to 12, preferably 7.5 to10.5.
At least one mannanase comprised in the composition of the invention may be selected from mannanases originating from Bacillus organisms, such as described in JP-0304706, JP- 63056289, JP-63036774, JP-08051975, WO 97/11164, WO 91/18974, WO 97/11164,
WO 2014/100018. Suitable mannanases are further described in WO 99/064619. The man nanase may be selected from mannanases originating from Trichoderma organisms, such as disclosed in WO 93/24622.
At least one mannanase may be selected from a commercially available mannanase such as Mannaway® (Novozymes A/S) (SEQ ID NO: 1 of W02009074685).
In one embodiment of the present invention, inventive compositions comprise at least one am ylase. “Amylases” according to the invention (alpha and/or beta) include those of bacterial or fungal origin (EC 3.2.1.1 and 3.2.1.2, respectively). Preferably, component (b) comprises at least one enzyme selected from the group of alpha-amylases (EC 3.2.1.1). Chemically modified or protein engineered mutants are included.
Amylases according to the invention have “amylolytic activity” or “amylase activity” involving (endo)hydrolysis of glucosidic linkages in polysaccharides alpha-amylase activity may be de termined by assays for measurement of alpha-amylase activity which are known to those skilled in the art. Examples for assays measuring alpha-amylase activity are: alpha-amylase activity can be determined by a method employing Phadebas tablets as sub strate (Phadebas Amylase Test, supplied by Magle Life Science). Starch is hydrolyzed by the alpha-amylase giving soluble blue fragments. The absorbance of the resulting blue solution, measured spectrophotometrically at 620 nm, is a function of the alpha-amylase activity. The measured absorbance is directly proportional to the specific activity (activity/mg of pure alpha- amylase protein) of the alpha-amylase in question under the given set of conditions. Alpha-amylase activity can also be determined by a method employing the Ethyliden-4- nitrophenyl-alpha-D-maltoheptaosid (EPS). D-maltoheptaoside is a blocked oligosaccharide which can be cleaved by an endo-amylase. Following the cleavage, the alpha-glucosidase in cluded in the kit to digest the substrate to liberate a free PNP molecule which has a yellow color and thus can be measured by visible spectophotometry at 405nm. Kits containing EPS sub strate and alpha-glucosidase is manufactured by Roche Costum Biotech (cat. No. 10880078103). The slope of the time dependent absorption-curve is directly proportional to the specific activity (activity per mg enzyme) of the alpha-amylase in question under the given set of conditions.
Amylolytic activity may be provided in units per gram enzyme. For example, 1 unit alpha- amylase may liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20°C.
In one aspect of the present invention, at least one amylase is selected from:
• amylases from Bacillus licheniformis having SEQ ID NO:2 as described in WO 95/10603. Suitable variants are described in WO 95/10603 comprising one or more substitutions in the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188,
190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444 which have amylolytic activity. Variants are described in WO 94/02597, WO 94/018314, WO 97/043424 and SEQ ID NO:4 of WO 99/019467.
• amylases from B. stearothermophilus having SEQ ID NO:6 as disclosed in WO 02/10355 or an amylase with optionally having a C-terminal truncation over the wildtype sequence. Suitable variants of SEQ ID NO:6 include those comprising a deletion in positions 181 and/or 182 and/or a substitution in position 193.
• amylases from Bacillus sp.707 having SEQ ID NO:6 as disclosed in WO 99/19467. Pre ferred variants of SEQ NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216 and K269.
• amylases from Bacillus halmapalus having SEQ ID NO:2 or SEQ ID NO:7 as described in WO 96/23872, also described herein as SP-722. Preferred variants are described in WO 97/3296, WO 99/194671 and WO 2013/001078.
• amylases from Bacillus sp. DSM 12649 having SEQ ID NO:4 as disclosed in WO 00/22103.
• amylases from Bacillus strain TS-23 having SEQ ID NO:2 as disclosed in WO 2009/061380.
• amylases from Cytophaga sp. having SEQ ID NO:1 as disclosed in WO 2013/184577.
• amylases from Bacillus megaterium DSM 90 having SEQ ID NO:1 as disclosed in WO 2010/104675.
• amylases from Bacillus sp. comprising amino acids 1 to 485 of SEQ ID NO:2 as described in WO 00/60060.
• amylases from Bacillus amyloliquefaciens or variants thereof, preferably selected from amylases according to SEQ ID NO: 3 as described in WO 2016/092009.
• amylases having SEQ ID NO: 12 as described in WO 2006/002643 or amylase variants comprising the substitutions Y295F and M202LITV within said SEQ ID NO: 12. • amylases having SEQ ID NO:6 as described in WO 2011/098531 or amylase variants comprising a substitution at one or more positions selected from the group consisting of 193 [G,A,S,T or M], 195 [F,W,Y,L,I or V], 197 [F,W,Y,L,I or V], 198 [Q or N], 200 [F,W,Y,L,I or V], 203 [F,W,Y,L,I or V], 206 [F,W,Y,N,L,I,V,H,Q,D or E], 210 [F,W,Y,L,I or V], 212 [F,W,Y,L,I or V], 213 [G,A,S,T or M] and 243 [F,W,Y,L,I or V] within said SEQ ID NO:6.
• amylases having SEQ ID NO:1 as described in WO 2013/001078 or amylase vari ants comprising an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and
G477 within said SEQ ID NO:1.
• amylases having SEQ ID NO:2 as described in WO 2013/001087 or amylase vari ants comprising a deletion of positions 181+182, or 182+183, or 183+184, within said SEQ ID NO:2, optionally comprising one or two or more modifications in any of positions corresponding to WHO, W159, W167, Q169, W189, E194, N260, F262, W284, F289, G304, G305, R320, W347, W439, W469, G476 and G477 within said SEQ ID NO:2.
• amylases which are hybrid alpha-amylases from above mentioned amylases as for exam ple as described in WO 2006/066594;
• hybrid amylases according to WO 2014/183920 with A and B domains having at least 90% identity to SEQ ID NO:2 of WO 2014/183920 and a C domain having at least 90% identity to SEQ ID NO:6 of WO 2014/183920, wherein the hybrid amylase has amylolytic activity; preferably the hybrid alpha-amylase is at least 95% identical to SEQ ID NO: 23 of WO 2014/183920 and having amylolytic activity;
• hybrid amylase according to WO 2014/183921 with A and B domains having at least 75% identity to SEQ ID NO: 2, SEQ ID NO: 15, SEQ ID NO: 20, SEQ ID NO: 23, SEQ ID
NO: 29, SEQ ID NO: 26, SEQ ID NO: 32, and SEQ ID NO: 39 as disclosed in WO 2014/183921 and a C domain having at least 90% identity to SEQ ID NO: 6 of WO 2014/183921, wherein the hybrid amylase has amylolytic activity; preferably, the hybrid alpha-amylase is at least 95% identical to SEQ ID NO: 30 as disclosed in WO 2014/183921 and having amylolytic activity.
Suitable amylases include also those, which are variants of the above described amylases which have amylolytic activity. In one embodiment amylase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment amylase variants having amylolytic activity are at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical to the full length polypeptide sequence of the parent enzyme as disclosed above. In another embodiment, the invention relates to amylase variants comprising conservative mu tations not pertaining the functional domain of the respective amylase. Amylase variants of this embodiment having amylolytic activity may be at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar to the full length polypeptide sequence of the parent enzyme.
In one embodiment, amylase variants have amylolytic activity according to the present invention when said amylase variants exhibit increased amylolytic activity when compared to the par ent amylase.
In one embodiment, amylase variants have amylolytic activity according to the present invention when said amylase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the amylolytic activity of the respective parent amylase.
In one embodiment, at least one amylase is selected from commercially available amylases which include but are not limited to products sold under the trade names Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liq uozyme X and BAN™, Amplify™, Amplify Prime™ (from Novozymes A/S), and Rapidase™, Purastar™, Powerase™, Effectenz™ (M100 from DuPont), Preferenz™ (S1000, S110 and F1000; from DuPont), PrimaGreen™ (ALL; DuPont), Optisize™ (DuPont).
At least one enzyme comprised in the composition of the invention may be selected from the group of cellulases. Cellulases according to the invention include those of bacterial or fungal origin.
At least one cellulase comprised in the composition of the invention may be selected from cellobiohydrolase (1,4-P-D-glucan cellobiohydrolase, EC 3.2.1.91), endo-ss-1 ,4-glucanase (EC 3.2.1.4) and ss-glucosidase (EC 3.2.1.21). Endoglucanases of EC class 3.2.1.4 may be named endoglucanase, endo-1,4-ss-D-glucan 4-glucano hydrolase, endo-1 ,4-beta-glucanase, carboxymethyl cellulase, and beta-1, 4-glucanase.
Endoglucanases may be classified by amino acid sequence similarities (Henrissat, B. Accessed at UniProt 10/26/2011) under family 5 containing more than 20 endoglucanases of EC 3.2.1.4. Reference is also made to T.-M. Enveri, "Microbial Cellulases" in W.M. Fogarty, Microbial En zymes and Biotechnology, Applied Science Publishers, p. 183-224 (1983); Methods in Enzy- mology, (1988) Vol. 160, p. 200-391 (edited by Wood, W.A. and Kellogg, S.T.); Beguin, P., "Mo lecular Biology of Cellulose Degradation", Annu. Rev. Microbiol. (1990), Vol. 44, pp. 219248; Begun, P. and Aubert, J-P., "The biological degradation of cellulose", FEMS Microbiology Re- views 13 (1994) p.25-58; Henrissat, B., "Cellulases and their interaction with cellulose", Cellu lose (1994), Vol. 1, pp. 169-196.
Preferably, at least one cellulase comprised in the composition of the invention is selected of the glycosyl hydrolase family 7 (GH7, pfam00840), preferably selected from endoglucanases (EC 3.2.1.4).
"Cellulases", “cellulase enzymes” or “cellulolytic enzymes” according to the invention are en zymes involved in hydrolysis of cellulose. Assays for measurement of “cellulase activity” or “cel lulolytic activity” are known to those skilled in the art. For example, cellulolytic activity may be determined by virtue of the fact that cellulase hydrolyses carboxymethyl cellulose to reducing carbohydrates, the reducing ability of which is determined colorimetrically by means of the ferri- cyanide reaction, according to Hoffman, W. S., J. Biol. Chem. 120, 51 (1937).
Cellulolytic activity may be provided in units per gram enzyme. For example, 1 unit may liberate 1.0 pmole of glucose from cellulose in one hour at pH 5.0 at 37°C (2 hour incubation time).
In one embodiment, at least one cellulase comprised in the composition of the invention is se lected from cellulases comprising a cellulose binding domain. In one embodiment, at least one cellulase is selected from cellulases comprising a catalytic domain only, meaning that the cellu lase lacks cellulose binding domain.
In one embodiment, the composition of the invention comprises at least one endoglucanases of EC class 3.2.1.4 is originating from
• Bacillus, such as Bacillus sp. CBS 670.93 and CBS 669.93
• Melanocarpus, such as Melanocarpus albomyces as disclosed in WO 97/14804
• Clostridium, e.g. Clostridium thermocellum
• Humicola, such as Humicola insolens (DSM1800) as disclosed in EP 0495257, EP 0531315, EP 0531372, US 4435307, US 5648263, US 5776757, WO 89/09259, WO 91/17244, WO 94/07998 (sequence displayed in figure 1 “43kd human variants there of), WO 95/24471, WO 96/11262 and WO 98/12307.
• Fusarium, such as Fusarium oxysporum e.g. strain J79 (DSM2672) as disclosed in EP 0495257, EP 0531315, EP 0531372, US 5648263, US 5776757, WO 89/09259, WO 91/17244, WO 95/24471 and WO 96/11262
• Thielavia, such as Thielavia terrestris or Myceliophthora thermophila strain CBS 11765 as disclosed in EP 0531315, US 5648263, US 5776757, WO 89/09259, WO 91/17244, WO 95/24471, WO 96/11262, WO 96/29397 (SEQ ID NO: 9 and variants thereof), and WO 98/12307.
• Trichoderma, such as Trichoderma reesei, Trichoderma longibrachiatum or Trichoderma harzianum as disclosed in EP 1305432, EP 1240525, WO 92/06165, WO 94/21801, WO 94/26880, WO 95/02043, WO 95/24471 and WO 02/099091. • Aspergillus, such as Aspergillus aculeatus as disclosed in WO 93/17244
• Erwinia, such as Erwinia chrysanthermi as described by M. H. Boyer et. al. in European Journal of Biochemistry, vol. 162, page 311-316 (1987).
• Acremonium such as Acremonium sp., Acremonium persicinum, Acremonium acremonium, Acremonium brachypenium, Ac remoni- um dichromosporum, Acremonium obclavatum, Acremonium pinkertoniae, Acremonium roseogriseum, Acremonium incoloratum, and Acremonium furatum as disclosed in WO 96/11262 and WO 96/29397 (SEQ ID NO: 5 and variants thereof).
• Cellvibrio such as Cellvibrio mixtus DSM 11683, Cellvibrio mixtus DSM 11684, Cellvibrio mixtus DSM 11685, Cellvibrio mixtus ACM
2601, Cellvibrio mixtus DSM 1523, and Cellvibrio gilvus DSM 11686, as disclosed in WO 98/08940.
• Cephalosporium, such as Cephalosporium sp. RYM-202 as disclosed in WO 96/11262. Suitable cellulases include also those, which are variants of the above described cellulases which have cellulolytic activity. In one embodiment cellulase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment cellulase variants having cellulolytic activi ty are at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar and/or identical to the full length polypeptide sequence of the parent enzyme as disclosed above.
In one embodiment, the composition of the invention comprises a Humicola insolens DSM 1800 cellulase complex having endoglucanase, cellobiohydrolase and beta-glucosidase activi ty.
In one embodiment, the composition of the invention comprises at least one Humicola insolens DSM 1800 endoglucanase (EC 3.2.1.4) having the amino acid se quence disclosed in Fig. 14A-E of WO 91/17244, preferably amino acids 20-434 according said sequence, more preferably having one or more substitutions at positions selected from 182,
223, and 231, most preferably selected from P182S, A223V, and A231V. In one embodiment, the endoglucanase is at least 80% similar and/or identical to a polypeptide according to SEQ ID NO: 2 of WO 95/02675.
In one embodiment, the composition of the invention comprises at least a Bacillus sp. cellulase (EC 3.2.1.4) selected from a polypeptide at least 80% similar and/or identical to the amino acid sequence of position 1 to position 773 of SEQ ID NO: 2 of WO 2004/053039 or a catalytically active fragment thereof. In one embodiment, the composition of the invention comprises at least a Thielavia terrestris cellulase (EC 3.2.1.4) having a polypeptide at least 80% similar and/or identical to the amino acid sequence of position 1 to position 299 of SEQ ID NO: 4 of WO 2004/053039 or a catalytically active fragment thereof.
In one embodiment, cellulase variants have cellulolytic activity according to the present inven tion when said cellulase variants exhibit increased cellulolytic activity when compared to the parent cellulase.
In one embodiment, cellulase variants have cellulolytic activity according to the present inven tion when said cellulase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the cellulolytic activity of the respective parent cellulase.
At least one cellulase may be selected from Renozyme®, Celluzyme®, Celluclean®, Endolase® and Carezyme® (Novozymes A/S), Clazinase™, and Puradax HA™ (Genencor Int. Inc.), and KAC-500(B)™ (Kao Corporation). At least one peroxidases may be selected from Guardzyme™ (Novozymes A/S).
At least one enzyme comprised in the composition of the invention may be a nuclease. Prefera bly, the nuclease is selected from the group of DNA degrading enzymes (DNAse). Said en zymes usually catalyzes the hydrolytic cleavage of phosphodiester linkages in DNA.
The DNAses are classified e.g. in E.C. 3.1.11, E.C. 3.1.12, E.C. 3.1.15, E.C. 3.1.16, E.C.
3.1.21, E.C 3.1.22, E.C 3.1.23, E.C 3.1.24 and E.C.3.1.25 as well as EC 3.1.21.X, where X=1,
2, 3, 4, 5, 6, 7, 8 or 9.
DNAse activity may be determined on DNAse Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), which should be prepared according to the manual from supplier. Briefly, 21 g of agar is dissolved in 500 ml water and then autoclaved for 15 min at 121 °C. Autoclaved agar is temperated 10 to 48°C in water bath, and 20 ml of agar is to be poured into petridishes with and allowed to solidify by incubation o/n at room temperature. On solidified agar plates, 5 pi of enzyme solution is added and DNAse activity is observed as colorless zones around the spot ted enzyme solutions.
DNAse activity may be determined by using the DNAseAlert™ Kit (11-02-01-04,
IDT Intergrated DNA Technologies) according to the supplier's manual. Briefly, 95mI DNase sample is mixed with 5mI substrate in a microtiter plate, and fluorescence is immediately meas ured using e.g. a Clariostar microtiter reader from BMG Labtech (536 nm excitation, 556 nm emission). At least one DNAse comprised in the composition of the invention may be selected from DNAses originating from Bacillus such as from Bacillus cibi, Bacillus horikoshii, Bacillus horneckiae, Bacillus idriensis, Bacillus algicola, B acillus vietnamensis, Bacillus hwajinpoensis, Paenibacillus mucilanginosus, Bacillus indi- cus, Bacillus luciferensis, Bacillus marisflavr, and variants thereof. In one embodiment, at least one DNAse comprised in the composition of the invention is selected from polypeptides 80% identical to SEQ ID NO: 1 of WO 2019/081724. Said polypeptide may comprise one or more substitutions at positions selected from T1, G4, S7, K8, S9, S13, N16, T22, S25, S27, D32, L33, S39, G41 , S42, D45, Q48, S57, S59, N61, T65, S66, V76, F78, P91, S101, S106, Q109, A112, S116, T127, S130, T138, Q140, S144, A147, C148, W154, T157, Y159, G162, S167, Q174, G175, L177, S179, and C180 - all as disclosed in WO 2019/081724 and WO 2019/081721.
The composition of the invention may comprise DNAse variants having DNA degrading activity which are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar and/or identical when compared to the full-length polypeptide sequence of the cor responding parent enzyme as disclosed above.
According to the present invention, the composition of the invention may comprise a combina tion of at least two DNAses.
At least one enzyme may be selected from acyltransferases (E.C 2.3.1) or perhydrolases. Perhydrolases catalyze perhydrolysis reaction that results in the production of a peracid from a carboxylic acid ester (acyl) substrate in the presence of a source of peroxygen (e.g., hydrogen peroxide). While many enzymes perform this reaction at low levels, perhydrolases exhibit a high perhydrolysis: hydrolysis ratio, often greater than 1. Suitable perhydrolases may be of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful perhydrolases include acyltransferases with homology to Candida antarctica lipase A (WO 2010/111143) and naturally occur ring Mycobacterium perhydrolase enzymes, or variants thereof - e.g. a variant of Mycobacterium smegmatis as described in WO 2005/056782, WO 2008/063400, US 2008145353, and US 2007167344; perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant (WO 2010/100028).
In order to supply hydrogen peroxide for bleaching purposes in detergent formulations, oxidore- ductase enzymes may be employed. The catalyzed reaction is the transfer of electrons from the organic substrate, for the glucose oxidase, for example, from the glucose, to the oxygen as the electron acceptor with the formation of the desired hydrogen peroxide. “Peroxidase activity” may be measured by the ABTS method as described in Childs et al. 1975 (Biochemical J, 145, p. 93-103) and commercial kits are available from different suppliers. Other measuring methods are known to those known in the art.
The hydrogen peroxide-producing oxidoreductases herein concern enzymes that produce hy drogen peroxide, using oxygen as an electron acceptor. In this regard, particularly preferred oxidoreductases include those of the EC classes E.C. 1.1.3 (CH — OH as the electron donor), E.C. 1.2.3 (aldehyde or oxo groups as the electron donor), E.C. 1.4.3 (CH — NH2 as the donor), E.C. 1.7.3 (N-containing groups as the donor) and E.C. 1.8.3 (S-containing groups as the do nor) come into consideration, wherein enzymes of the EC class EC 1.1.3.
In a preferred embodiment, the hydrogen peroxide-producing oxidoreductase is one in which a sugar is used as the electron donor. The hydrogen peroxide-producing and sugar-oxidizing oxi doreductase is preferably chosen from glucose oxidase (EC 1.1.3.4), hexose oxidase (EC 1.1.3.5), galactose oxidase (EC 1.1.3.9) and pyranose oxidase (EC 1.1.3.10). According to the invention, glucose oxidase (EC 1.1.3.4) is particularly preferred. In one embodiment, aromatic compounds are added that interact with the enzymes to enhance the activity of the oxidoreduc tases (Enhancer) or to facilitate electron flow (Mediators) between the oxidizing enzymes and the stains over strongly different redox potentials.
At least one enzyme may be selected from oxidases such as amino acid oxidase and polyol oxidase (e.g., WO 2008/051491). Oxidases and their corresponding substrates may be used as hydrogen peroxide generating enzyme systems, and thus a source of hydrogen peroxide. Several enzymes, such as peroxidases, haloperoxidases and perhydrolases, require a source of hydrogen peroxide. By studying EC 1.1.3._, EC 1.2.3._, EC 1.4.3._, and EC 1.5.3._ or simi lar classes (under the International Union of Biochemistry), other examples of such combina tions of oxidases and substrates are easily recognized by one skilled in the art.
In one embodiment at least one oxidoreductase is chosen from enzymes that use peroxides as the electron accepter (EC-Classes 1.11 or 1.11.1), in particular, from catalases (EC 1.11.1.6), peroxidases (EC 1.11.1.7), glutathione peroxidases (EC 1.11.1.9), chloride peroxidases (EC 1.11.1.10), manganese peroxidases (EC 1.11.1.13) and/or lignin peroxidases (EC 1.11.1.14), which can also be generally classified under the term peroxidases. Examples of use ful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, WO 98/10060 and WO 98/15257.
A peroxidase for use in the invention also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions. In an embodiment, the haloperoxidase is a chloroperoxidase. In one embodiment, the haloperoxidase is a vanadium haloperoxidase, i.e. , a vanadate-containing haloperoxidase.
In one embodiment of the present invention the vanadate-containing haloperoxidase is com bined with a source of chloride ion.
Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis. Haloperoxidases h ave also been isolated from bacteria such as Pseudomonas, e.g. P. pyrrocinia, and Streptomyces, e.g. S. aureofaciens.
In one embodiment, the haloperoxidase is from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartlebii as described in WO 2001/79459, Dendryphiella salina as described in
WO 2001/79458, Phaeotrichoconis crotalarie as described in WO 2001/79461, or Geniculosporium sp. as described in WO 2001/79460.
Commercially available peroxidases include Guardzyme™ (Novozymes A/S), PrimaGreen™ Oxy (DuPont).
At least one enzyme may be selected from laccases. The term “laccase activity” is defined here in as covered by enzyme classification EC 1.10.3.2, or a similar activity, such as a catechol oxi dase activity (EC 1.10.3.1), o-aminophenol oxidase activity (EC 1.10.3.4), or bilirubin oxidase activity (EC 1.3.3.5), that catalyzes the oxidation of a substrate using molecular oxygen. ’’Laccase activity” is determined by oxidation of syringaldazin under aerobic conditions. The vio let colour produced is measured at 530 nm. The analytical conditions are 19 mM syringaldazin, 23 mM Tris/maleate buffer, pH 7.5, 30°C, and 1 min reaction time.
Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts; e.g. Polyporus radiata (WO 92/01046), Coriolus hirsutus (JP 2238885), Coprinopsis cinerea (WO 97/08325), Myceliophthora thermophila (WO 95/33836)).
In one embodiment, laccase is selected from those as described in SEQ ID NO: 2, 4, 6, and 8 of WO 2009/127702 and variants thereof.
At least one laccase may be selected from commercially available laccase Denilite® 1 and 2 from Novozymes. In one embodiment, at least one enzyme is selected from lyases. “Lyase” may be a pectate ly ase derived from Bacillus, particularly B. licheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6,124,127, WO 99/027083, WO 99/027084,
WO 2002/006442, WO 2002/092741, WO 2003/095638.
Commercially available pectate lyases are Xpect™, Pectawash™ and Pectaway™ (Novozymes A/S); PrimaGreen™, EcoScour (DuPont).
In one embodiment, at least one enzyme is selected from the group of pectinases (EC 3.2.1.15 gycosidase), and/or arabinases (EC 3.2.1.99), and/or galactanases (EC 3.2.1.89 and EC 3.2.1.181), and/or xylanases (EC 3.2.1.8, EC 3.2.1.32, EC 3.2.1.136, and EC 3.2.1.156).
Combination of different enzymes can also be used. Any combination of the enzymes cited above can be used. The combination of enzymes can include several enzymes of a different class, several different enzymes of the same class, and combinations thereof. Preferably the combination of enzymes is selected from the group consisting of amylase, protease, lipase, mannanase, nuclease, and cellulase; protease, lipase, mannanase, and cellulase; protease, lipase, and mannanase; protease and lipase; protease and mannanase, preferably the combi nation of enzymes is protease, lipase, and mannanase.
It is preferred to use a combination of lipase and protease in compositions, for example 1 to 2% by weight of protease and 0.1 to 0.5% by weight of lipase, both referring to the total weight of the composition. Further, it is preferred to use a combination of lipase, protease and a man nanase in the compositions, for example 1 to 2% by weight of protease, 0.1 to 0.5% by weight of lipase and 0.1 to 0.5% by weight of mannanase, all referring to the total weight of the compo sition. Further, it is preferred to use a protease in the compositions, for example 1 to 2% by weight of protease.
In the context of the present invention, lipase and/or protease and/or mannanase is deemed called stable when its enzymatic activity “available in application” equals at least 60% when compared to the initial enzymatic activity before storage. An enzyme may be called stable within this invention if its enzymatic activity available in application is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% when compared to the initial enzymatic activity before storage.
Subtracting a% from 100% gives the “loss of enzymatic activity during storage” when compared to the initial enzymatic activity before storage. In one embodiment, an enzyme is stable accord- ing to the invention when essentially no loss of enzymatic activity occurs during storage, i.e. loss in enzymatic activity equals 0% when compared to the initial enzymatic activity before stor age. Essentially no loss of enzymatic activity within this invention may mean that the loss of enzymatic activity is less than 30%, less than 25%, less than 20%, less than 15%, less than 10%, less than 9%, less than 8%, less than 7%, less than 6%, less than 5%.
In one embodiment, the present invention is directed to a detergent composition comprising (A) at least one polymer comprising
(a) a core that bears one to 3 moieties of the general formula (I)
Figure imgf000025_0001
wherein Z are different or the same and selected from C2-Ci2-alkylene and C3-C12- cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non- substituted or substituted with one or more 0-CrC4-alkyl groups and wherein C3- Ci2-cycloalkylene may bear one to three methyl groups,
X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, preferred are methyl and more preferred is hydrogen, n is in the range of from 1 to 4,
(b) polyalkylene oxide chains; and
(B) at least one enzyme, preferably selected from the group consisting of amylase, protease, lipase, mannanase, xylanase, nuclease, cellulase, and combinations thereof; preferably at least one protease, and optionally, at least one lipase, and optionally at least one man nanase; preferably at least one protease, and at least one lipase, and optionally at least one mannanase; preferably at least one protease, and at least one lipase, and at least one mannanase.
The detergent composition can be solid or liquid. Preferably, the detergent composition is liquid. The composition of the present invention, as further described herein, can be used in laundry and/or hard surface cleaning, both either in home care or l&l applications, with hard surface cleaning being dish washing (manual (hand) dish washing or automated dish washing), but also meaning cleaning of hard surfaces inside a washing machine (dishwashing or laundry washing machine, preferably laundry washing machine). In one embodiment of the present invention, inventive compositions comprise at least one sur factant (C). The surfactant can be selected from anionic surfactant, cationic surfactant, non ionic surfactant, amphoteric surfactants, amine oxide surfactants, and combinations thereof, preferably, the surfactant is an anionic surfactant.
Examples of anionic surfactants are alkali metal and ammonium salts of Cs-Cis-alkyl sulfates, of Cs-Ci8-fatty alcohol polyether sulfates, of sulfuric acid half-esters of ethoxylated C4-C12- alkylphenols (ethoxylation: 1 to 50 mol of ethylene oxide/mol), C12-C18 sulfo fatty acid alkyl esters, for example of C12-C18 sulfo fatty acid methyl esters, furthermore of Ci2-Ci8-alkylsulfonic acids and of Cio-Ci8-alkylarylsulfonic acids. Preference is given to the alkali metal salts of the aforementioned compounds, particularly preferably the sodium salts.
Further examples of anionic surfactants are soaps, for example the sodium or potassium salts of stearic acid, oleic acid, palmitic acid, ether carboxylates, and alkylether phosphates.
In a preferred embodiment of the present invention, anionic surfactant is selected from com pounds according to general formula (II)
R1-0(CH2CH20)X-S03M (II) wherein
R1 n-Cio-Ci8-alkyl, especially with an even number of carbon atoms, for example n-decyl, n- dodecyl, n-tetradecyl, n-hexadecyl, or n-octadecyl, preferably Cio-Ci4-alkyl, and even more preferably n-Ci2-alkyl, x being a number in the range of from 1 to 5, preferably 2 to 4 and even more preferably 3.
M being selected from alkali metals, preferably potassium and even more preferably sodium.
In anionic surfactant, x may be an average number and therefore n is not necessarily a whole number, while in individual molecules according to formula (I), x denotes a whole number.
In one embodiment of the present invention, inventive compositions may contain 0.1 to 60 % by weight of anionic surfactant, preferably 5 to 50 % by weight.
Inventive compositions may comprise ingredients other than the aforementioned. Examples are non-ionic surfactants, fragrances, dyestuffs, biocides, preservatives, enzymes, hydrotropes, builders, viscosity modifiers, polymers, buffers, defoamers, and anti-corrosion additives.
Preferred inventive compositions may contain one or more non-ionic surfactants.
Preferred non-ionic surfactants are alkoxylated alcohols, di- and multiblock copolymers of eth ylene oxide and propylene oxide and reaction products of sorbitan with ethylene oxide or pro pylene oxide, alkyl polyglycosides (APG), hydroxyalkyl mixed ethers and amine oxides. Preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds of the general formula (III a)
Figure imgf000027_0001
in which the variables are defined as follows:
R2 is identical or different and selected from hydrogen and linear Ci-Cio-alkyl, preferably in each case identical and ethyl and particularly preferably hydrogen or methyl,
R3 is selected from Cs-C22-alkyl, branched or linear, for example n-CsH^, n-CioHbi, n-Ci2H25, n-C14H29, n-C16H33 or n-CisH37,
R4 is selected from Ci-Cio-alkyl, methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, isopentyl, sec-pentyl, neopentyl, 1,2-dimethylpropyl, isoamyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl or isodecyl,
The variables e and f are in the range from zero to 300, where the sum of e and f is at least one, preferably in the range of from 3 to 50. Preferably, e is in the range from 1 to 100 and f is in the range from 0 to 30.
In one embodiment, compounds of the general formula (II) may be block copolymers or random copolymers, preference being given to block copolymers.
Other preferred examples of alkoxylated alcohols are, for example, compounds of the general formula (III b)
Figure imgf000027_0002
in which the variables are defined as follows:
R2 is identical or different and selected from hydrogen and linear Ci-Co-alkyl, preferably iden tical in each case and ethyl and particularly preferably hydrogen or methyl,
R5 is selected from C6-C2o-alkyl, branched or linear, in particular n-CsH^, n-CioHbi, n-Ci2H25, n-C13H27, n-Ci5H3i, n-Ci4H29, n-Ci6H33, n-CisH37, a is a number in the range from zero to 10, preferably from 1 to 6, b is a number in the range from 1 to 80, preferably from 4 to 20, d is a number in the range from zero to 50, preferably 4 to 25.
The sum a + b + d is preferably in the range of from 5 to 100, even more preferably in the range of from 9 to 50.
Compounds of the general formula (III) may be block copolymers or random copolymers, pref erence being given to block copolymers.
Further suitable nonionic surfactants are selected from di- and multiblock copolymers, com posed of ethylene oxide and propylene oxide. Further suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Amine oxides or alkyl polyglycosides, espe cially linear C4-Ci6-alkyl polyglucosides and branched Cs-Cn-alkyl polyglycosides such as com pounds of general average formula (IV) are likewise suitable.
Figure imgf000028_0001
wherein:
R6 is CrC4-alkyl, in particular ethyl, n-propyl or isopropyl,
R7 is -(CH2)2-R6,
G1 is selected from monosaccharides with 4 to 6 carbon atoms, especially from glucose and xylose, y in the range of from 1.1 to 4, y being an average number,
Further examples of non-ionic surfactants are compounds of general formula (V) and (VI)
Figure imgf000028_0002
AO is selected from ethylene oxide, propylene oxide and butylene oxide,
EO is ethylene oxide, CH2CH2-O,
R8 selected from Cs-Cis-alkyl, branched or linear, and R5 is defined as above.
A30 is selected from propylene oxide and butylene oxide, w is a number in the range of from 15 to 70, preferably 30 to 50, w1 and w3 are numbers in the range of from 1 to 5, and w2 is a number in the range of from 13 to 35.
An overview of suitable further nonionic surfactants can be found in EP-A 0 851 023 and in DE- A 198 19 187.
Mixtures of two or more different nonionic surfactants selected from the foregoing may also be present.
Other surfactants that may be present are selected from amphoteric (zwitterionic) surfactants and anionic surfactants and mixtures thereof.
Examples of amphoteric surfactants are those that bear a positive and a negative charge in the same molecule under use conditions. Preferred examples of amphoteric surfactants are so- called betaine-surfactants. Many examples of betaine-surfactants bear one quaternized nitrogen atom and one carboxylic acid group per molecule. A particularly preferred example of amphoter ic surfactants is cocamidopropyl betaine (lauramidopropyl betaine).
Examples of amine oxide surfactants are compounds of the general formula (VII)
R9R10R11N O (VII) wherein R9, R10, and R11 are selected independently from each other from aliphatic, cycloali phatic or C2-C4-alkylene Cio-C2o-alkylamido moieties. Preferably, R9 is selected from C8-C20- alkyl or C2-C4-alkylene Cio-C2o-alkylamido and R10 and R11 are both methyl.
A particularly preferred example is lauryl dimethyl aminoxide, sometimes also called lauramine oxide. A further particularly preferred example is cocamidylpropyl dimethylaminoxide, some times also called cocamidopropylamine oxide.
In one embodiment of the present invention, inventive compositions may contain 0.1 to 60 % by weight of at least one surfactant, selected from non-ionic surfactants, amphoteric surfactants and amine oxide surfactants. In a preferred embodiment, inventive solid detergent compositions for cleaners and especially those for automatic dishwashing do not contain any anionic surfactant.
Inventive compositions may contain at least one bleaching agent, also referred to as bleach. Bleaching agents may be selected from chlorine bleach and peroxide bleach, and peroxide bleach may be selected from inorganic peroxide bleach and organic peroxide bleach. Preferred are inorganic peroxide bleaches, selected from alkali metal percarbonate, alkali metal perborate and alkali metal persulfate.
Examples of organic peroxide bleaches are organic percarboxylic acids, especially organic per- carboxylic acids.
In inventive compositions, alkali metal percarbonates, especially sodium percarbonates, are preferably used in coated form. Such coatings may be of organic or inorganic nature. Examples are glycerol, sodium sulfate, silicate, sodium carbonate, and combinations of at least two of the foregoing, for example combinations of sodium carbonate and sodium sulfate.
Suitable chlorine-containing bleaches are, for example, 1,3-dichloro-5,5-dimethylhydantoin, N-chlorosulfamide, chloramine T, chloramine B, sodium hypochlorite, calcium hypochlorite, magnesium hypochlorite, potassium hypochlorite, potassium dichloroisocyanurate and sodium dichloroisocyanurate.
Inventive compositions may comprise, for example, in the range from 3 to 10% by weight of chlorine-containing bleach.
Inventive compositions may comprise one or more bleach catalysts. Bleach catalysts can be selected from bleach-boosting transition metal salts or transition metal complexes such as, for example, manganese-, iron-, cobalt-, ruthenium- or molybdenum-salen complexes or carbonyl complexes. Manganese, iron, cobalt, ruthenium, molybdenum, titanium, vanadium and copper complexes with nitrogen-containing tripod ligands and also cobalt-, iron-, copper- and rutheni um-amine complexes can also be used as bleach catalysts.
Inventive compositions may comprise one or more bleach activators, for example N- methylmorpholinium-acetonitrile salts (“MMA salts”), trimethylammonium acetonitrile salts, N- acylimides such as, for example, N-nonanoylsuccinimide, 1,5-diacetyl-2,2-dioxohexahydro- 1,3,5-triazine (“DADHT”) or nitrile quats (trimethylammonium acetonitrile salts).
Further examples of suitable bleach activators are tetraacetylethylenediamine (TAED) and tetraacetylhexylenediamine.
Examples of fragrances are benzyl salicylate, 2-(4-tert.-butylphenyl) 2-methylpropional, com mercially available as Lilial®, and hexyl cinnamaldehyde. Examples of dyestuffs are Acid Blue 9, Acid Yellow 3, Acid Yellow 23, Acid Yellow 73, Pigment Yellow 101, Acid Green 1, Solvent Green 7, and Acid Green 25.
Inventive compositions may contain one or more preservatives or biocides. Biocides and pre servatives prevent alterations of inventive liquid detergent compositions due to attacks from microorganisms. Instead of or in addition to their function as preservatives, some biocides, as part of the laundry detergent compositions may help to kill or deactivate or prevent growth or prevent biofilm formation of microorganisms on the textiles and clothes that are washed or on surfaces inside the washing machine. Examples of biocides and preservatives are BTA (1,2,3- benzotriazole), benzalkonium chlorides, 1,2-benzisothiazolin-3-one (“BIT”), 2-methyl-2H- isothiazol-3-one („MIT“) and 5-chloro-2-methyl-2H-isothiazol-3-one („CIT“), benzoic acid, sorbic acid, iodopropynyl butylcarbamate (“IPBC”), dichlorodimethylhydantoine (“DCDMH”), bromo- chlorodimethylhydantoine (“BCDMH”), and dibromodimethylhydantoine (“DBDMH”).
Preferably, the preservative or biocide is selected from the group consisting of 2- phenoxyethanol, glutaraldehyde, 2-bromo-2-nitropropane-1,3-diol, formic acid in acid form or as its salt, 4,4’-dichloro 2-hydroxydiphenyl ether, and combinations thereof.
The preservative or biocide is added to the composition in a concentration of 0.0001 to 10% relative to the total weight of the composition.
More preferably, the preservative or biocide is selected from the group consisting of
2.2-dibromo-2-cyanoacetamide (DBNPA, CAS No. 10222-01-2); 2,2'-dithiobis[N-methylbenzamide] (DTBMA, CAS No. 2527-58-4); 2-bromo-2-(bromomethyl)pentanedinitrile (DBDCB, CAS No. 35691-65-7); 2-butyl-benzo[d]isothiazol-3-one (BBIT, CAS No. 4299-07-4);
2-methyl-2H-isothiazol-3-one (MIT, CAS No 2682-20-4);
2-octyl-2H-isothiazol-3-one (OIT, CAS No. 26530-20-1);
5-Chloro-2-methyl-2H-isothiazol-3-one (CIT, CMIT, CAS No. 26172-55-4);
Mixture of 5-chloro-2-methyl-2H- isothiazol-3-one (CMIT, EINECS 247-500-7) and 2-methyl-2H- isothiazol-3-one (MIT, EINECS 220-239-6) (Mixture of CMIT/MIT, CAS No. 55965-84-9);
1.2-benzisothiazol-3(2H)-one (BIT, CAS No. 2634-33-5);
Benzyl Alcohol (CAS No. 100-51-6);
Biphenyl-2-ol (CAS No. 90-43-7);
Biphenyl -2-ol, and its salts, o-phenylphenol, MEA-o-phenylphenate, potassium phenylphenate, sodium phenylphenate;
Sodium 2-biphenylate (CAS No. 132-27-4);
Didecyldimethylammonium chloride (DDAC, CAS No. 68424-95-3 and CAS No. 7173-51-5); Dodecylguanidine monohydrochloride (CAS No 13590-97-1); Ethanol (CAS. No 64-17-5); n-propanol (1 -propanol, CAS No. 71-23-8)
Hexa-2,4-dienoic acid (Sorbic acid, CAS No. 110-44-1) and its salts, e.g. calcium sorbate, sodi um sorbate
Potassium (E,E)-hexa-2,4-dienoate (Potassium Sorbate, CAS No. 24634-61-5);
Hydrogen peroxide (CAS No. 7722-84-1);
Lactic acid and its salts;
L-(+)-lactic acid (CAS No. 79-33-4);
2-methyl-1,2-benzothiazol-3(2H)-one (MBIT, CAS No. 2527-66-4); N-(3-aminopropyl)-N-dodecylpropane-1, 3-diamine (Diamine, CAS No. 2372-82-9);
Peracetic acid (CAS No. 79-21-0); polyhexamethylene biguanide hydrochloride (PHMB, CAS No 1802181-67-4), polyhexameth- ylene biguanide hydrochloride (PHMB, CAS No. 27083-27-8), e.g. poly(iminoimidocarbonyl)iminohexamethylene hydrochloride, poly(iminocarbonimidoyliminocarbonimidoylimino -1,6-hexanediyl), polyaminopropyl biguanide; Pyridine-2-thiol 1-oxide, sodium salt (Sodium pyrithione, CAS No. 3811-73-2);
Pyrithione zinc (Zinc pyrithione, CAS No. 13463-41-7);
Salts of benzoic acid e.g. ammonium benzoate, calcium benzoate, magnesium benzoate, MEA- benzoate, potassium benzoate;
Benzoic acid and its sodium salt (CAS No 65-85-0, CAS No. 532-32-1);
Salicylic acid and its salts, e.g. calcium salicylate, magnesium salicylate, MEA salicylate, sodi um salicylate, potassium salicylate, TEA salicylate;
3,3' -Dibromo-4,4'-hexamethylenedioxydibenzamidine and its salts (including isethionate), e.g. dibromohexamidine isethionate (CAS No. 93856-83-8);
Undec -10-enoic acid and its salts, e.g. undecylenic acid, potassium undecylenic acid, sodium undecylenic acid, calcium undecylenic acid, MEA-undecylenic acid, TEA-undecylenic acid;
1 -(4-Chlorophenyl)-3-(3,4-dichlorophenyl)urea, e.g. triclocarban (CAS No 101-20-2); Chloroxylenol (CAS Nos 88-04-0, 1321-23-9);
N,N' -bis(4-chlorophenyl)-3,12-diimino-2,4,11,13-tetraazatetradecanediamidine and its diglu conate, diacetate and dihydrochloride, e.g. chlorohexidine, chlorhexidine digluconate, chloro- hexidine diacetate, chlorhexidine dihydrochloride (CAS Nos 55-56-1, 56-95-1, 18472-51-0, 3697-42-5);
Benzenemethanaminium, N,N -dimethyl-N-[2-[2-[4-(1, 1,3,3, - tetramethylbutyl)phenoxy]ethoxy]ethyl]-, chloride, synonym: benzethonium chloride CAS No 121-54-0); Benzalkonium chloride, bromide and saccharinate, e.g. benzalkonium chloride, benzalkonium bromide, benzalkonium saccharinate (CAS Nos 8001-54-5, 63449-41-2, 91080-29-4, 68989-01- 5, 68424-85-1 , 68391-01-5, 61789-71-7, 85409-22-9);
Methanol, (phenyl methoxy), synonym: benzylhemiformal (CAS No 14548-60-8);
3 -lodo-2-propynylbutylcarbamate (IPBC, CAS No 55406-53-6)
2,4-dichlorobenzyl alcohol (CAS-No. 1777-82-8, further names: dichlorobenzyl alcohol, 2,4- dichloro-benzenemethanol, (2,4-dichloro-phenyl)-methanol, DCBA, Protectol® DA);
1-propanol (CAS-No. 71-23-8, further names: n-propanol, propan-1-ol, n-propyl alcohol, Protec tol® NP S);
5-bromo-5-nitro-1,3-dioxane (CAS-No. 30007-47-7, further names: 5-bromo-5-nitro-m-dioxane, Bronidox ®);
2-bromo-2-nitropropane-1,3-diol (CAS-No. 52-51-7, further names: 2-bromo-2-nitro-1,3- propanediol, Bronopol®, Protectol® BN, Myacide AS);
Glutaraldehyde (CAS-No. 111-30-8, further names: 1-5-pentandial, pentane-1, 5-dial, glutaral, glutardialdehyde, Protectol® GA, Protectol® GA 50, Myacide® GA);
2,4,4'-trichloro-2'-hydroxydiphenyl ether (CAS No. 3380-34-5, further names: triclosan, Irgasan® DP 300, Irgacare® MP, TCS);
4,4’-dichloro 2-hydroxydi phenyl ether (CAS-No. 3380-30-1), further names: 5-chloro-2-(4- chlorophenoxy) phenol, Diclosan, DCPP, which is commercially available as a solution of 30 wt% of 4,4’-dichloro 2-hydroxydiphenyl ether in 1 ,2 propyleneglycol under the trade name Tino- san® HP 100 (BASF);
2-Phenoxyethanol (CAS-no. 122-99-6, further names: Phenoxyethanol, Methylphenylglycol, Phenoxetol, ethylene glycol phenyl ether, Ethylene glycol monophenyl ether, Protectol® PE); Phenoxypropanol (CAS-No. 770-35-4, CAS No 4169-04-4, propylene glycol phenyl ether, phe- noxyisopropanol 1-phenoxy-2-propanol, 2-phenoxy-1 -propanol);
Glucoprotamine (CAS-No. 164907-72-6, chemical description: reaction product of glutamic acid and alkylpropylenediamine, further names: Glucoprotamine 50);
Cyclohexyl hydroxyl diazenium-1 -oxide, potassium salt (CAS No. 66603-10-9, further names: N- cyclohexyl-diazenium dioxide, Potassium HDO, Xyligene, Protectol® KD);
Formic acid (CAS-No. 64-18-6, further names: methanoic acid, Protectol® FM, Protectol® FM 75, Protectol® FM 85, Protectol® FM 99, Lutensol® FM) and its salts, e.g. sodium formiate (CAS No 141-53-7); and performic acid and its salts.
Preferably, the composition comprises 2-phenoxyethanol in a concentration of 0.01% to 5%, more preferably 0.1% to 2%, and/or bronopol in a concentration of 5ppm to 5000ppm, more preferably 20ppm to lOOOppm, and/or glutaraldehyde in a concentration of 2ppm to 5000ppm, more preferably 10ppm to 2000ppm, and/or formic acid (as an acid or its salt) in a concentration of 0.01% to 3%, more preferably 0.05% to 0.5%, and/or 4,4’-dichloro 2-hydroxydiphenyl ether in a concentration of 0.001% to 1%, more preferably 0.002% to 0.6% (in all cases relative to the total weight of the composition). Preferably, the composition comprises 2-phenoxyethanol in a concentration from 0.01% to 5%, preferably 0.1% to 2%, and/or 4,4’-dichloro 2- hydroxydiphenylether in a concentration from 0.001 to 3%, preferably 0.002 to 1%, more prefer ably 0.01 to 0.6%, each by weight of the composition:
In a preferred embodiment, the composition is an aqueous composition comprising 2- phenoxyethanol, bronopol, glutaraldehyde and/or formic acid (as an acid or its salt), especially in the amount indicated above.
The invention thus further pertains to a method of preserving an aqueous composition accord ing to the invention against microbial contamination or growth, which method comprises addition of an preservative or biocide selected from the group consisting of 2-phenoxyethanol, glutaral dehyde, 2-bromo-2-nitropropane-1,3-diol, and formic acid in acid form or as its salt.
In a further preferred embodiment, the composition contains a surfactant and 4,4’-dichloro 2- hydroxydiphenyl ether, typically formulated as a cleansing product or laundry detergent; the amount of 4,4’-dichloro 2-hydroxydiphenyl ether therein is preferably as noted above, and the amount of surfactant in the cleansing product or laundry detergent is typically from the range 1% to 95%, each relative to the total weight of the composition.
The invention thus further pertains to the use of present composition further comprising a sur factant and 4,4’-dichloro 2-hydroxydiphenyl ether, as a cleansing composition especially for hard surfaces, or as a laundry detergent or as a softener composition, and to a corresponding method of laundering fabric or of cleaning hard surfaces.
Examples of viscosity modifiers are agar-agar, carragene, tragacanth, gum arabic, alginates, pectins, hydroxyethyl cellulose, hydroxypropyl cellulose, starch, gelatin, locust bean gum, cross- linked poly(meth)acrlyates, for example polyacrlyic acid cross-linked with bis-(meth)acrylamide, furthermore silicic acid, clay such as - but not limited to - montmorrilionite, zeolite, dextrin, and casein.
Hydrotropes in the context with the present invention are compounds that facilitate the dissolu tion of compounds that exhibit limited solubility in water. Examples of hydrotropes are organic solvents such as ethanol, isopropanol, ethylene glycol, 1,2-propylene glycol, and further organic solvents that are water-miscible under normal conditions without limitation. Further examples of suitable hydrotropes are the sodium salts of toluene sulfonic acid, of xylene sulfonic acid, and of cumene sulfonic acid. Examples of polymers other than polymer (A) are especially polyacrylic acid and its respective alkali metal salts, especially its sodium salt. A suitable polymer is in particular polyacrylic acid, preferably with an average molecular weight Mw in the range from 2,000 to 40,000 g/mol. pref erably 2,000 to 10,000 g/mol, in particular 3,000 to 8,000 g/mol, each partially or fully neutral ized with alkali, especially with sodium. Suitable as well are copolymeric polycarboxylates, in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid and/or fumaric acid. Polyacrylic acid and its respective alkali metal salts may serve as soil anti-redeposition agents.
Further examples of polymers are polyvinylpyrrolidones (PVP). Polyvinylpyrrolidones may serve as dye transfer inhibitors.
Further examples of polymers are polyethylene terephthalates, polyoxyethylene terephthalates, and polyethylene terephthalates that are end-capped with one or two hydrophilic groups per molecule, hydrophilic groups being selected from CFhCFhCFh-SOsNa, CH2CH(CH2-SC>3Na)2, and CH2CH(CH2S02Na)CH2-S03Na.
Examples of buffers are monoethanolamine and N,N,N-triethanolamine.
Examples of defoamers are silicones.
Inventive compositions are not only good in cleaning soiled laundry and/or hard surfaces, pref erably laundry, with respect to organic fatty soil such as oil. Inventive liquid detergent composi tions are very useful for removing non-bleachable stains such as, but not limited to stains from red wine, tea, coffee, vegetables, and various fruit juices like berry juices from laundry and/or hard surfaces, preferably laundry. They still do not leave residues on the clothes or hard surfac es.
In order to be suitable as liquid laundry or liquid dish washing, preferably laundry, compositions, inventive compositions may be in bulk form or as unit doses, for example in the form of sachets or pouches. Suitable materials for pouches are water-soluble polymers such as polyvinyl alco hol.
In a preferred embodiment of the present invention, inventive compositions are liquid or gel- type.
In one embodiment of the present invention, inventive compositions are liquid or gel-type and have a pH value in the range of from 7 to 9, preferably 7.5 to 8.5. In one embodiment of the present invention, inventive compositions are liquid or gel-type and have a total solids content in the range of from 8 to 80%, preferably 10 to 50%, determined by drying under vacuum at 80°C.
In one aspect, the invention is directed to a method of improving the cleaning performance of a detergent composition, preferably a liquid detergent composition, by adding a polymer (A) ac cording to the invention to a detergent composition preferably comprising at least one lipase and/or at least one protease.
The term "improved cleaning performance" herein may indicate that the polymer (A) provides better, i.e. improved, properties in stain removal under relevant cleaning conditions, when com pared to the cleaning performance of a detergent composition lacking polymer (A). In one em bodiment, “improved cleaning performance” means that the cleaning performance of a deter gent comprising polymer (A) and at least one enzyme (B), preferably at least one lipase and/or at least one protease and/or a mannanase, is improved when compared to the cleaning perfor mance of a detergent comprising polymer (A) and no enzyme (B). In one embodiment, “im proved cleaning performance” means that the cleaning performance of a detergent comprising polymer (A) and an enzyme (B), preferably lipase and/or protease and/or mannanase, is im proved when compared to the cleaning performance of a detergent comprising at least one en zyme (B), preferably at least one lipase and/or at least one protease and/or mannanase, and no polymer (A).
The term "relevant cleaning conditions" herein refers to the conditions, particularly cleaning temperature, time, cleaning mechanics, suds concentration, type of detergent and water hard ness, actually used in laundry machines, automatic dish washers or in manual cleaning pro cesses. Thus, the present invention is also directed to the use of a composition as described herein for laundry or hard surface care. Moreover, the present invention is also directed to the use of a composition as described herein for improved cleaning performance, in particular in laundry or hard surface care.
Moreover, the present invention is also directed to the use of a composition described herein for biofilm and/or sebum stain removal and/or for malodour reduction on a textile or hard surface, with hard surface cleaning preferably being dish washing (manual (hand) dish washing or auto mated dish washing) or cleaning of hard surfaces inside a washing machine, but in this embod iment preferably being cleaning of hard surfaces inside a washing machine (dishwashing or laundry washing machine, preferably laundry washing machine). Hence, the present invention is also directed to a method of biofilm removal and/or biofilm pre vention and/or sebum stain removal and/or for malodour reduction on a textile or hard surface comprising the steps of
(i) providing a liquid composition, preferably a detergent composition, preferably comprising a surfactant as described herein, comprising (A) at least one polymer comprising
(a) a core that bears one to 3 moieties of the general formula (I)
Figure imgf000037_0001
wherein Z are different or the same and selected from C2-Ci2-alkylene and C3-C12- cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non- substituted or substituted with one or more 0-CrC4-alkyl groups and wherein C3- Ci2-cycloalkylene may bear one to three methyl groups,
X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, n is in the range of from 1 to 4,
(b) polyalkylene oxide chains; and (B) at least one enzyme;
(ii) contacting a textile or a hard surface with the liquid composition of step (i) for a time and under conditions suitable to allow biofilm removal and/or biofilm prevention and/or sebum stain removal and/or malodour reduction.
Preferably, the enzyme used in the method of biofilm removal and/or biofilm prevention and/or sebum stain removal and/or for malodour reduction on a textile or hard surface described above is selected from the group consisting of amylase, protease, lipase, mannanase, xylanase, nu clease, cellulase, and combinations thereof, preferably selected from the group consisting of protease, lipase, mannanase, and combinations thereof. Most preferably, the enzyme is a pro tease, preferably a subtilisin protease. In another preferred embodiment, the method biofilm and/or sebum stain removal and/or for malodour reduction on a textile or hard surface described herein comprises the use of several enzymes. Preferably the combination of enzymes is prote ase and/or lipase and/or mannanse, preferably protease and lipase, further preferred protease, lipase and mannanase. Preferably, the enzyme used in the method of biofilm removal described herein is a protease, preferably a subtilisin.
Preferably, the enzyme used in the method of sebum stain removal described herein is selected from the group consisting of protease, lipase, mannanase, and combinations thereof, preferably a protease; more preferably, the at least one enzyme is a combination of enzymes selected from the group consisting of a protease and a lipase; and a protease, a lipase, and a man nanase, preferably the combination of enzymes in the method of sebum stain removal de scribed herein is a protease, a lipase, and a mannanase.
A further aspect of the present invention relates to a process for making inventive polymers (A), hereinafter also referred to as inventive process. The inventive process comprises steps (a), (b) and (y):
(a) reacting a diamine according to general formula H2-N-Z-NH2 with alkylene oxide in a mo lar ratio alkylene oxide : diamine of from 4:1 to 1:1, preferably 2.5:1 to 1:0.7 with alkylene oxide being selected from ethylene oxide and propylene oxide, thereby forming an inter mediate,
(b) subjecting the intermediate from step (a) to polycondensation under catalysis of at least one acidic catalyst, thereby obtaining a polycondensate,
(g) reacting the polycondensate from step (b) with at least one C2-C4-alkylene oxide in one or more steps.
Steps (a), (b) and (g) are described in more detail below.
In step (a), a diamine according to general formula H2-N-Z-NH2 is reacted with an alkylene ox ide. The variable Z has been defined above. For the purpose of the present invention, mixtures of isomeric diamines are considered “a diamine”. For example, diamino-methylcyclohexane is usually generated as a mixture of various isomers
Figure imgf000038_0001
Alkylene oxides reacted in step (a) are selected from ethylene oxide („EO“), propylene oxide (“PO”), and mixtures of the foregoing. Preferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.
In step (a), the molar ratio alkylene oxide: diamine is in the range of from 4:1 to 1:1, preferably 2.5:1 to 1 :0.7.
Figure imgf000039_0001
Step (a) may be performed with or without a solvent. In embodiments wherein diamine accord ing to general formula H2-N-Z-NH2 is liquid at reaction temperature it is preferred to use said diamine in bulk. In embodiments wherein diamine according to general formula H2-N-Z-NH2 is solid at reaction temperature it is preferred to use a solvent. Suitable solvents are aprotic sol vents, for example hydrocarbons such as toluene and ethers, e.g. di-n-butyl ether.
In one embodiment of the present invention, step (a) may include dilution of diamine according to general formula H2-N-Z-NH2 with water before alkoxylation, for example in a ratio diamine : water of 100 : 1 to 1 :1 , especially from 20 : 1 to 5 :1 by weight.
Preferably, step (a) is carried out in the absence of a catalyst.
In one embodiment of the present invention, step (a) is performed at a reaction temperature from 90 to 150°C, preferably from 100 to 135°C.
In one embodiment of the present invention, step (a) may be carried out at a pressure of up to 15 bar, preferably up to 10 bar, for example 1 to 8 bar. Preferred vessels for carrying out step (a) are autoclaves and tubular reactors. In one embodiment of the present invention, step (a) has a duration in the range of from 30 minutes to 10 hours, preferably 1 hour to 7 hours.
Step (a) may be carried out under an inert gas atmosphere, for example nitrogen or a noble gas. In another embodiment, step (a) is carried out under an atmosphere of alkylene oxide. Inert gas atmosphere is preferred. From step (a), an intermediate is formed. It is possible to work up the intermediate, for example by removal of unreacted alkylene oxide and of water, if present, or to use the intermediate from step (a) without further work-up. Said removal of unreacted al kylene oxide and of water, if present, may be performed by evaporation at a pressure in the range of from 500 mbar to 0 mbar, preferred: 100 mbar to 20 mbar and at a temperature in the range of from 20 to 120 °C, preferred are 60 to 100 °C. The intermediate from step (a) is usually a mixture of compounds, a main component being H-AO-NH-Z-NH-AO-H, with AO being CH2CH2-O or CH2CH(CH3)-0, and the degree of alkoxylation is usually an average number.
In step (b), the intermediate from step (a) is subjected to polycondensation under catalysis of at least one acidic catalyst.
Suitable acidic catalysts for step (b) are selected from organic sulfonic acids such as para- toluene sulfonic acid, sulfuric acid and phosphorus-bearing acids, preferred are H3PO3, H3PO4, and phosphinic acid (H3PO2), even more preferred are H3PO4 and H3PO2. Lewis acids such as, but not limited to AICI3, FeC , diethyl tin dilaurate, and Ti(0-te/tbutyl)4 may serve as catalyst as well.
The acidic catalyst can be applied in bulk or as aqueous solution.
In one embodiment of the present invention, the catalyst is added generally in an amount of 0.001 to 10 mole-%, preferably of 0.005 to 7, more preferably 0.01 to 5 mol-%, based on the amount of intermediate from step (a).
Step (b) may be carried out by using a solvent. Examples of solvents that can be used to per form the inventive process are aromatic and/or (cyclo)aliphatic hydrocarbons and their mixtures, and halogenated hydrocarbons. Preference is given monoalkylated or polyalkylated benzenes and naphthalenes and mixtures thereof.
Preferred aromatic hydrocarbon mixtures are those predominantly comprising aromatic C7 to CM hydrocarbons and possibly encompassing a boiling range from 110 to 300 °C, particular preference being given to toluene, 0-, m- or p-xylene, trimethylbenzene isomers, tetra- methylbenzene isomers, ethylbenzene, cumene, tetrahydronaphthalene, and mixtures compris ing them. Examples thereof are the Solvesso® grades from ExxonMobil Chemical, especially Solvesso® 100 (CAS No. 64742-95-6, predominantly Cg and Cio aromatics, boiling range about 154 to 178 °C), 150 (boiling range about 182 - 207°C), and 200 (CAS No. 64742-94-5), and also the Shellsol® grades from Shell. Hydrocarbon mixtures comprising paraffins, cycloparaf fins, and aromatics are also available commercially under the names Kristalloel (e.g., Kristalloel 30, boiling range about 158 to 198°C or Kristalloel 60: CAS No. 64742-82-1), white spirit (like wise, for example, CAS No. 64742-82-1) or solvent naphtha (light: boiling range about 155 to 180 °C, heavy: boiling range about 225 to 300 °C).
Halogenated hydrocarbons are, for example, chlorobenzene and dichlorobenzene or its isomer mixtures. Examples of esters are n-butyl acetate, ethyl acetate, 1-methoxyprop-2-yl acetate, and 2-methoxyethyl acetate. Examples of ethers are THF, dioxane, and the dimethyl, diethyl or di-n-butyl ethers of ethylene glycol.
Examples of (cyclo)aliphatic hydrocarbons are decalin, alkylated decalin, and isomer mixtures of linear or branched alkanes and/or cycloalkanes.
Preferred solvents are those that form low-boiling azeotropic mixtures with water and thus facili tate removal of water.
Preference is given, though, to not using a solvent for carrying out step (b).
In a preferred embodiment, step (b) is carried out in a way that the temperature during polycon densation does not exceed 240 °C. For example, the polycondensation is carried out at temper atures in the range of from 100 to 230 °C, preferably 150 to 210 °C. Even more preferably, the temperature during polycondensation does not exceed 210 °C.
In one embodiment of the present invention, step (b) is carried out in a way that the duration of the polycondensation is one to 25 hours, preferably 1 to 15 hours, more preferably 2 to 10 hours.
In one embodiment of the present invention, step (b) can be carried out at a pressure in the range of from 0.5 bar to 20 bar, while normal pressure being preferred. In a preferred embodi ment, the inventive process is being performed at normal pressure. In an alternative embodi ment, step (b) is carried out in vacuo or at a pressure in the range of from 1 mbar to 0.5 bar. Step (b) is preferably followed by removal or blow-off of residual monomers, for example, by distilling them off at normal pressure or at reduced pressure, e. g., in the range of from 0.1 to 0.75 bar. In one embodiment of step (b), water or other volatile products released during the polyconden sation can be removed from the reaction mixture in order to accelerate the reaction, such re moval being accomplished by distillation, for example, and optionally under reduced pressure. The removal of water or of other low molecular mass reaction by-products can also be assisted by passing through the reaction mixture a stream of gas which is substantially inert under the reaction conditions (stripping), such as nitrogen, for example, or a noble gas such as helium, neon or argon, for example.
In one embodiment of the present invention, 0.4 to 1.0 and preferably 0.4 to 0.7 mol H2O moles of water per mole of intermediate from step (a) are removed in step (b).
By performing step (b), a polycondensate is obtained. Said polycondensate is usually a mixture of compounds, e.g., with a different value of the variable n, or with branching or cross-linking.
For example, in embodiments wherein H2N-Z-NH2 is selected from 2,4-diamino- methylcyclohexane and alkylene oxide is ethylene oxide and 0.5 mole of water are removed from the intermediate, a mixture containing the below compounds is made.
Figure imgf000042_0001
An - optional - step of work-up may include the deactivation of catalyst used in step (b).
In step (y), polycondensate from step (b) is reacted with at least one C2-C4-alkylene oxide. Ex amples of C2-C4-alkylene oxides are ethylene oxide („EO“), propylene oxide (“PO”), butylene oxide (“BuO”), and mixtures of at least two of the foregoing. Preferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.
Step (g) is preferably carried out in the presence of a catalyst, for example a base or a double metal cyanide. In one embodiment of the present invention, step (g) is carried out in the presence of a base. Suitable bases such as potassium hydroxide, sodium hydroxide, sodium or potassium alkoxides such as potassium methylate (KOCH3), potassium tert-butoxide, sodium ethoxide and sodium methylate (NaOCHs), preferably from potassium hydroxide and sodium hydroxide. Further ex amples of catalysts are alkali metal hydrides and alkaline earth metal hydrides such as sodium hydride and calcium hydride, and alkali metal carbonates such as sodium carbonate and potas sium carbonate. Preference is given to the alkali metal hydroxides, preference being given to potassium hydroxide and sodium hydroxide, and to alkali metal alkoxides, particular preference being given to potassium t-butoxide in t-butanol, sodium n-hexanolate in n-hexanol, and to so dium methanolate in n-nonanol. Typical use amounts for the base are from 0.05 to 10% by weight, in particular from 0.5 to 2% by weight, based on the total amount of polycondensate from step (b) and C2-C4-alkylene oxide.
In one embodiment of the present invention, step (g) is carried out in the presence of a double metal cyanide. Double-metal cyanides, hereinafter also referred to as double metal cyanide compounds or DMC compounds, usually comprise at least two different metals, at least one of them being selected from transition metals and the other one being selected from transition metals and alkali earth metals, and furthermore cyanide counterions. Particularly suitable cata lysts for the alkoxylation are double-metal cyanide compounds which contain zinc, cobalt or iron or two thereof. Berlin blue, for example, is particularly suitable.
Preference is given to using crystalline DMC compounds. In a preferred embodiment, a crystal line DMC compound of the Zn-Co type which comprises zinc acetate as further metal salt com ponent is used as catalyst. Such compounds crystallize in monoclinic structure and have a platelet-like habit.
In one embodiment of the present invention, the inventive synthesis is carried out in the pres ence of at least one double-metal cyanide selected from hexacyano cobaltates.
In one embodiment of the present invention, the inventive synthesis is carried out in the pres ence of at least one double-metal cyanide selected from compounds according to general for mula (VIII)
M1 r1[M2(CN)r2(A)r3]r4 6 M1 r7X2 mr r8(H20) i^L· kP (VIII), wherein M1 is at least one metal ion chosen from the group consisting of Zn2+, Fe2+, Fe3+, Co3+, Ni2+,
Figure imgf000045_0001
M2 is at least one metal ion chosen from the group consisting of Fe2+, Fe3+, Co2+, Co3+, Mn2+, Mn3+, V4+, V5+, Cr2+, Cr3*, Rh3+, Ru2+, Ir3*, and in a way that M1 and M2 are not identical,
A and X2, independently of one another, are anions selected from the group consisting of halide, hydroxide, sulfate, carbonate, cyanide, thiocyanate, isocyanate, cyanate, carboxylate, oxalate, nitrate, nitrosyl, hydrogensulfate, phosphate, dihydrogenphosphate, hydrogenphosphate or hy- drogencarbonate,
L is a ligand chosen from the group consisting of alcohols, aldehydes, ketones, ethers, polyeth ers, esters, polyesters, polycarbonate, ureas, amides, primary, secondary and tertiary amines, ligands with pyridine nitrogen, nitriles, sulfides, phosphides, phosphites, phosphanes, phospho- nates and phosphates, k is greater than or equal to zero, and up to 6. The variable k can be a whole number or a frac tion.
P is an organic additive, selected for example from polyethers, polyesters, polycarbonates, poly- alkylene glycol sorbitan esters, polyalkylene glycol glycidyl ethers, polyacrylamides, poly(acrylamide-co-acrylic acid), polyacrylic acids, poly(acrylamide-co-maleic acid), polyacrylo nitriles, polyalkyl acrylates, polyalkyl methacrylates, polyvinyl methyl ethers, polyvinyl ethyl ethers, polyvinyl acetates, polyvinyl alcohol, poly-N-vinylpyrrolidone, poly(N-vinylpyrrolidone-co- acrylic acid), polyvinyl methyl ketone, poly(4-vinylphenol), poly(acrylic acid-co-styrene), oxazo- line polymer, maleic acid and maleic anhydride copolymers, hydroxyethylcellulose, polyace tates, ionic surface-active and interface-active compounds, bile acid or salts thereof, esters or amides, carboxylic esters of polyhydric alcohols and glycosides. r1 , r2, r3, r4, r7 and ml are chosen such that the electroneutrality of the compound (I) is en sured, where each f and r3 may be 0, r5 is the number of ligand molecules, for example a fraction or an integer greater than zero, or zero, r6 and r6, independently of one another, are fractions or integers greater than zero, or zero.
In one embodiment, the upper limits of r5, r6, and r8 are each 6.
Double-metal cyanide compounds can be used as powder, paste or suspension or be moulded to give a moulding, be introduced into mouldings, foams or the like or be applied to mouldings, foams or the like.
Preferably, the DMC catalyst used for step (y), based on polycondensate obtained in step (b), is from 5 to 2000 ppm (i.e. mg of catalyst per kg of product), preferably less than 1000 ppm, in particular less than 500 ppm, particularly preferably less than 100 ppm, for example less than 50 ppm or 35 ppm, particularly preferably less than 25 ppm; ppm referring to mass-ppm (parts per million) of polycondensate obtained in step (b).
Step (g) may be carried out in bulk, embodiment (i), or in an organic solvent, embodiment (ii). In embodiment (i), water can be removed from the polycondensate obtained in step (b). Such wa ter removal can be done by heating to a temperature in the range of from 80 to 150°C under a reduced pressure in the range of from 0.01 to 0.5 bar and distilling off the water.
In one embodiment of the present invention, step (g) is carried out at a reaction temperature in the range of from 70 to 200°C and preferably from 100 to 180°C.
In one embodiment of the present invention, step (g) is carried out once per synthesis of in ventive polymer (A). In an alternative embodiment, step (g) is carried out several time, for ex ample up to four times per synthesis of an inventive polymer (A), for example with the same or preferably with different C2-C4-alkylene oxides. It is, for example, possible to subject a polycon densate obtained in step (b) to a first alkoxylation (g1) with ethylene oxide and to subject the product from step (g1) to a second alkoxylation (g2), for example with propylene oxide.
In one embodiment of the present invention, step (g) is carried out at a pressure of up to 10 bar and in particular up to 8 bar, for example 1 to 8 bar.
In one embodiment of the present invention, the reaction time of step (g) is generally in the range of from 0.5 to 12 hours.
Examples of suitable organic solvents for embodiment (ii) of step (g) are nonpolar and polar aprotic organic solvents. Examples of particularly suitable nonpolar aprotic solvents include ali- phatic and aromatic hydrocarbons such as hexane, cyclohexane, toluene and xylene. Examples of particularly suitable polar aprotic solvents are ethers, in particular cyclic ethers such as tetra- hydrofuran and 1 ,4-dioxane, furthermore N,N-dialkylamides such as dimethylformamide and dimethylacetamide, and N-alkyllactams such as N-methylpyrrolidone. It is as well possible to use mixtures of at least two of the above organic solvents. Preferred organic solvents are xy lene and toluene.
In embodiment (ii), the solution obtained in the first step, before or after addition of catalyst and solvent, is dewatered before being subjected to alkylene oxide, said water removal advanta geously being done by removing the water at a temperature in the range of from 120 to 180°C, preferably supported by a stream of nitrogen. The subsequent reaction with the alkylene oxide may be effected as in embodiment (i). In embodiment (i), alkoxylated polyalkylenimines accord ing to the invention is obtained directly in bulk and may be dissolved in water, if desired. In em bodiment (ii), for work-up organic solvent is typically replaced by water. Alkoxylated polyalkylen imines according to the invention may alternatively be isolated in bulk.
An - optional - step of work-up may include the deactivation of catalyst used in step (y), in the case of basic catalysts by neutralization.
The inventive process does not require bleaching steps or reductive removal of impurities.
The invention is also directed to a method of making a composition comprising a polymer (A) and at least one enzyme (B) and optionally one surfactant (C) comprising the steps of
(i) making the polymer (A) described herein in a process comprising the steps of
(a) reacting a diamine according to general formula H2-N-Z-NH2 with alkylene oxide in a molar ratio alkylene oxide: diamine of from 4:1 to 1:1 with alkylene oxide being se lected from ethylene oxide and propylene oxide, thereby forming an intermediate,
(b) subjecting the intermediate from step (a) to polycondensation under catalysis of at least one acidic catalyst, thereby obtaining a polycondensate,
(g) reacting the polycondensate from step (b) with at least one C2-C4-alkylene oxide in one or more steps,
(ii) obtaining a composition comprising the polymer obtained in step (i), and
(iii) adding at least one enzyme (B) to the composition obtained in step (ii); and optionally
(iv) adding at least one surfactant (C) to the composition obtained in step (iii).
It is apparent for the person skilled in the art that the composition can also obtained in a differ ent order, e.g., step (iii) prior step (ii) and step (iv) prior step (iii) or (ii), etc.. The present invention is further illustrated by working examples.
General remarks: percentages refer to % by weight unless expressly stated otherwise. GPC was carried out with THF as mobile phase, with linear PMMA as internal standard Hydroxyl values (OH values) were determined according to 53240 (2013).
Amine values were determined according to ASTM D2074-07.
The Hazen colour number was determined according to DIN ISO 6271, ASTM D 1209, with spectrophotometric detection. (2° norm observer, normal light, layer thickness 11 mm, against distilled water).
I. Synthesis of inventive polymers 1.1 Synthesis of inventive polymer (A.1 )
Step (a.1)
A 2-L steel autoclave was charged with 256 g methylcyclohexyldiamine (MCDA) as 4:1 mixture of 2,4-diamines and 2,6-diamines:
Figure imgf000048_0001
and 43 g water and then heated to 100 °C. Then, 30 g of ethylene oxide were dosed into the autoclave. The start of an exothermic reaction was observed. Subsequently, 146 g of ethylene oxide were dosed into the autoclave within 4 hours. The system was kept at 100 °C for further 6 hours. After hat, the mixture is removed from the autoclave and residual EO and water were stripped under reduced pressure (20 mbar) at 80 °C for two hours. 430 g of intermediate were obtained as a yellow viscous liquid.
Analytics:
OH value: 939 mg KOH/g
Amine value: total amines: 469 mg KOH/g, primary amines: 61 mg KOH /g, secondary amines: 259 mg KOH/g, tertiary amines: 149 mg KOH/g Step (b.1): polycondensation:
A 500 ml_ four-neck flask equipped with stirrer, distillation bridge, N2 inlet, and internal ther mometer was charged with 315 g of the intermediate from step (a.1) and 1.6 g of a 50% aque ous solution of phosphinic acid (H3PO2). The resulting reaction mixture was heated to 200 °C and then stirred at 200 °C under nitrogen for 2 hours while the distillate was collected. Then the temperature was reduced to 80 °C and the resulting polycondensate was collected as a viscous liquid.
OH value: 609 mg KOH/g
GPC: Mn: 960 g/mol, Mw: 2160 (g/mol)
Step (Y 1.1 ) : ethoxylation
A 2-liter steel autoclave was charged with 92 g of polycondensate from step (b.1) and 3.9 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under re duced pressure. Then the residue was heated to 120 °C and 30 g of ethylene oxide were added within 10 minutes. After start of the exothermic reaction, 851 g of ethylene oxide were added within 12 hours. The resultant reaction mixture was maintained at 120 °C for 6 hours and then cooled to 80 °C. The autoclave was vented and discharged. Residual EO was stripped from the residue under reduced pressure at 80 °C. An amount of 987 g of inventive polymer (A.1) was obtained.
Analytics:
OH value: 76 mg KOH/g Amine value: 44 mg KOH/g
1.2 Synthesis of inventive polymer (A.2)
Step (y2.2): propoxylation
A 2-liter steel autoclave was charged with 292 g of inventive polymer (A.1) and 2.3 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under reduced pres sure. Then the residue was heated to 130 °C and 50 g of propylene oxide were added within 10 minutes. After start of the exothermic reaction, 229 g of propylene oxide were added within 6 hours. The resultant reaction mixture was maintained at 130 °C for 6 hours and then cooled to 100 °C. The autoclave was vented and discharged. Residual PO was stripped under reduced pressure at 80 °C. An amount of 575 g of inventive polymer (A.2) as a brown solid material were obtained. Analytics:
OH value: 47 mg KOH/g Amine value: 24 mg KOH/g
1.3 Synthesis of inventive polymer (A.3)
Step (a.3)
A 2-liter steel autoclave was charged with 641 g methylcyclohexyldiamine (MCDA) as 4:1 mix ture of 2,4-diamines and 2,6-diamines and 64 g water and then heated to 100 °C. Then, 30 g of ethylene oxide were dosed into the autoclave. The start of an exothermic reaction was ob served. Subsequently, 322 g of ethylene oxide were dosed into the autoclave within 6 hours. The system was kept at 100 °C for further 6 hours. After hat, the mixture is removed from the autoclave and residual EO and water were stripped under reduced pressure (20 mbar) at 80 °C for two hours 991 g of intermediate of stepl were obtained as a yellow viscous liquid.
Analytics:
OH value: 917 mg KOH/g
Amine value: total amines: 553 mg KOH/g
Step (b.3): polycondensation
A 500 ml_ four-neck flask equipped with stirrer, distillation bridge, N2 inlet, and internal ther mometer was charged with 180.5 g of the intermediate from step a.3 and 0.94 g of a 50% aqueous solution of phosphinic acid (H3PO2). The reaction mixture was stirred under nitrogen and heated up to 200 °C under stirring. The reaction was kept at 200 °C under nitrogen and stirring for 14 hours while the distillate was collected. Then the temperature was reduced to 130 °C and the product was collected as a viscous liquid.
The resulting product was characterized via gel permeation chromatography (GPC) in HFIP and OH value.
Analytics:
OH value: 544 mg KOH/g
GPC (HFIP): Mn: 5364 g/mol, Mw: 51695 g/mol
Step (y3.3): ethoxylation
A 2-liter steel autoclave was charged with 70 g of polycondensate from step (b.3) and 2.8 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under re duced pressure. The resulting residue was then heated to 120 °C and 30 g of ethylene oxide were added within 10 minutes. After start of the exothermic reaction, 587 g of ethylene oxide were added within 12 hours. The resultant reaction mixture was maintained at 120 °C for 6 hours and then cooled to 100 °C. The autoclave was vented and discharged. Residual EO was stripped from the residue under reduced pressure at 80 °C. An amount of 689 g of inventive polymer (of step3) was obtained.
Analytics:
OH value: 65 mg KOH/g Amine value: 58 mg KOH/g
I.4 Synthesis of inventive polymer (A.4)
Step (y4.4): propoxylation
A 2-liter steel autoclave was charged with 197 g of inventive polymer A.3 and 1.5 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under reduced pres sure. The resultant residue was then heated to 130 °C and 30 g of propylene oxide was added within 10 minutes. After start of the exothermic reaction, 156 g of propylene oxide were added within 20 hours. The resultant reaction mixture was maintained at 130 °C for 4 hours and then cooled to 100 °C. The autoclave was vented and discharged. Residual PO was stripped under reduced pressure at 80 °C. An amount of 383 g of inventive polymer (A.4) as a brown solid ma terial were obtained.
Analytics:
OH value: 41 mg KOH/g Amine value: 29 mg KOH/g
II. Washing performance ll.l Washing performance, Experiment 1
All tests in washing performance Experiment 1 were carried out with inventive polymer (A.2). Lipase (B.1): Lipex® 100 L, a lipase commercially available from Novozymes (lipase variant of amino acids 1-269 of SEQ ID NO: 2 of US5869438 with T231R and N233R substitutions) Quantities of the respective enzyme are tel quel.
The primary wash performance of the inventive polymer (A.2) was tested in the washing ma chine preparing wash solutions using water of 14°dH hardness (2.5 mmol/L; Ca:Mg:HCC>34:1 :8) containing 3.0-4.0 g/L of the liquid test detergent L.1, see composition in Table 1, and 0.7-1.0% of inventive polymer (A.2) and/or in combination with 0.1% by weight (B.1) and 0.5% by weight (C.1).
Table 1. L.1 Ingredients of base mixture for a liquid detergent formulation
Figure imgf000052_0001
For the performance test in the washing machine (Miele SOFTTRONIC W 1935 WTL, 30°C, short program, 1200 rpm, 3.5 kg ballast load), four multi-stain monitors (MS1, MS2) were washed together with two SBL-2004 sheets (wfk Testgewebe GmbH, DE; corresponding to 32 grams of ballast soil) as additional soil ballast.
The multi-stain monitors MS1 and MS2 (Table 2) contain respectively 8 and 4, standardized soiled fabrics, of respectively 5.0 x 5.0 cm and 4.5x4.5 cm size, all of them stitched on two sides to a polyester carrier.
Table 2. Multi-stain monitors for the washing machine tests MS1:
CFT C-S-10: butterfat with colorant on cotton CFT C-S-62: lard, colored on cotton CFT C-S-78: soybean oil with pigment on cotton EM PA 112: cocoa on cotton EM PA 141/1: lipstick on cotton
EMPA 125: soiling on cotton fabric, sensitive to surfactants as well as to lipases wfk20D: pigment and sebum-type fat on polyester/cotton mixed fabric CFT C-S-70: chocolate/mousse cream on cotton MS2:
CFT C-S-10: butterfat with colorant on cotton CFT C-S-62: lard, colored on cotton CFT C-S-61: beef fat, colored on cotton CFT PC-S-04: Saturated with colored olive oil on Polyester/Cotton (65/35)
The total level of cleaning was evaluated using color measurements. Reflectance values of the stains on the monitors were measured using a sphere reflectance spectrometer (SF 500 type from Datacolor, USA, wavelength range 360-700 nm, optical geometry d/8°) with a UV cutoff filter at 460 nm. In this case, with the aid of the CIE-Lab color space classification, the bright ness L *, the value a * on the red - green color axis and the b * value on the yellow - blue color axis, were measured before and after washing and averaged for the respective stains of the monitor. The change of the color value (Delta E, DE) value, defined and calculated automatical-
Figure imgf000053_0001
ly by the evaluation color tools on the following formula is a measure of the achieved cleaning effect. All experiments were repeated three times to fur nish an average number.
Higher Delta E values show better cleaning. For each stain, a difference of 1 unit can be detect ed visually by a skilled person. A non-expert can visually detect 2 units easily. The DE values of the formulations for the 8 and 4 stains of correspondingly MS1 and MS2 and for selected single stains are shown in Table 3. In the tests, an additional cleaning performance benefit can be seen with the inventive polymer, also in combination with lipase (B.1).
Table 3. Results of washing machine test fabric monitors
Figure imgf000053_0002
In an additional experiment, the respective formulations were stored for 28 days at each 30 and 37°C, then, the washing experiments were repeated. No significant deterioration of the activities of the respective enzymes was observed.
Lipase activity was determined by employing para-nitrophenol-valerate (2.4 mM pNP-C5 in 100 mM Tris pH 8.0, 0.01% Triton X100) as a substrate. The absorption at 405 nm was measured at 20°C every 30 seconds over 5 minutes. The slope (absorbance increase at 405 nm per minute) of the time dependent absorption-curve is directly proportional to the activity of the lipase.
11.11 Washing performance, Experiment 2
All tests in wash performance Experiment 2 were carried out with inventive compositions com prising polymer (A.4) and comprising one or more of the following enzymes:
Lipase (B.1): Lipex® 100L, a lipase commercially available from Novozymes (amino acids 1-269 of SEQ ID NO: 2 of US5869438 with T231R and N233R substitutions);
Protease (B.2): BLAP protease formulation (formulation comprising 4.6% Bacillus lentus alka line protease (BLAP) with R99E substitution (W09523221));
Mannanase (B.3): Mannaway® 4.0 L, a mannanase commercially available from Novozymes (amino acids of SEQ ID NO: 1 of W02009074685).
Quantities mentioned in this example refer to the enzyme products used as such.
The primary wash performance of the inventive compositions was tested in the washing ma chine (Miele SOFTTRONIC W 1935 WTL, 30°C, short program, 1200 rpm, 3.5 kg ballast load), in which wash solutions using water of 14°dH hardness (2.5 mmol/L; Ca:Mg:HC034:1:8) were prepared. In all cases 45 g of the liquid test detergent L.1 (see composition in Table 1 above) was added. This corresponds to about 3 g/L in the wash liquor.
For the performance test in the washing several stained fabric swatches of ca. 5x5 cm each, usually a certain number attached to a textile carrier, were washed together with two SBL-2004 sheets (wfk Testgewebe GmbH, DE; corresponding to 32 grams of ballast soil) as additional soil ballast. All stained fabric swatches were purchased at CFT B.V., NL. At the website cftbv.nl a more detailed description of the stains is provided. Table 4. stained fabric swatches used.
Figure imgf000055_0001
The total level of cleaning was evaluated using color measurements, using a MACH 5 color measurement instrument, see http://colourconsult.nl/products/mach5-colour-instrument/.
In this case, with the aid of the CIE-Lab color space classification, the brightness L *, the value a * on the red - green color axis and the b * value on the yellow - blue color axis, were meas ured before and after washing and averaged for the respective stains of the monitor. The change of the color value (Delta E, DE), defined and calculated automatically by the evaluation color tools on the formula below, is a measure of the achieved cleaning effect. Some experi ments were repeated 1 time to furnish an average number DE* = L/(D L*2 + Aa*2 + Ab*2).
Higher Delta E values show better cleaning. For each stain, a difference of 1 unit can be detect ed visually by a skilled person. A non-expert can visually detect 2 units easily. The DE values of the detergent formulations corresponding to the indicated multi-stain monitor(s) or individual stains are shown in Table 5a and 5b.
Table 5a. Results of washing machine test fabrics
Figure imgf000056_0001
The wash liquor containing both polymer A.4 and a protease gives overall the best washing per formance.
Table 5b Results of washing machine test fabrics. Numbers are the average over 2 washing experiments per detergent formulation.
Figure imgf000056_0002
Figure imgf000057_0001
*) percentage refers to total weight of detergent formulation L.1
In Table 5b, for the sum of Delta E over all 25 stains, the net benefit of Polymer A.4 over deter gent only is DE=8 (first 2 entries in Table 5b). However, the net benefit of polymer A.4 on top of a detergent containing an enzyme mix is much higher: Delta E = 30 (last 2 entries of the Table 5b). This indicates a synergistic effect of polymer A.4 together with the enzyme mix of protease, lipase and mannanase. A similar effect is shown for a single stain (C-S-62, lard) in the last col umn.
III. Inhibition of biofilm formation
Biofilms were cultivated in a nutrient medium in microtiter plates in the presence of potentially inhibiting additives or mixtures of additives. After culturing, the biofilm was stained with a dye (safranin), the dye was then re-dissolved in a solvent. The absorption of the dye solution at 540 nm is a measure of the amount of biofilm that was grown in the well.
Test organism Pseudomonas aeruginosa DSM 1117 (P. aeruginosa) was cultured on tryptic soy agar at 35°C for 24 h. The first passage was stored at +4°C for 9 days.
The inoculum was prepared by suspending 5 single colonies of the first passage in 200 ml 30% TSB + 2.5g/L glucose in a 200 ml_ shake flask at 35°C, on a shaker with agitation speed of -160 rpm for 24 h. The cell density of this o/n culture was photometrically determined at 595 nm (OD595nm) and adjusted in 60 % TSB + 5 g/L glucose to OD595nm = 0.4.
Solutions of the additives were prepared in twice the final concentrations in the wells in deion ized water, sterile filtered and 75 pi were added to the appropriate wells of a transparent 96 well-microtiter plate. 75 mI_ of the OD595nm = 0.4 cell suspension (inoculum) were transferred to each of the appropriate wells of the microtiter plate. Biofilms were thus cultivated in 30 %
TSB + 2.5 g/L glucose. The plate was incubated in a humid chamber at 33°C and 40 rpm for 24 h.
After incubation the supernatant containing planktonic cells was removed with a pipette, wells were washed 3 x with 195 pL 0.85 % NaCI solution. After removing the NaCI solution, the plate was tapped on a tissue to minimize residual NaCI in wells, empty plate was dried in the laminar flow. Safranin (Gram’s safranin, Sigma-Aldrich) was used for staining the biofilm: 175 mI_ was used per well and left for 30 min at room temperature (RT).
The supernatant was removed with a pipette, wells were washed 4 x with 195 mI_ 0.85% NaCI solution and finally the liquid was removed with a pipette and the plate was tapped on a tissue to minimize residual NaCI in wells. Empty plate was dried in the laminar flow. The wells were filled with 175 mI_ 30 % acetic acid in deionized H2O (dye solvent). Dye was further dissolved by pipetting up and down and liquid was transferred to a fresh microtiter plate.
The absorption of the safranin solutions was determined using a plate reader at 540 nm.
Each composition was tested in parallel in 10 wells. The average over 10 results was taken. From each of these average absorption values a blank background value (average of at least 3 wells with growth medium, but without bacteria) was subtracted. A relative biofilm formation (in %) is calculated relative to the formation in the blank experiment (100% by definition). A biofilm inhibition effect (in %) is calculated by taking 100% - relative biofilm formation (%).
5 systems were tested:
(1) No addition of any anti-biofilm agents to the biofilm growth medium (“blank experiment w/o agent”)
(2) Addition of 0.005% polymer A.2 to the growth medium, where the indication % refers to the weight of A.2 with respect to the weight of liquid in each well of the microtiter plate
(3) Addition of 0.005% protease formulation (formulation comprising 4.6% BLAP protease with R99E substitution) to the growth medium, where the indication % refers to the weight of the protease formulation with respect to the weight of liquid in each well of the microtiter plate
(4) Addition of 0.01% nonionic surfactant Lutensol AO 7 (BASF) to the growth medium, where the indication % refers to the weight of the surfactant product with respect to the weight of liquid in each well of the microtiter plate
(5) Addition of a combination of 3 products, protease, polymer A.2 and surfactant as in the
Results are given in Table 6
Table 6: Biofilm inhibition effect of various additives
Figure imgf000058_0001
Figure imgf000059_0001
Protease only, appears not to inhibit, but slightly promote biofilm growth (negative number). Polymer A.2 shows a significant biofilm inhibition of 36%. Surfactant Lutensol A07 shows a very slight biofilm inhibition of 9%. The combination of all 3 shows a very pronounced biofilm inhibi- tion of 72%.
IV. Exemplified liquid laundry detergent formulations
The following liquid laundry detergent formulations are illustrative examples of typical detergent formulations according to the present invention.
Figure imgf000059_0002
Figure imgf000060_0001
AEO: C12/C14 fatty alcohol (7EO) Lutensol A07 (BASF)
AES: Alcohol Ethoxysulfate: Texapon N 70 (BASF).
LAS: Linear alkylbenzene sulfonate Maranil DBS/LC (BASF) Coco fatty acid: Edenor K12-18 (Emery Oleochemicals)
Tinosan HP 100 is a solution of 30% w/w of 4,4’-dichloro-2-hydroxydiphenylether (CAS: 3380- 30-1) in 1,2-propyleneglycol.
The above formulations were prepared by first preparing a premix, containing surfactants, sol- vents, fatty acid, citric acid and NaOH and water up to 90%. This pre-mix was prepared by add ing all components to the appropriate amount of water and stir at room temperature. Subse quently the pH was set to pH=8.5 using NaOH. Then the final formulations were prepared by stirring at room temperature: 90% of this pre-mix, the appropriate concentrations of Protease (B.2), Polymer (A.2), phenoxyethanol and/or Tinosan HP 100 and water up 100%.
*For the density measurement 1.00 ml of the formulation (taken with a calibrated Eppendorf pipette) was weighed on an analytical balance.

Claims

Patent claims
1. Composition comprising
(A) at least one polymer comprising
(a) a core that bears one to 3 moieties of the general formula (I)
Figure imgf000061_0001
wherein Z are different or the same and selected from C2-Ci2-alkylene and C3-C12- cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non- substituted or substituted with one or more 0-CrC4-alkyl groups and wherein C3- Ci2-cycloalkylene may bear one to three methyl groups,
X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, n is in the range of from 1 to 4,
(b) polyalkylene oxide chains; and
(B) at least one enzyme.
2. Composition according to claim 1 wherein all Z are selected from cyclohexylene and cy- clopentylene, each non-substituted or substituted with one to 2 methyl or methoxy groups.
3. Composition according to claim 1 or 2 wherein said at least one enzyme is selected from the group consisting of amylase, protease, lipase, mannanase, phytase, xylanase, lac tase, phosphatase, glucoamylase, nuclease, cellulase, and combinations thereof, prefera bly selected from lipase, protease, mannanase, and combinations thereof.
4. Composition according to any of the preceding claims wherein said composition is a de tergent composition, preferably a laundry or hard surface cleaning detergent composition.
5. Composition according to any of the preceding claims wherein said composition compris es
(C) at least one surfactant, preferably an anionic surfactant.
6. Composition according to any of the preceding claims wherein such composition is gel- type or liquid at ambient temperature.
7. Composition according to any of the preceding claims wherein said polymer (A) has an average molecular weight Mw in the range of from 1 ,000 to 80,000 g/mol.
8. Composition according to any of the preceding claims wherein Z is selected from combi nations of
Figure imgf000062_0001
9. Composition according to any of the preceding claims further comprising a preservative or biocide, preferably selected from the group consisting of 2-phenoxyethanol, glutaralde- hyde, 2-bromo-2-nitropropane-1,3-diol, formic acid in acid form or as its salt, 4,4’-dichloro 2-hydroxydiphenylether, and combinations thereof.
10. Use of a composition according to any of the preceding claims for laundry or hard surface care.
11. Process for making a composition according to any of claims 1 to 9 comprising the steps of
(i) making the polymer cited in any of claims 1 to 9 in a process comprising the steps of (a) reacting a diamine according to general formula H2-N-Z-NH2 with alkylene oxide in a molar ratio alkylene oxide: diamine of from 4:1 to 1:1 with alkylene oxide being se lected from ethylene oxide and propylene oxide, thereby forming an intermediate,
(b) subjecting the intermediate from step (a) to polycondensation under catalysis of at least one acidic catalyst, thereby obtaining a polycondensate, (y) reacting the polycondensate from step (b) with at least one C2-C4-alkylene oxide in one or more steps,
(ii) obtaining a composition comprising the polymer obtained in step (i), and
(iii) adding at least one enzyme to the composition obtained in step (ii), and optionally
(iv) adding a surfactant to the composition obtained in step (iii).
12. Method of improving the cleaning performance of a detergent composition, preferably a liquid detergent composition, by adding a polymer (A) cited in any of claims 1 to 9 to a de tergent composition comprising at least one enzyme (B), preferably a lipase and/or at least one protease and/or a mannanase, most preferably comprising a protease.
13. Use of a composition according to any of claims 1 to 9 for biofilm removal and/or biofilm prevention and/or sebum stain removal and/or for malodour reduction on a textile or hard surface.
14. Method for biofilm removal and/or biofilm prevention and/or sebum stain removal and/or for malodour reduction on a textile or hard surface comprising the steps of
(i) providing a liquid composition comprising (A) at least one polymer comprising
(a) a core that bears one to 3 moieties of the general formula (I)
Figure imgf000063_0001
wherein Z are different or the same and selected from C2-Ci2-alkylene and C3- Ci2-cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-CrC4-alkyl groups and wherein C3-Ci2-cycloalkylene may bear one to three methyl groups,
X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, n is in the range of from 1 to 4, (b) polyalkylene oxide chains; and (B) at least one enzyme;
(ii) contacting a textile or a hard surface with the liquid composition of step (i) for a time and under conditions suitable to allow biofilm removal and/or biofilm prevention and/or sebum stain removal and/or malodour reduction.
PCT/EP2020/083599 2019-11-29 2020-11-27 Compositions comprising polymer and enzyme WO2021105336A1 (en)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP19212620.9 2019-11-29
EP19212620 2019-11-29

Publications (1)

Publication Number Publication Date
WO2021105336A1 true WO2021105336A1 (en) 2021-06-03

Family

ID=68732987

Family Applications (2)

Application Number Title Priority Date Filing Date
PCT/EP2020/083599 WO2021105336A1 (en) 2019-11-29 2020-11-27 Compositions comprising polymer and enzyme
PCT/EP2020/083591 WO2021105330A1 (en) 2019-11-29 2020-11-27 Compositions and polymers useful for such compositions

Family Applications After (1)

Application Number Title Priority Date Filing Date
PCT/EP2020/083591 WO2021105330A1 (en) 2019-11-29 2020-11-27 Compositions and polymers useful for such compositions

Country Status (3)

Country Link
CN (1) CN113891931A (en)
BR (1) BR112021021050A2 (en)
WO (2) WO2021105336A1 (en)

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2023061827A1 (en) * 2021-10-13 2023-04-20 Basf Se Compositions comprising polymers, polymers, and their use
WO2023148086A1 (en) * 2022-02-04 2023-08-10 Basf Se Compositions comprising polymers, polymers, and their use
EP4368691A1 (en) * 2022-11-09 2024-05-15 Henkel AG & Co. KGaA Detergent composition with improved properties

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2023110599A2 (en) * 2021-12-17 2023-06-22 Basf Se Compositions and their applications

Citations (145)

* 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
US4435307A (en) 1980-04-30 1984-03-06 Novo Industri A/S Detergent cellulase
EP0218272A1 (en) 1985-08-09 1987-04-15 Gist-Brocades N.V. Novel lipolytic enzymes and their use in detergent compositions
EP0258068A2 (en) 1986-08-29 1988-03-02 Novo Nordisk A/S Enzymatic detergent additive
EP0260105A2 (en) 1986-09-09 1988-03-16 Genencor, Inc. Preparation of enzymes having altered activity
JPS6336774B2 (en) 1979-05-25 1988-07-21 Tokyo Shibaura Electric Co
EP0283075A2 (en) 1987-02-27 1988-09-21 Gist-Brocades N.V. Molecular cloning and expression of genes encoding proteolytic enzymes
JPS6356289B2 (en) 1979-11-15 1988-11-08 Kansai Denryoku Kk
EP0305216A1 (en) 1987-08-28 1989-03-01 Novo Nordisk A/S Recombinant Humicola lipase and process for the production of recombinant humicola lipases
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
WO1989006279A1 (en) 1988-01-07 1989-07-13 Novo-Nordisk A/S Mutated subtilisin genes
EP0331376A2 (en) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. Recombinant DNA, bacterium of the genus pseudomonas containing it, and process for preparing lipase by using it
WO1989009259A1 (en) 1988-03-24 1989-10-05 Novo-Nordisk A/S A cellulase preparation
JPH02238885A (en) 1989-03-13 1990-09-21 Oji Paper Co Ltd Phenol oxidase gene recombination dna, microorganism transformed with same recombinant dna, culture mixture thereof and production of phenol oxidase
EP0407225A1 (en) 1989-07-07 1991-01-09 Unilever Plc Enzymes and enzymatic detergent compositions
JPH034706A (en) 1989-05-31 1991-01-10 Kubota Corp Preparation of artificial seed
WO1991002792A1 (en) 1989-08-25 1991-03-07 Henkel Research Corporation Alkaline proteolytic enzyme and method of production
WO1991016422A1 (en) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Alkaline bacillus lipases, coding dna sequences therefor and bacilli which produce these lipases
WO1991017244A1 (en) 1990-05-09 1991-11-14 Novo Nordisk A/S An enzyme capable of degrading cellulose or hemicellulose
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
WO1992001046A1 (en) 1990-07-06 1992-01-23 Valtion Teknillinen Tutkimuskeskus Laccase production by recombinant organisms
WO1992005249A1 (en) 1990-09-13 1992-04-02 Novo Nordisk A/S Lipase variants
WO1992006165A1 (en) 1991-06-11 1992-04-16 Genencor International, Inc. Detergent compositions containing cellulase compositions deficient in cbh i type components
EP0495257A1 (en) 1991-01-16 1992-07-22 The Procter & Gamble Company Compact detergent compositions with high activity cellulase
WO1992019729A1 (en) 1991-05-01 1992-11-12 Novo Nordisk A/S Stabilized enzymes and detergent compositions
EP0531372A1 (en) 1990-05-09 1993-03-17 Novo Nordisk As A cellulase preparation comprising an endoglucanase enzyme.
WO1993017244A1 (en) 1992-02-28 1993-09-02 Institut Teplofiziki Jet-type vacuum pump
WO1993024618A1 (en) 1992-06-01 1993-12-09 Novo Nordisk A/S Peroxidase variants with improved hydrogen peroxide stability
WO1993024622A1 (en) 1992-05-22 1993-12-09 Alko Ltd. Mannanase enzymes, genes coding for them, methods for isolating the genes, and methods for bleaching lignocellulosic pulps
WO1994001541A1 (en) 1992-07-06 1994-01-20 Novo Nordisk A/S C. antarctica lipase and lipase variants
WO1994002597A1 (en) 1992-07-23 1994-02-03 Novo Nordisk A/S MUTANT α-AMYLASE, DETERGENT, DISH WASHING AGENT, AND LIQUEFACTION AGENT
WO1994007998A1 (en) 1992-10-06 1994-04-14 Novo Nordisk A/S Cellulase variants
WO1994018314A1 (en) 1993-02-11 1994-08-18 Genencor International, Inc. Oxidatively stable alpha-amylase
WO1994021801A2 (en) 1993-03-17 1994-09-29 Genencor International, Inc. Purification and molecular cloning of eg iii cellulase
WO1994025578A1 (en) 1993-04-27 1994-11-10 Gist-Brocades N.V. New lipase variants for use in detergent applications
WO1994026880A1 (en) 1993-05-10 1994-11-24 Gist-Brocades N.V. Combined action of endoglucanases and cellobiohydrolases
WO1995002043A1 (en) 1993-07-06 1995-01-19 Novo Nordisk A/S DNA ENCODING AN ENZYME WITH ENDOGLUCANASE ACTIVITY FROM $i(TRICHODERMA HARZIANUM)
WO1995002675A1 (en) 1993-07-12 1995-01-26 Novo Nordisk A/S A detergent composition comprising two cellulase components
WO1995006720A1 (en) 1993-08-30 1995-03-09 Showa Denko K.K. Novel lipase, microorganism producing the lipase, process for producing the lipase, and use of the lipase
WO1995010603A1 (en) 1993-10-08 1995-04-20 Novo Nordisk A/S Amylase variants
WO1995010602A1 (en) 1993-10-13 1995-04-20 Novo Nordisk A/S H2o2-stable peroxidase variants
WO1995014783A1 (en) 1993-11-24 1995-06-01 Showa Denko K.K. Lipase gene and variant lipase
WO1995022615A1 (en) 1994-02-22 1995-08-24 Novo Nordisk A/S A method of preparing a variant of a lipolytic enzyme
WO1995023221A1 (en) 1994-02-24 1995-08-31 Cognis, Inc. Improved enzymes and detergents containing them
WO1995024471A1 (en) 1994-03-08 1995-09-14 Novo Nordisk A/S Novel alkaline cellulases
WO1995027046A2 (en) 1994-03-31 1995-10-12 Unilever Nv Enzymatic antimicrobial compositions containing haloperoxidases
WO1995030744A2 (en) 1994-05-04 1995-11-16 Genencor International Inc. Lipases with improved surfactant resistance
WO1995033836A1 (en) 1994-06-03 1995-12-14 Novo Nordisk Biotech, Inc. Phosphonyldipeptides useful in the treatment of cardiovascular diseases
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
JPH0851975A (en) 1991-10-09 1996-02-27 Res Dev Corp Of Japan New beta-mannanase and method for producing the same
WO1996011262A1 (en) 1994-10-06 1996-04-18 Novo Nordisk A/S An enzyme and enzyme preparation with endoglucanase activity
WO1996012012A1 (en) 1994-10-14 1996-04-25 Solvay S.A. Lipase, microorganism producing same, method for preparing said lipase and uses thereof
WO1996013580A1 (en) 1994-10-26 1996-05-09 Novo Nordisk A/S An enzyme with lipolytic activity
WO1996023872A1 (en) 1995-02-02 1996-08-08 Stichting Centraal Laboratorium Van De Bloedtransfusiedienst Van Het Nederlandse Rode Kruis Enrichment of hematopoietic stem cells from blood or bone marrow
WO1996027002A1 (en) 1995-02-27 1996-09-06 Novo Nordisk A/S Novel lipase gene and process for the production of lipase with the use of the same
WO1996029397A1 (en) 1995-03-17 1996-09-26 Novo Nordisk A/S Novel endoglucanases
WO1996034946A1 (en) 1995-05-05 1996-11-07 Novo Nordisk A/S Protease variants and compositions
WO1997003296A1 (en) 1995-07-08 1997-01-30 Hohmann Joerg Device for measuring the extension of a threaded bolt or screw
WO1997004079A1 (en) 1995-07-14 1997-02-06 Novo Nordisk A/S A modified enzyme with lipolytic activity
WO1997004102A1 (en) 1995-07-14 1997-02-06 Novo Nordisk A/S Haloperoxidases from curvularia verruculosa and nucleic acids encoding same
WO1997007202A1 (en) 1995-08-11 1997-02-27 Novo Nordisk A/S Novel lipolytic enzymes
WO1997008325A2 (en) 1995-08-25 1997-03-06 Novo Nordisk Biotech, Inc. Purified coprinus laccases and nucleic acids encoding same
WO1997011164A1 (en) 1995-09-20 1997-03-27 Genencor International, Inc. Purified mannanase from bacillus amyloliquefaciens and method of preparation
WO1997014804A1 (en) 1995-10-17 1997-04-24 Röhn Enzyme Finland OY Cellulases, the genes encoding them and uses thereof
US5648263A (en) 1988-03-24 1997-07-15 Novo Nordisk A/S Methods for reducing the harshness of a cotton-containing fabric
WO1997043424A1 (en) 1996-05-14 1997-11-20 Genencor International, Inc. MODIFIED α-AMYLASES HAVING ALTERED CALCIUM BINDING PROPERTIES
WO1998008940A1 (en) 1996-08-26 1998-03-05 Novo Nordisk A/S A novel endoglucanase
WO1998010060A1 (en) 1996-09-03 1998-03-12 Novo Nordisk A/S Peroxidase variants
WO1998012307A1 (en) 1996-09-17 1998-03-26 Novo Nordisk A/S Cellulase variants
WO1998015257A1 (en) 1996-10-08 1998-04-16 Novo Nordisk A/S Diaminobenzoic acid derivatives as dye precursors
WO1998020115A1 (en) 1996-11-04 1998-05-14 Novo Nordisk A/S Subtilase variants and compositions
WO1998020116A1 (en) 1996-11-04 1998-05-14 Novo Nordisk A/S Subtilase variants and compositions
EP0851023A2 (en) 1996-12-23 1998-07-01 Unilever N.V. Machine dishwashing tablets containing a peracid
US5869438A (en) 1990-09-13 1999-02-09 Novo Nordisk A/S Lipase variants
WO1999011768A1 (en) 1997-08-29 1999-03-11 Novo Nordisk A/S Protease variants and compositions
WO1999019467A1 (en) 1997-10-13 1999-04-22 Novo Nordisk A/S α-AMYLASE MUTANTS
WO1999027083A1 (en) 1997-11-24 1999-06-03 Novo Nordisk A/S PECTIN DEGRADING ENZYMES FROM $i(BACILLUS LICHENIFORMIS)
WO1999027084A1 (en) 1997-11-24 1999-06-03 Novo Nordisk A/S Novel pectate lyases
DE19819187A1 (en) 1998-04-30 1999-11-11 Henkel Kgaa Solid dishwasher detergent with phosphate and crystalline layered silicates
WO1999064619A2 (en) 1998-06-10 1999-12-16 Novozymes A/S Novel mannanases
WO2000022103A1 (en) 1998-10-13 2000-04-20 Novozymes A/S A modified polypeptide with reduced immune response
US6124127A (en) 1997-11-24 2000-09-26 Novo Nordisk A/S Pectate lyase
WO2000060063A1 (en) 1999-03-31 2000-10-12 Novozymes A/S Lipase variant
WO2000060060A2 (en) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides having alkaline alpha-amylase activity and nucleic acids encoding same
WO2001044452A1 (en) 1999-12-15 2001-06-21 Novozymes A/S Subtilase variants having an improved wash performance on egg stains
WO2001079459A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2001079458A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2001079461A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2001079460A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2002006442A2 (en) 2000-07-19 2002-01-24 Novozymes A/S Cell-wall degrading enzyme variants
WO2002010355A2 (en) 2000-08-01 2002-02-07 Novozymes A/S Alpha-amylase mutants with altered stability
DE10064983A1 (en) 2000-12-23 2002-07-18 Henkel Kgaa New subtilisin protease from Bacillus alcalophilus, useful e.g. in washing and cleaning compositions, comprises at positions 230, 256 and 259 amino acids Val, Gly and Asn
EP1240525A2 (en) 1999-12-23 2002-09-18 PHARMACIA & UPJOHN COMPANY Sodium channels as targets for amyloid beta
WO2002088340A2 (en) 2001-05-02 2002-11-07 Henkel Kommanditgesellschaft Auf Aktien Alkaline protease variants and detergents and cleaning agents containing said alkaline protease variants
WO2002092741A2 (en) 2001-05-14 2002-11-21 Novozymes A/S 0etergent compositions comprising bacillus subtilis pectate lyases
WO2002099091A2 (en) 2001-06-06 2002-12-12 Novozymes A/S Endo-beta-1,4-glucanase from bacillus
WO2003006602A2 (en) 2001-07-12 2003-01-23 Novozymes A/S Subtilase variants
EP1305432A2 (en) 2000-08-04 2003-05-02 Genencor International, Inc. Mutant trichoderma reesei egiii cellulases, dna encoding such egiii compositions and methods for obtaining same
WO2003054184A1 (en) 2001-12-20 2003-07-03 Henkel Kommanditgesellschaft Auf Aktien Novel alkali protease formed by bacillus gibsonii (dsm 14393) and washing and cleaning agents containing said novel alkali protease
WO2003056017A2 (en) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Alkaline protease from bacillus sp. (dsm 14390) and washing and cleaning products comprising said alkaline protease
WO2003055974A2 (en) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Novel alkaline protease from bacillus sp. (dsm 14392) and washing and cleaning products comprising said novel alkaline protease
WO2003095638A1 (en) 2002-05-14 2003-11-20 Novozymes A/S Pectate lyase variants
WO2004003186A2 (en) 2002-06-26 2004-01-08 Novozymes A/S Subtilases and subtilase variants having altered immunogenicity
WO2004041979A2 (en) 2002-11-06 2004-05-21 Novozymes A/S Subtilase variants
WO2004053039A2 (en) 2002-12-11 2004-06-24 Novozymes A/S Detergent composition comprising endo-glucanase
WO2005056782A2 (en) 2003-12-03 2005-06-23 Genencor International, Inc. Perhydrolase
WO2005063974A1 (en) 2003-12-23 2005-07-14 Henkel Kommanditgesellschaft Auf Aktien Novel alkaline protease and washing and cleaning products containing said novel alkaline protease
WO2005103244A1 (en) 2004-04-23 2005-11-03 Henkel Kommanditgesellschaft Auf Aktien Novel alkaline proteases, and detergents and cleaners containing the same
WO2006002643A2 (en) 2004-07-05 2006-01-12 Novozymes A/S Alpha-amylase variants with altered properties
WO2006066594A2 (en) 2004-12-23 2006-06-29 Novozymes A/S Alpha-amylase variants
WO2007006305A1 (en) 2005-07-08 2007-01-18 Novozymes A/S Subtilase variants
US20070167344A1 (en) 2003-12-03 2007-07-19 Amin Neelam S Enzyme for the production of long chain peracid
WO2007087508A2 (en) 2006-01-23 2007-08-02 Novozymes A/S Lipase variants
WO2008051491A2 (en) 2006-10-20 2008-05-02 Danisco Us, Inc. Genencor Division Polyol oxidases
WO2009061380A2 (en) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division VARIANTS OF BACILLUS sp. TS-23 ALPHA-AMYLASE WITH ALTERED PROPERTIES
US20090124531A1 (en) * 2007-11-09 2009-05-14 James Lee Danziger Cleaning compositions with amphiphilic water-soluble polyalkylenimines having an inner polyethylene oxide block and an outer polypropylene oxide block
WO2009067279A1 (en) 2007-11-21 2009-05-28 E.I. Du Pont De Nemours And Company Production of peracids using an enzyme having perhydrolysis activity
WO2009074685A1 (en) 2007-12-12 2009-06-18 Novozymes A/S Enzymatic degradation of biomass substrates comprising mannan
WO2009109500A1 (en) 2008-02-29 2009-09-11 Novozymes A/S Polypeptides having lipase activity and polynucleotides encoding same
WO2009127702A2 (en) 2008-04-17 2009-10-22 Novozymes A/S Laccase variants
WO2010065455A2 (en) 2008-12-01 2010-06-10 Danisco Us Inc. Enzymes with lipase activity
WO2010100028A2 (en) 2009-03-06 2010-09-10 Huntsman Advanced Materials (Switzerland) Gmbh Enzymatic textile bleach-whitening methods
WO2010104675A1 (en) 2009-03-10 2010-09-16 Danisco Us Inc. Bacillus megaterium strain dsm90-related alpha-amylases, and methods of use, thereof
WO2010111143A2 (en) 2009-03-23 2010-09-30 Danisco Us Inc. Cal a-related acyltransferases and methods of use, thereof
WO2011036263A1 (en) 2009-09-25 2011-03-31 Novozymes A/S Subtilase variants
WO2011036264A1 (en) 2009-09-25 2011-03-31 Novozymes A/S Use of protease variants
WO2011072099A2 (en) 2009-12-09 2011-06-16 Danisco Us Inc. Compositions and methods comprising protease variants
WO2011084417A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing geobacillus stearothermophilus lipase and methods of use thereof
WO2011084412A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing thermobifida fusca lipase and methods of use thereof
WO2011084599A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing bacillus subtilis lipase and methods of use thereof
WO2011098531A1 (en) 2010-02-10 2011-08-18 Novozymes A/S Variants and compositions comprising variants with high stability in presence of a chelating agent
WO2011150157A2 (en) 2010-05-28 2011-12-01 Danisco Us Inc. Detergent compositions containing streptomyces griseus lipase and methods of use thereof
WO2012137147A1 (en) 2011-04-08 2012-10-11 Danisco Us, Inc. Compositions
WO2013001087A2 (en) 2011-06-30 2013-01-03 Novozymes A/S Method for screening alpha-amylases
WO2013001078A1 (en) 2011-06-30 2013-01-03 Novozymes A/S Alpha-amylase variants
WO2013184577A1 (en) 2012-06-08 2013-12-12 Danisco Us Inc. Alpha-amylase variants derived from the alpha amylase of cytophaga sp.amylase|(cspamy2).
WO2014100018A1 (en) 2012-12-19 2014-06-26 Danisco Us Inc. Novel mannanase, compositions and methods of use thereof
WO2014183921A1 (en) 2013-05-17 2014-11-20 Novozymes A/S Polypeptides having alpha amylase activity
WO2014183920A1 (en) 2013-05-17 2014-11-20 Novozymes A/S Polypeptides having alpha amylase activity
WO2016092009A1 (en) 2014-12-10 2016-06-16 Henkel Ag & Co. Kgaa Solid detergents and cleaning agents with amylase
EP3162878A1 (en) * 2015-10-29 2017-05-03 The Procter and Gamble Company Liquid detergent composition
WO2018029021A1 (en) * 2016-08-08 2018-02-15 Basf Se Liquid laundry formulation
WO2019081724A1 (en) 2017-10-27 2019-05-02 Novozymes A/S Dnase variants
WO2019201636A1 (en) * 2018-04-19 2019-10-24 Basf Se Compositions and polymers useful for such compositions

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2008094238A1 (en) * 2007-01-30 2008-08-07 Dow Global Technologies, Inc. Ortho-cyclohexanediamine-initiated polyols and rigid polyurethane foam made therefrom

Patent Citations (151)

* 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
JPS6336774B2 (en) 1979-05-25 1988-07-21 Tokyo Shibaura Electric Co
JPS6356289B2 (en) 1979-11-15 1988-11-08 Kansai Denryoku Kk
US4435307A (en) 1980-04-30 1984-03-06 Novo Industri A/S Detergent cellulase
EP0218272A1 (en) 1985-08-09 1987-04-15 Gist-Brocades N.V. Novel lipolytic enzymes and their use in detergent compositions
EP0258068A2 (en) 1986-08-29 1988-03-02 Novo Nordisk A/S Enzymatic detergent additive
EP0260105A2 (en) 1986-09-09 1988-03-16 Genencor, Inc. Preparation of enzymes having altered activity
EP0283075A2 (en) 1987-02-27 1988-09-21 Gist-Brocades N.V. Molecular cloning and expression of genes encoding proteolytic enzymes
EP0305216A1 (en) 1987-08-28 1989-03-01 Novo Nordisk A/S Recombinant Humicola lipase and process for the production of recombinant humicola lipases
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
WO1989006279A1 (en) 1988-01-07 1989-07-13 Novo-Nordisk A/S Mutated subtilisin genes
EP0331376A2 (en) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. Recombinant DNA, bacterium of the genus pseudomonas containing it, and process for preparing lipase by using it
WO1989009259A1 (en) 1988-03-24 1989-10-05 Novo-Nordisk A/S A cellulase preparation
US5648263A (en) 1988-03-24 1997-07-15 Novo Nordisk A/S Methods for reducing the harshness of a cotton-containing fabric
US5776757A (en) 1988-03-24 1998-07-07 Novo Nordisk A/S Fungal cellulase composition containing alkaline CMC-endoglucanase and essentially no cellobiohydrolase and method of making thereof
JPH02238885A (en) 1989-03-13 1990-09-21 Oji Paper Co Ltd Phenol oxidase gene recombination dna, microorganism transformed with same recombinant dna, culture mixture thereof and production of phenol oxidase
JPH034706A (en) 1989-05-31 1991-01-10 Kubota Corp Preparation of artificial seed
EP0407225A1 (en) 1989-07-07 1991-01-09 Unilever Plc Enzymes and enzymatic detergent compositions
WO1991002792A1 (en) 1989-08-25 1991-03-07 Henkel Research Corporation Alkaline proteolytic enzyme and method of production
WO1991016422A1 (en) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Alkaline bacillus lipases, coding dna sequences therefor and bacilli which produce these lipases
WO1991017244A1 (en) 1990-05-09 1991-11-14 Novo Nordisk A/S An enzyme capable of degrading cellulose or hemicellulose
EP0531372A1 (en) 1990-05-09 1993-03-17 Novo Nordisk As A cellulase preparation comprising an endoglucanase enzyme.
EP0531315A1 (en) 1990-05-09 1993-03-17 Novo Nordisk As An enzyme capable of degrading cellulose or hemicellulose.
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
WO1992001046A1 (en) 1990-07-06 1992-01-23 Valtion Teknillinen Tutkimuskeskus Laccase production by recombinant organisms
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
EP0495257A1 (en) 1991-01-16 1992-07-22 The Procter & Gamble Company Compact detergent compositions with high activity cellulase
WO1992019729A1 (en) 1991-05-01 1992-11-12 Novo Nordisk A/S Stabilized enzymes and detergent compositions
WO1992006165A1 (en) 1991-06-11 1992-04-16 Genencor International, Inc. Detergent compositions containing cellulase compositions deficient in cbh i type components
JPH0851975A (en) 1991-10-09 1996-02-27 Res Dev Corp Of Japan New beta-mannanase and method for producing the same
WO1993017244A1 (en) 1992-02-28 1993-09-02 Institut Teplofiziki Jet-type vacuum pump
WO1993024622A1 (en) 1992-05-22 1993-12-09 Alko Ltd. Mannanase enzymes, genes coding for them, methods for isolating the genes, and methods for bleaching lignocellulosic pulps
WO1993024618A1 (en) 1992-06-01 1993-12-09 Novo Nordisk A/S Peroxidase variants with improved hydrogen peroxide stability
WO1994001541A1 (en) 1992-07-06 1994-01-20 Novo Nordisk A/S C. antarctica lipase and lipase variants
WO1994002597A1 (en) 1992-07-23 1994-02-03 Novo Nordisk A/S MUTANT α-AMYLASE, DETERGENT, DISH WASHING AGENT, AND LIQUEFACTION AGENT
WO1994007998A1 (en) 1992-10-06 1994-04-14 Novo Nordisk A/S Cellulase variants
WO1994018314A1 (en) 1993-02-11 1994-08-18 Genencor International, Inc. Oxidatively stable alpha-amylase
WO1994021801A2 (en) 1993-03-17 1994-09-29 Genencor International, Inc. Purification and molecular cloning of eg iii cellulase
WO1994025578A1 (en) 1993-04-27 1994-11-10 Gist-Brocades N.V. New lipase variants for use in detergent applications
WO1994026880A1 (en) 1993-05-10 1994-11-24 Gist-Brocades N.V. Combined action of endoglucanases and cellobiohydrolases
WO1995002043A1 (en) 1993-07-06 1995-01-19 Novo Nordisk A/S DNA ENCODING AN ENZYME WITH ENDOGLUCANASE ACTIVITY FROM $i(TRICHODERMA HARZIANUM)
WO1995002675A1 (en) 1993-07-12 1995-01-26 Novo Nordisk A/S A detergent composition comprising two cellulase components
WO1995006720A1 (en) 1993-08-30 1995-03-09 Showa Denko K.K. Novel lipase, microorganism producing the lipase, process for producing the lipase, and use of the lipase
WO1995010603A1 (en) 1993-10-08 1995-04-20 Novo Nordisk A/S Amylase variants
WO1995010602A1 (en) 1993-10-13 1995-04-20 Novo Nordisk A/S H2o2-stable peroxidase variants
WO1995014783A1 (en) 1993-11-24 1995-06-01 Showa Denko K.K. Lipase gene and variant lipase
WO1995022615A1 (en) 1994-02-22 1995-08-24 Novo Nordisk A/S A method of preparing a variant of a lipolytic enzyme
WO1995023221A1 (en) 1994-02-24 1995-08-31 Cognis, Inc. Improved enzymes and detergents containing them
EP1921147A2 (en) 1994-02-24 2008-05-14 Henkel Kommanditgesellschaft auf Aktien Improved enzymes and detergents containing them
WO1995024471A1 (en) 1994-03-08 1995-09-14 Novo Nordisk A/S Novel alkaline cellulases
WO1995027046A2 (en) 1994-03-31 1995-10-12 Unilever Nv Enzymatic antimicrobial compositions containing haloperoxidases
WO1995030744A2 (en) 1994-05-04 1995-11-16 Genencor International Inc. Lipases with improved surfactant resistance
WO1995033836A1 (en) 1994-06-03 1995-12-14 Novo Nordisk Biotech, Inc. Phosphonyldipeptides useful in the treatment of cardiovascular diseases
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
WO1996011262A1 (en) 1994-10-06 1996-04-18 Novo Nordisk A/S An enzyme and enzyme preparation with endoglucanase activity
WO1996012012A1 (en) 1994-10-14 1996-04-25 Solvay S.A. Lipase, microorganism producing same, method for preparing said lipase and uses thereof
WO1996013580A1 (en) 1994-10-26 1996-05-09 Novo Nordisk A/S An enzyme with lipolytic activity
WO1996023872A1 (en) 1995-02-02 1996-08-08 Stichting Centraal Laboratorium Van De Bloedtransfusiedienst Van Het Nederlandse Rode Kruis Enrichment of hematopoietic stem cells from blood or bone marrow
WO1996027002A1 (en) 1995-02-27 1996-09-06 Novo Nordisk A/S Novel lipase gene and process for the production of lipase with the use of the same
WO1996029397A1 (en) 1995-03-17 1996-09-26 Novo Nordisk A/S Novel endoglucanases
WO1996034946A1 (en) 1995-05-05 1996-11-07 Novo Nordisk A/S Protease variants and compositions
WO1997003296A1 (en) 1995-07-08 1997-01-30 Hohmann Joerg Device for measuring the extension of a threaded bolt or screw
WO1997004079A1 (en) 1995-07-14 1997-02-06 Novo Nordisk A/S A modified enzyme with lipolytic activity
WO1997004102A1 (en) 1995-07-14 1997-02-06 Novo Nordisk A/S Haloperoxidases from curvularia verruculosa and nucleic acids encoding same
WO1997007202A1 (en) 1995-08-11 1997-02-27 Novo Nordisk A/S Novel lipolytic enzymes
WO1997008325A2 (en) 1995-08-25 1997-03-06 Novo Nordisk Biotech, Inc. Purified coprinus laccases and nucleic acids encoding same
WO1997011164A1 (en) 1995-09-20 1997-03-27 Genencor International, Inc. Purified mannanase from bacillus amyloliquefaciens and method of preparation
WO1997014804A1 (en) 1995-10-17 1997-04-24 Röhn Enzyme Finland OY Cellulases, the genes encoding them and uses thereof
WO1997043424A1 (en) 1996-05-14 1997-11-20 Genencor International, Inc. MODIFIED α-AMYLASES HAVING ALTERED CALCIUM BINDING PROPERTIES
WO1998008940A1 (en) 1996-08-26 1998-03-05 Novo Nordisk A/S A novel endoglucanase
WO1998010060A1 (en) 1996-09-03 1998-03-12 Novo Nordisk A/S Peroxidase variants
WO1998012307A1 (en) 1996-09-17 1998-03-26 Novo Nordisk A/S Cellulase variants
WO1998015257A1 (en) 1996-10-08 1998-04-16 Novo Nordisk A/S Diaminobenzoic acid derivatives as dye precursors
WO1998020116A1 (en) 1996-11-04 1998-05-14 Novo Nordisk A/S Subtilase variants and compositions
WO1998020115A1 (en) 1996-11-04 1998-05-14 Novo Nordisk A/S Subtilase variants and compositions
EP0851023A2 (en) 1996-12-23 1998-07-01 Unilever N.V. Machine dishwashing tablets containing a peracid
WO1999011768A1 (en) 1997-08-29 1999-03-11 Novo Nordisk A/S Protease variants and compositions
WO1999019467A1 (en) 1997-10-13 1999-04-22 Novo Nordisk A/S α-AMYLASE MUTANTS
WO1999027083A1 (en) 1997-11-24 1999-06-03 Novo Nordisk A/S PECTIN DEGRADING ENZYMES FROM $i(BACILLUS LICHENIFORMIS)
WO1999027084A1 (en) 1997-11-24 1999-06-03 Novo Nordisk A/S Novel pectate lyases
US6124127A (en) 1997-11-24 2000-09-26 Novo Nordisk A/S Pectate lyase
DE19819187A1 (en) 1998-04-30 1999-11-11 Henkel Kgaa Solid dishwasher detergent with phosphate and crystalline layered silicates
WO1999064619A2 (en) 1998-06-10 1999-12-16 Novozymes A/S Novel mannanases
WO2000022103A1 (en) 1998-10-13 2000-04-20 Novozymes A/S A modified polypeptide with reduced immune response
WO2000060060A2 (en) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides having alkaline alpha-amylase activity and nucleic acids encoding same
WO2000060063A1 (en) 1999-03-31 2000-10-12 Novozymes A/S Lipase variant
WO2001044452A1 (en) 1999-12-15 2001-06-21 Novozymes A/S Subtilase variants having an improved wash performance on egg stains
EP1240525A2 (en) 1999-12-23 2002-09-18 PHARMACIA & UPJOHN COMPANY Sodium channels as targets for amyloid beta
WO2001079459A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2001079458A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2001079461A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2001079460A2 (en) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides having haloperoxidase activity
WO2002006442A2 (en) 2000-07-19 2002-01-24 Novozymes A/S Cell-wall degrading enzyme variants
WO2002010355A2 (en) 2000-08-01 2002-02-07 Novozymes A/S Alpha-amylase mutants with altered stability
EP1305432A2 (en) 2000-08-04 2003-05-02 Genencor International, Inc. Mutant trichoderma reesei egiii cellulases, dna encoding such egiii compositions and methods for obtaining same
DE10064983A1 (en) 2000-12-23 2002-07-18 Henkel Kgaa New subtilisin protease from Bacillus alcalophilus, useful e.g. in washing and cleaning compositions, comprises at positions 230, 256 and 259 amino acids Val, Gly and Asn
WO2002088340A2 (en) 2001-05-02 2002-11-07 Henkel Kommanditgesellschaft Auf Aktien Alkaline protease variants and detergents and cleaning agents containing said alkaline protease variants
WO2002092741A2 (en) 2001-05-14 2002-11-21 Novozymes A/S 0etergent compositions comprising bacillus subtilis pectate lyases
WO2002099091A2 (en) 2001-06-06 2002-12-12 Novozymes A/S Endo-beta-1,4-glucanase from bacillus
WO2003006602A2 (en) 2001-07-12 2003-01-23 Novozymes A/S Subtilase variants
WO2003054184A1 (en) 2001-12-20 2003-07-03 Henkel Kommanditgesellschaft Auf Aktien Novel alkali protease formed by bacillus gibsonii (dsm 14393) and washing and cleaning agents containing said novel alkali protease
WO2003056017A2 (en) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Alkaline protease from bacillus sp. (dsm 14390) and washing and cleaning products comprising said alkaline protease
WO2003055974A2 (en) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Novel alkaline protease from bacillus sp. (dsm 14392) and washing and cleaning products comprising said novel alkaline protease
WO2003095638A1 (en) 2002-05-14 2003-11-20 Novozymes A/S Pectate lyase variants
WO2004003186A2 (en) 2002-06-26 2004-01-08 Novozymes A/S Subtilases and subtilase variants having altered immunogenicity
WO2004041979A2 (en) 2002-11-06 2004-05-21 Novozymes A/S Subtilase variants
WO2004053039A2 (en) 2002-12-11 2004-06-24 Novozymes A/S Detergent composition comprising endo-glucanase
WO2005056782A2 (en) 2003-12-03 2005-06-23 Genencor International, Inc. Perhydrolase
US20080145353A1 (en) 2003-12-03 2008-06-19 Amin Neelam S Perhydrolase
US20070167344A1 (en) 2003-12-03 2007-07-19 Amin Neelam S Enzyme for the production of long chain peracid
WO2005063974A1 (en) 2003-12-23 2005-07-14 Henkel Kommanditgesellschaft Auf Aktien Novel alkaline protease and washing and cleaning products containing said novel alkaline protease
WO2005103244A1 (en) 2004-04-23 2005-11-03 Henkel Kommanditgesellschaft Auf Aktien Novel alkaline proteases, and detergents and cleaners containing the same
WO2006002643A2 (en) 2004-07-05 2006-01-12 Novozymes A/S Alpha-amylase variants with altered properties
WO2006066594A2 (en) 2004-12-23 2006-06-29 Novozymes A/S Alpha-amylase variants
WO2007006305A1 (en) 2005-07-08 2007-01-18 Novozymes A/S Subtilase variants
WO2007087508A2 (en) 2006-01-23 2007-08-02 Novozymes A/S Lipase variants
WO2008051491A2 (en) 2006-10-20 2008-05-02 Danisco Us, Inc. Genencor Division Polyol oxidases
WO2008063400A1 (en) 2006-11-09 2008-05-29 Danisco Us, Inc., Genencor Division Enzyme for the production of long chain peracid
WO2009061380A2 (en) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division VARIANTS OF BACILLUS sp. TS-23 ALPHA-AMYLASE WITH ALTERED PROPERTIES
US20090124531A1 (en) * 2007-11-09 2009-05-14 James Lee Danziger Cleaning compositions with amphiphilic water-soluble polyalkylenimines having an inner polyethylene oxide block and an outer polypropylene oxide block
WO2009067279A1 (en) 2007-11-21 2009-05-28 E.I. Du Pont De Nemours And Company Production of peracids using an enzyme having perhydrolysis activity
WO2009074685A1 (en) 2007-12-12 2009-06-18 Novozymes A/S Enzymatic degradation of biomass substrates comprising mannan
WO2009109500A1 (en) 2008-02-29 2009-09-11 Novozymes A/S Polypeptides having lipase activity and polynucleotides encoding same
WO2009127702A2 (en) 2008-04-17 2009-10-22 Novozymes A/S Laccase variants
WO2010065455A2 (en) 2008-12-01 2010-06-10 Danisco Us Inc. Enzymes with lipase activity
WO2010100028A2 (en) 2009-03-06 2010-09-10 Huntsman Advanced Materials (Switzerland) Gmbh Enzymatic textile bleach-whitening methods
WO2010104675A1 (en) 2009-03-10 2010-09-16 Danisco Us Inc. Bacillus megaterium strain dsm90-related alpha-amylases, and methods of use, thereof
WO2010111143A2 (en) 2009-03-23 2010-09-30 Danisco Us Inc. Cal a-related acyltransferases and methods of use, thereof
WO2011036263A1 (en) 2009-09-25 2011-03-31 Novozymes A/S Subtilase variants
WO2011036264A1 (en) 2009-09-25 2011-03-31 Novozymes A/S Use of protease variants
WO2011072099A2 (en) 2009-12-09 2011-06-16 Danisco Us Inc. Compositions and methods comprising protease variants
WO2011084417A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing geobacillus stearothermophilus lipase and methods of use thereof
WO2011084412A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing thermobifida fusca lipase and methods of use thereof
WO2011084599A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing bacillus subtilis lipase and methods of use thereof
WO2011098531A1 (en) 2010-02-10 2011-08-18 Novozymes A/S Variants and compositions comprising variants with high stability in presence of a chelating agent
WO2011150157A2 (en) 2010-05-28 2011-12-01 Danisco Us Inc. Detergent compositions containing streptomyces griseus lipase and methods of use thereof
WO2012137147A1 (en) 2011-04-08 2012-10-11 Danisco Us, Inc. Compositions
WO2013001087A2 (en) 2011-06-30 2013-01-03 Novozymes A/S Method for screening alpha-amylases
WO2013001078A1 (en) 2011-06-30 2013-01-03 Novozymes A/S Alpha-amylase variants
WO2013184577A1 (en) 2012-06-08 2013-12-12 Danisco Us Inc. Alpha-amylase variants derived from the alpha amylase of cytophaga sp.amylase|(cspamy2).
WO2014100018A1 (en) 2012-12-19 2014-06-26 Danisco Us Inc. Novel mannanase, compositions and methods of use thereof
WO2014183921A1 (en) 2013-05-17 2014-11-20 Novozymes A/S Polypeptides having alpha amylase activity
WO2014183920A1 (en) 2013-05-17 2014-11-20 Novozymes A/S Polypeptides having alpha amylase activity
WO2016092009A1 (en) 2014-12-10 2016-06-16 Henkel Ag & Co. Kgaa Solid detergents and cleaning agents with amylase
EP3162878A1 (en) * 2015-10-29 2017-05-03 The Procter and Gamble Company Liquid detergent composition
WO2018029021A1 (en) * 2016-08-08 2018-02-15 Basf Se Liquid laundry formulation
WO2019081724A1 (en) 2017-10-27 2019-05-02 Novozymes A/S Dnase variants
WO2019081721A1 (en) 2017-10-27 2019-05-02 Novozymes A/S Dnase variants
WO2019201636A1 (en) * 2018-04-19 2019-10-24 Basf Se Compositions and polymers useful for such compositions

Non-Patent Citations (22)

* Cited by examiner, † Cited by third party
Title
"Methods in Enzymology", vol. 160, 1988, pages: 200 - 391
BEGUIN, P.: "Molecular Biology of Cellulose Degradation", ANNU. REV. MICROBIOL., vol. 44, 1990, pages 219248
BEGUN, P.AUBERT, J-P.: "The biological degradation of cellulose", FEMS MICROBIOLOGY RE VIEWS, vol. 13, 1994, pages 25 - 58
CAS , no. 1802181-67-4
CAS, no. 164907-72-6
CHILDS ET AL., BIOCHEMICAL J, vol. 145, pages 93 - 103
DARTOIS ET AL., BIOCHEMICA ET BIOPHYSICA ACTA, vol. 1131, 1992, pages 253 - 360
DELMAR ET AL., ANALYTICAL BIOCHEM, vol. 99, 1979, pages 316 - 320
EL SMITH ET AL., J. BIOL CHEM, vol. 243, 1968, pages 2184 - 2191
GUPTA ET AL., APPL. MICROBIOL. BIOTECHNOL., vol. 60, 2002, pages 381 - 395
GUPTA ET AL., BIOTECHNOL. APPL. BIOCHEM., vol. 37, 2003, pages 63 - 71
HENRISSAT, B.: "Cellulases and their interaction with cellulose", CELLULOSE, vol. 1, 1994, pages 169 - 196, XP009062749, DOI: 10.1007/BF00813506
HOFFMAN, W. S., J. BIOL. CHEM., vol. 120, 1937, pages 51
J. MOL. BIOL., vol. 48, 1979, pages 443 - 453
JA WELLS ET AL., NUCLEIC ACIDS RESEARCH, vol. 11, 1983, pages 7911 - 7925
JACOBS ET AL., NUCL. ACIDS RES, vol. 13, 1985, pages 8913 - 8926
M. H. BOYER, EUROPEAN JOURNAL OF BIOCHEMISTRY, vol. 162, 1987, pages 311 - 316
MCCLEARY, B. V., CARBOHYDRATE RESEARCH, vol. 67, no. 1, 1978, pages 213 - 221
MILLER, G. L.: "Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugars", ANALYTICAL CHEMISTRY, vol. 31, 1959, pages 426 - 428
NOMENCLATURE COMMITTEE OF THE INTERNATIONAL UNION OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, ENZYME NOMENCLATURE, RECOMMENDATIONS, 1992
T.-M. ENVERIW.M. FOGARTY: "Microbial Enzymes and Biotechnology", 1983, APPLIED SCIENCE PUBLISHERS, article "Microbial Cellulases", pages: 183 - 224
VASANTHA ET AL., J. BAC-TERIOL., vol. 159, 1984, pages 811 - 819

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2023061827A1 (en) * 2021-10-13 2023-04-20 Basf Se Compositions comprising polymers, polymers, and their use
WO2023148086A1 (en) * 2022-02-04 2023-08-10 Basf Se Compositions comprising polymers, polymers, and their use
EP4368691A1 (en) * 2022-11-09 2024-05-15 Henkel AG & Co. KGaA Detergent composition with improved properties

Also Published As

Publication number Publication date
BR112021021050A2 (en) 2022-09-13
WO2021105330A1 (en) 2021-06-03
CN113891931A (en) 2022-01-04

Similar Documents

Publication Publication Date Title
US11739287B2 (en) Cleaning compositions and uses thereof
US11352591B2 (en) Cleaning compositions and uses thereof
EP3433347B1 (en) Use of polypeptide having dnase activity for treating fabrics
EP3478811B1 (en) Cleaning compositions and uses thereof
WO2021105336A1 (en) Compositions comprising polymer and enzyme
US20210189296A1 (en) Cleaning compositions and uses thereof
US20210340466A1 (en) Detergent compositions and uses thereof
US20230033580A1 (en) Use of cellulase for improvement of sustainability of detergents
WO2018161899A1 (en) Use of one or more enzymes in preventing, inhibiting or reducing microbe growth on a surface
US20200332227A1 (en) Use of Enzyme in Removing Airborne Particulate Matter from Textile
US20200277553A1 (en) Use of Enzymes for Improving Water Absorption And/Or Whiteness
US20190093055A1 (en) Laundry method, use of polypeptide and detergent composition
WO2006131503A2 (en) Detergents with enzymatic builder and bleach systems
US20230024242A1 (en) Cleaning compositions comprising dispersins viii
WO2021074430A1 (en) Storage-stable hydrolase containing liquids
US20230159861A1 (en) Enzyme compositions and uses thereof
CN116096731A (en) Improved combinations of protease and protease inhibitor with a second enzyme
US20230040230A1 (en) Cleaning composition comprising a dispersin and a carbohydrase
US20230045289A1 (en) Cleaning compositions comprising dispersins ix
US20220033739A1 (en) Cleaning compositions and uses thereof
EP4314222A1 (en) Detergent composition with reduced polymer content
US20230048546A1 (en) Cleaning compositions comprising dispersins vi
WO2022083538A1 (en) Use of polypeptide, detergent composition and cleaning method
DK202330021A1 (en) Detergent powder comprising laccase

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 20811369

Country of ref document: EP

Kind code of ref document: A1

NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 20811369

Country of ref document: EP

Kind code of ref document: A1