JP2020500980A - Cleaning compositions containing enzymes - Google Patents

Abstract

A cleaning composition comprising an amylase enzyme and a glycosyl hydrolase enzyme. Methods for producing and using a cleaning composition comprising a glycosyl hydrolase enzyme. Use of glycosyl hydrolase enzymes.

Description

  The present disclosure relates to cleaning compositions that include certain glycoside hydrolase enzymes. The present disclosure also relates to methods of making and using such cleaning compositions. The present disclosure also relates to the use of glycoside hydrolase enzymes.

(Refer to sequence list)
The present application includes a sequence listing in computer readable form, which is incorporated herein by reference.

  Detergent formulators are always aiming to improve the performance of detergent compositions. One of the specific challenges is the removal of certain microorganism-derived soils from surfaces such as textile products. Such dirt may be sticky and difficult to remove. Furthermore, since these stains are sticky, they tend to stick body stains and / or particulate stains to the surface, making it difficult to remove stains and tending to accumulate over time. This can be particularly noticeable, for example, at the collar and cuff portions where incomplete cleaning can occur.

  There is a need for improved cleaning compositions that clean such soils. The present inventors have discovered that a cleaning composition comprising certain glycoside hydrolases can ameliorate this problem. Glycosyl hydrolases are enzymes that catalyze the hydrolysis of glycosyl bonds and release smaller sugars. More than 100 classes of glycosyl hydrolases and many different enzymes, such as cellulases and xyloglucanases that can be used in cleaning compositions, are included within this class of glycosyl hydrolases. Surprisingly, certain specific glycosyl hydrolases can provide particularly improved washes.

  Glycoside hydrolases are described in Coutinho, P .; M. And Henrissat, B .; , 1999, Carbohydrate-active Enzymes: an integrated database approach, "Recent Advances in Carbohydrate Bioengineering", H. et al. J. Gilbert, G .; Davies, B .; Henrissat and B.A. Svensson eds. , The Royal Society of Chemistry, Cambridge, pp. 3-12.

Coutinho, P .; M. And Henrissat, B .; , 1999, Carbohydrate-active Enzymes: an integrated database approach, "Recent Advances in Carbohydrate Bioengineering", H. et al. J. Gilbert, G .; Davies, B .; Henrissat and B.A. Svensson eds. , The Royal Society of Chemistry, Cambridge, pp. 3-12

  The present invention relates to a cleaning and / or treating composition comprising an amylase enzyme and an enzyme having glycoside hydrolase activity, wherein the glycoside hydrolase enzyme classifies endo-α-1,4-polygalactosaminidase. A composition selected from the enzymes of (EC 3.2.1.109).

  Preferred glycoside hydrolase enzymes having glycoside hydrolase activity are at least 60% identity to SEQ ID NO: 1, or at least 65%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or A variant having at least 90%, or at least 95% identity, less than 100% or up to 100% identity.

  Preferably, the composition comprises from 1 to 80% by weight of a surfactant system, preferably comprising an anionic surfactant. The present invention is a method of cleaning a surface, for example, a textile product, comprising mixing the cleaning composition described herein with water to form an aqueous liquid, and in the washing step, the surface and the aqueous solution. Contacting with a liquid. Preferably, the glycoside hydrolase enzyme is present in the aqueous liquor in an amount of 0.01 ppm to 1000 ppm enzyme based on active protein.

  The present invention also has an amylase enzyme and a glycoside hydrolase activity for enhancing dirt and / or stain removal and / or for reducing malodors, in particular for removing body soil, and has an endo- selected from enzymes of the class of α-1,4-polygalactosaminidase (EC 3.2.1.109), preferably at least 60%, or at least 65%, or at least 70%, relative to SEQ ID NO: 1. Or an enzyme having at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95% identity, up to 100% identity.

  A preferred composition comprises a second glycosyl hydrolase enzyme selected from glycoside hydrolase family 39.

  The components of the compositions and processes of the present disclosure are described in more detail below.

  As used herein, the articles "a" and "an", as used in the claims, are understood to mean one or more of those claimed or described. You. As used herein, the terms "include", "includes", and "including" are meant to be non-limiting. The compositions of the present disclosure can comprise, consist essentially of, or consist of the components of the present disclosure.

  As used herein, the terms “substantially free of” or “substantially free from” may be used. This means that the indicated material is in a minimal amount and is not intentionally added to the composition to form part of the composition, or preferably is analytically detectable Means not present in concentration. That means that the indicated material comprises a composition that is only present as an impurity in one of the other materials intentionally included. The indicated materials, if any, may be present at a level of less than 1%, or less than 0.1%, or less than 0.01%, or even 0% by weight of the composition.

  As used herein, the term "etheramine" includes the term "polyetheramine" and includes amines having one or more ether groups.

  Unless otherwise specified, all concentrations of a component or composition are with respect to the active portion of the component or composition and any impurities, such as residual solvents or by-products, that may be present in commercial sources of such component or composition. Things are excluded.

  All temperatures in this specification are in degrees Celsius (° C.) unless otherwise noted. Unless otherwise specified, all measurements herein are performed at 20 ° C. under atmospheric pressure.

  In all embodiments of the present disclosure, all percentages (%) are by weight of the total composition, unless otherwise specified. All ratios are by weight unless otherwise indicated.

  All maximum numerical limitations set forth throughout this specification are intended to include all lower numerical limitations, as if such lower numerical limitations were expressly written herein. You should understand. Every minimum numerical limitation given throughout this specification will include every higher numerical limitation, as if such higher numerical limitations were expressly written herein. All numerical ranges given throughout this specification are to be deemed to include all narrower numerical ranges falling within such broader numerical ranges, as if such narrower numerical ranges were all expressly written herein. So to include.

  As used herein, the term "alkoxy" is intended to include C1-C8 alkoxy and C1-C8 alkoxy derivatives of polyols having repeating units such as butylene oxide, glycidol oxide, ethylene oxide or propylene oxide.

  As used herein, unless otherwise stated, the terms "alkyl" and "alkyl end-protection" are intended to include C1-C18 alkyl groups, or even C1-C6 alkyl groups.

  As used herein, unless otherwise stated, the term "aryl" is intended to include C3-C12 aryl groups.

  As used herein, unless otherwise specified, the terms "arylalkyl" and "alkaryl" are equivalent, and typically refer to a C1-C18 alkyl group and, in one embodiment, a C1-C6 alkyl group, respectively. It is intended to include groups having an alkyl moiety attached to an aromatic moiety.

  As used herein, the terms "ethylene oxide", "propylene oxide", and "butylene oxide" may be designated by their typical notations, "EO", "PO", and "BO", respectively.

  As used herein, the term “cleaning and / or treating composition”, unless otherwise stated, refers to a granular, powder, liquid, gel, paste, single dose, bar form and / or flake type cleaning agent. And / or a fabric treatment composition comprising a fabric treatment composition, a fabric softening composition, a fabric strengthening composition, a fabric freshening composition, and other products for care and maintenance of the fabric, and These combinations include, but are not limited to. Such a composition may be a pre-treatment composition for use prior to the washing step, but also a rinse addition composition, and a bleaching additive and / or "stain-removing stick", or a pre-treatment composition, or A cleaning aid such as a product having a substrate such as a sheet for adding a dryer may be used.

  As used herein, "cellulosic substrate" refers to 100% by weight of cellulose, or at least 20%, or at least 30%, or at least 40%, or at least 50%, or even at least 60%. It is intended to include any substrate that includes weight percent cellulose. Cellulose can be found in wood, cotton, linen, jute and linen. The cellulosic substrate may be in the form of powder, fiber, pulp, and in the form of articles formed from powder, fiber, and pulp. Cellulose fibers include, but are not limited to, cotton, rayon (regenerated cellulose), acetate (cellulose acetate), triacetate (cellulose triacetate), and mixtures thereof. Typically, the cellulosic substrate comprises cotton. Articles formed from cellulosic fibers include woven articles such as fabrics. Articles formed from pulp include paper.

  As used herein, the term "maximum extinction coefficient" is intended to represent the molar extinction coefficient at the wavelength of the absorption maximum in the range of 400 nanometers to 750 nanometers (also referred to herein as the maximum wavelength). .

  As used herein, "average molecular weight" is reported as the weight average molecular weight as determined by its molecular weight distribution, and as a result of these manufacturing processes, the polymers disclosed herein have a , A repeating unit of a certain distribution.

  As used herein, the term "variant" refers to a polypeptide that contains an amino acid sequence that differs from a wild-type or reference sequence. A variant polypeptide may differ from a wild-type or reference sequence described above by a nucleotide deletion, insertion or substitution relative to the reference or wild-type nucleotide sequence. The reference or wild-type sequence can be a full-length native polypeptide sequence or any other fragment of a full-length polypeptide sequence. Polypeptide variants generally have at least about 70% amino acid sequence identity with the reference sequence, but have 75% amino acid sequence identity with the reference sequence, 80% amino acid sequence identity with the reference sequence, 85% amino acid sequence identity, 86% amino acid sequence identity with reference sequence, 87% amino acid sequence identity with reference sequence, 88% amino acid sequence identity with reference sequence, 89% amino acid sequence with reference sequence Identity, 90% amino acid sequence identity with reference sequence, 91% amino acid sequence identity with reference sequence, 92% amino acid sequence identity with reference sequence, 93% amino acid sequence identity with reference sequence, reference sequence 94% amino acid sequence identity, 95% amino acid sequence identity with reference sequence, 96% amino acid sequence identity with reference sequence, 97% amino acid sequence identity with reference sequence, reference Columns and 98% amino acid sequence identity to a reference sequence and 98.5% amino acid sequence identity, or reference sequence may contain 99% amino acid sequence identity.

  As used herein, the term "solid" includes granule, powder, bar and tablet product forms.

  As used herein, the term "fluid" includes liquid, gel, paste and gaseous product forms.

Cleaning compositions The present disclosure relates to cleaning compositions and / or treatment compositions. The cleaning compositions include mild liquid detergent compositions, strong liquid detergent compositions, solids such as powder detergents, hard surface cleaning compositions, detergent gels commonly used in laundry, bleaching compositions, laundry additives, textiles. It may be selected from the group consisting of enhancing compositions, shampoos, body soaps, other personal care compositions, and mixtures thereof. The cleaning composition may be a hard surface cleaning composition (such as a dishwashing composition) or a laundry composition (such as a heavy liquid detergent composition).

  The cleaning composition can be in any suitable form. The composition can be selected from a liquid, a solid or a combination thereof. As used herein, "liquid" includes free flowing liquids, as well as pastes, gels, foams, and mousses. Non-limiting examples of liquids include light and heavy liquid detergent compositions, fabric softeners, detergent gels commonly used in laundry, bleaches and laundry additives. Gases (eg, suspended bubbles) or solids (eg, particles) may be included in the liquid. As used herein, "solid" includes, but is not limited to, powders, agglomerates, and mixtures thereof. Non-limiting examples of solids include granules, microcapsules, beads, noodles, and pearlescent balls. Solid compositions can provide technical benefits, including but not limited to benefits during cleaning, benefits of pre-treatment, and / or aesthetic effects.

  The cleaning composition may be in the form of a unitized dose article, such as a tablet, or in the form of a pouch. Such pouches typically include a water-soluble film that at least partially encapsulates the composition, for example, a polyvinyl alcohol water-soluble film. Suitable films are available from MonoSol, LLC (Indiana, USA). The composition may be enclosed in a single compartment pouch or in a multi-compartment pouch. A multi-compartment pouch may have at least two, at least three, or at least four compartments. Multi-compartment pouches may include compartments arranged side by side and / or stacked. The composition contained within the pouch may be a liquid, a solid (such as a powder), or a combination thereof.

Glycoside Hydrolase Enzyme The enzyme essential for the present invention has a glycoside hydrolase activity belonging to the endo-α-1,4-polygalactosaminidase class (EC 3.2.1.109), preferably SEQ ID NO: It has at least 60% or 65%, or more preferably at least 70% or 75%, or 80%, or 85%, or 90%, or 95%, up to 100% identity to 1.

  Preferably, the glycoside hydrolase is from GH family 114.

  Preferably, the glycoside hydrolase enzyme is a microbial enzyme. Glycoside hydrolase enzymes may be of fungal or bacterial origin. Bacterial glycoside hydrolases may be most preferred. Fungal glycoside hydrolases may be most preferred.

  Glycoside hydrolases can be obtained from Pseudomonas, for example, Pseudomonas aeruginosa. Suitable examples of the classification EC 3.2.1.109 are described in Baker et al. , (2016) Sci Adv, 2, and is, for example, the mature polypeptide of the present invention from Pseudomonas aeruginosa SEQ ID NO: 1. Preferably, the glycoside hydrolase in the cleaning composition of the present invention is PelAh, optionally in addition to a further glycoside hydrolase.

  Preferably, the glycoside hydrolase is an isolated glycoside hydrolase.

  Preferably, the glycoside hydrolase enzyme is present in the cleaning composition from 0.001 to 1% by weight, based on the active protein in the composition, or from 0.005 to 0.5% by weight, based on the weight of the composition. It is present in an amount of 0.01 to 0.25% by weight.

  Preferably, the glycoside hydrolase enzyme is present in the aqueous wash liquor in an amount of 0.01 ppm to 1000 ppm of enzyme, based on active protein, or in an amount of 0.05 ppm or 0.1 ppm to 750 ppm or 500 ppm.

  The glycoside hydrolases described herein may also produce a biofilm disrupting effect or an anti-redeposition effect.

Amylase enzyme The composition comprises an amylase enzyme. Suitable α-amylases include those of bacterial or fungal origin. Chemically or genetically modified mutants (variants) are included. Preferred alkaline [alpha] -amylases are Bacillus strains, e.g., Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or other Bacillus sp. For example, Bacillus sp. NCIB 12289, NCIB 12512, NCIB 12513, DSM 9375 (US Pat. No. 7,153,818), DSM 12368, DSMZ no. 12649, KSM AP1378 (WO 97/00324), KSM K36 or KSM K38 (European Patent No. 1,022,334). Preferred amylases include:
(A) the variants described in WO 94/02597, WO 94/18314, WO 96/23874 and WO 97/43424, in particular the SEQ ID NOs: WO 96/23874 For the enzyme listed as SEQ ID No. 2 (SEQ ID NO: 2 herein), the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 181, 188, 190, 197, A variant in which one or more of 202, 208, 209, 243, 264, 304, 305, 391, 408, and 444 has been substituted.
(B) variants described in U.S. Pat. No. 5,856,164, and WO 99/23211, WO 96/23873, WO 00/60060 and WO 06/002643; In particular, for the AA560 enzyme listed herein as SEQ ID NO: 12 in WO 06/002643 (SEQ ID NO: 3 herein), a variant having one or more substitutions at the following positions:
26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 203, 214, 231, 256, 257, 258, 269, 270, 272, 283,295,296,298,299,303,304,305,311,314,315,318,319,339,345,361,378,383,419,421,437,441,444,445,446, A variant in which one or more of 447, 450, 461, 471, 482, 484 is substituted, preferably a variant also containing a deletion of D183 ^* and G184 ^* .
(C) variants exhibiting at least 90% identity to SEQ ID NO: 4 (SEQ ID NO: 4 herein) in WO 06/002643, a wild-type enzyme from Bacillus SP722, especially 183 And variants with deletions at positions 184 and 184, and variants described in WO 00/60060, which are incorporated herein by reference.
(D) Bacillus sp. 707 (SEQ ID NO: 7 of US Pat. No. 6,093,562) showing at least 95% identity to the wild-type enzyme (SEQ ID NO: 5 herein), particularly the following mutations: M202, M208 , S255, R172 and / or M261. Preferably, the amylase comprises one or more of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N and / or R172Q. Particularly preferred are those containing the M202L or M202T mutation.
(E) variants described in WO 09/149130, preferably SEQ ID NO: 1 or SEQ ID NO: 2 in WO 09/149130 (SEQ ID NO: 6 or SEQ ID NO: 7, respectively herein) Those showing at least 90% identity, the wild-type enzyme from Geobacillus stearopherophilus or a truncated version thereof.
(F) Mutants described in European Patent Nos. 2,540,825, 2,357,220 and 2,534,233.
(G) Mutants described in WO2009100102 and WO2010115028.
(H) variants exhibiting at least 89% identity to SEQ ID NO: 1 (SEQ ID NO: 8 herein) of WO201609688, particularly deletions at positions H183 + G184 and 405, 421, 422 and / or 428 A variant comprising one or more mutations at positions.
(I) A mutant showing at least 60% amino acid sequence identity with “PcuAmyl α-amylase” (SEQ ID NO: 3 of WO201499523) derived from Paenibacillus curdlanolyticus YK9 (SEQ ID NO: 9 in the present specification).
(J) Cytophaga sp. A variant exhibiting at least 60% amino acid sequence identity with “CspAmy2 amylase” (SEQ ID NO: 1 of WO2014164777) (SEQ ID NO: 10 herein) derived from the strain.
(K) A variant showing at least 85% amino acid sequence identity with Bacillus subtilis (SEQ ID NO: 1 of WO2009149271 (SEQ ID NO: 11 herein)).
(L) Bacillus sp. With accession number AB051102 A variant showing at least 90% identity to wild-type amylase from KSM-K38.

  Suitable commercially available α-amylases include DURAMYL®, LIQUEZYME®, TERMAMYL®, TERMAMYL ULTRA®, NATALASE®, SUPRAMYL®, STAINZYME® (Registered trademark), STAINZYME PLUS (registered trademark), FUNGAMYL (registered trademark) and BAN (registered trademark) (Novozymes A / S (Bagsvaerd, Denmark)), KEMZYM (registered trademark) AT 9000 (Biozym Biotechnology Trading Gas Trading Gas-Bridge Technology) 1200 Wien Austria), RAPIDASE (registered trademark), PURASTAR (registered trademark), ENZYSIZE (registered trademark) (Trademark), OPTISISE HT PLUS (registered trademark), POWERASE (registered trademark) and PURASTAR OXAM (registered trademark) (Genencor International Inc., (Palo Alto, California), and KAM (registered trademark) (Kao (103-8210, Tokyo, Japan) In one embodiment, suitable amylase includes NATALASE®, STAINZYME® and STAINZYME PLUS®, and mixtures thereof. The amylase is preferably from about 0.00001% to about 2%, from about 0.0001% to about 1%, or even from about 0.001% to about 0.5% by weight of the composition. Wt% enzyme tan Present in the amount of protein.

Optional Second Glycosyl Hydrolase Enzyme A preferred composition comprises a second glycosyl hydrolase enzyme, and is preferably selected from GH family 39. A preferred second glycosyl hydrolase is at least 60%, or at least 65%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least, based on SEQ ID NO: 13. Contains glycoside hydrolase enzymes with 95%, or less than 100%, or up to 100% identity. Preferably, the second glycosyl hydrolase enzyme comprises a microbial enzyme and may be of fungal or bacterial origin.

  The second glycoside hydrolase can be obtained from Pseudomonas, for example, Pseudomonas aeruginosa. Suitable examples are described in Baker et al. , (2016) Sci Adv, 2, and is, for example, the mature polypeptide of the present invention from Pseudomonas aeruginosa SEQ ID NO: 12. A preferred second glycoside hydrolase in the cleaning composition of the present invention is PslGh. When present in a composition, the second glycoside hydrolase described above can comprise from about 0.00001% to about 2%, from about 0.0001% to about 1%, or even about 0. 1% by weight of the composition. It may be present at a concentration of the enzyme protein of from 001% to about 0.5% by weight.

Additives The cleaning compositions described herein optionally include other additive components, such as fabric care benefit agents; additional enzymes; surfactant systems; fabric shading dyes; deposition aids; Denaturant; builder; chelating agent; bleach; bleach activator; bleach; bleach precursor; bleach accelerator; bleach catalyst; fragrance and / or fragrance microcapsules; fragrance-filled zeolite; starch-encapsulated accord; polyglycerol ester; Whitening agents; pearlescent agents; enzyme stabilizer systems; scavengers including anionic dye fixatives, anionic surfactant complexing agents, and mixtures thereof; optional bleaching or fluorescent agents; Polymers, including but not limited to polymers and / or soil suspension polymers; dispersants; defoamers; non-aqueous solvents; fatty acids; Cationic starch; scum dispersants; direct dyes; colorants; opacifiers; antioxidants; hydrotropes such as toluenesulfonate, cumenesulfonate and naphthalene sulfonate; color particles; colored beads, spheres or extrudates; , An antibacterial agent, and a quaternary ammonium compound. In particular, a quaternary ammonium compound may be present for a fabric-enhancing composition (eg, a fabric softener) and has the structure NR ₄ ^{+ where} R is an alkyl or aryl group. A quaternary ammonium cation that is a positively charged polyatomic ion.

Additional Enzymes Preferably, the compositions of the present invention comprise an additional enzyme selected from, for example, lipases, proteases, nucleases, galactanases, mannanases, pectate lyases, cellulases, cutinases, and mixtures thereof. The cleaning composition preferably comprises one or more additional enzymes from the group selected from nucleases, galactanases, mannanases, and mixtures thereof. The cleaning composition preferably comprises one or more additional enzymes from the group selected from the group consisting of nucleases, galactanases, mannanases, and mixtures thereof. Preferably, in addition to this, the cleaning composition comprises one or more additional enzymes selected from proteases. Preferably, the cleaning composition comprises one or more additional enzymes selected from lipases. The composition comprises hemicellulase, peroxidase, xylanase, pectinase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, pullulanase, tannase, pentosanase, malanase, β-glucanase, arabinosidase, hyaluronidase, chondroitinase, laccase. And mixtures thereof. When present in the composition, the additional enzyme comprises from about 0.00001% to about 2%, from about 0.0001% to about 1%, or even about 0.001% by weight of the composition. % To about 0.5% by weight of the enzyme protein.

Nuclease In a preferred composition, the composition further comprises a nuclease enzyme. Nuclease enzymes are enzymes that can cleave phosphodiester bonds between nucleotide subunits of nucleic acids. A suitable nuclease enzyme may be a deoxyribonuclease or a ribonuclease enzyme, or a functional fragment thereof. By functional fragment or moiety is meant a portion of a nuclease enzyme that catalyzes the cleavage of a phosphodiester bond in the DNA backbone, and is thus a region of the nuclease protein that retains catalytic activity. Thus, it includes truncated but functional versions of enzymes and / or variants and / or derivatives and / or homologs whose function is maintained.

  Preferably, the nuclease enzyme is a deoxyribonuclease, preferably selected from any of the following classes: C. 3.1.21. x (where x = 1, 2, 3, 4, 5, 6, 7, 8 or 9); C. 3.1.22. y (where y = 1, 2, 4, or 5); C. 3.1.30. z (where z = 1 or 2), E.I. C. 3.1.31.1, and mixtures thereof. Classification E. C. 3.1.21. Nuclease enzymes derived from x, especially x = 1, are particularly preferred. Classification E. C. 3.1.22. The nuclease in y cleaves at the 5 'hydroxyl, releasing the 3' phosphomonoester. Classification E. C. 3.1.30. The enzyme in z may be preferred because it acts on both DNA and RNA, releasing 5'-phosphomonoesters. Classification E. C. Suitable examples from 3.1.31.2 are described in U.S. Patent Publication No. 2012/0135498 (A), for example, SEQ ID NO: 3 therein. Such an enzyme is commercially available from c-LECTA as DENARASE® enzyme. Classification E. C. The nuclease enzyme from 3.1.31.1 produces a 3 'phosphomonoester.

  Preferably, the nuclease enzyme comprises a microbial enzyme. The nuclease enzyme may be of fungal or bacterial origin. Bacterial nucleases may be most preferred. Fungal nucleases may be most preferred.

  Microbial nucleases can be obtained from Bacillus, such as Bacillus licheniformis or Bacillus subtilis bacterial nuclease. Preferred nucleases can be obtained from Bacillus licheniformis, preferably strain EI-34-6. A preferred deoxyribonuclease is a mutant of Bacillus licheniformis derived from EI-34-6 strain nucB deoxyribonuclease, as defined in SEQ ID NO: 14 herein, or a mutant thereof, eg, at least 70% or 75% thereof. Or 80%, or 85%, or 90%, or 95%, 96%, 97%, 98%, 99% or 100% identity. Other suitable nucleases are set forth in SEQ ID NO: 15 herein, or variants thereof, for example, at least 70%, or 75%, or 80%, or 85%, or 90%, Or 95%, 96%, 97%, 98%, 99% or 100% identity. Other suitable nucleases are set forth in SEQ ID NO: 16 herein, or variants thereof, eg, at least 70%, or 75%, or 80%, or 85%, or 90%, thereto. Or 95%, 96%, 97%, 98%, 99% or 100% identity.

  Fungal nucleases can be obtained from Aspergillus, for example, Aspergillus oryzae. A preferred nuclease is Aspergillus oryzae as defined herein in SEQ ID NO: 17, or a variant thereof, eg, at least 60%, or 70%, or 75%, or 80%, or 85%, or 90% thereto. Or 95%, 96%, 97%, 98%, 99% or 100% identity.

  Another suitable fungal nuclease can be obtained from Trichoderma, for example, Trichoderma harzianum. A preferred nuclease is Trichoderma harzianam as defined herein in SEQ ID NO: 18, or a variant thereof, eg, at least 60%, or 70%, or 75%, or 80%, or 85%, or It can be obtained from those having 90%, or 95%, 96%, 97%, 98%, 99% or 100% identity.

  Other fungal nuclease, Aspergillus oryzae RIB40, Aspergillus oryzae 3.042, Aspergillus flavus NRRL3357, Aspergillus parasiticus SU-1, Aspergillus nomius NRRL13137, Trichoderma reesei QM6a, Trichoderma virens Gv29-8, Oidiodendron maius Zn, Metarhizium guizhouense ARSEF 977, Metalhizium majus ARCEF 297, Metalhizium Robertsii ARCEF 23, Metalhizium acridum CQMa 1 2, Metarhizium brunneum ARSEF 3297, Metarhizium anisopliae, Colletotrichum fioriniae PJ7, Colletotrichum sublineola, Trichoderma atroviride IMI 206040, Tolypocladium ophioglossoides CBS 100239, Beauveria bassiana ARSEF 2860, Colletotrichum higginsianum, Hirsutella minnesotensis 3608, Scedosporium apiospermum, Phaeomoniella chlamydospora, Fusarium ver icillioides 7600, Fusarium oxysporum f. sp. cubense variety 4, Colletotrichum graminicola M1.001, Fusarium oxysporum FOSC 3-a, Fusarium avenuesum. sp. cubense varieties 1, Magnaporthe oryzae 70-15, Beauveria bassiana D1-5, Fusarium pseudograinamineum CS3096, Neo nectria tis ti pos ti ti m s ti pi s s s s s sp. "Multigermtubi" MB_m1, Diaporthe ampelina, Metalhizium album ARCEF 1941, Colletotrichum gloeosporoides Narumec. 102, Gaeumanomyces graminis varieties tritici R3-111a-1, Nectria haematococca mpVI 77-13-4, Verticillium longisporum, Verticillium dahliae VdLs. 17, Torrubiella hemipterigena, Verticillium longisporum, Verticillium dahliae VdLs. 17, Botrytis cinerea B05.10, Chaetomium globosum CBS 148.51, Metarhizium anisopliae, Stemphylium lycopersici, Sclerotinia borealis F-4157, Metarhizium robertsii ARSEF 23, Myceliophthora thermophila ATCC 42464, Phaeosphaeria nodorum SN15, Phialophora attae, Ustilaginoidea virens, Diplodia seriata, Ophistoma piceae UAMH 11346, Pseudogymnoascus pannorum KM F-4515 (FW-2607), Bipolaris oryzae ATCC 44560, Metarhizium guizhouense ARSEF 977, Chaetomium thermophilum variant thermophilum DSM 1495, Pestalotiopsis fici W106-1, Bipolaris zeicola 26-R-13, Setosphaeria turcica Et28A, Arthroderma otae CBS 113480, And nucleases encoded by the DNA sequence of Pyrenophora tritici-repentis Pt-1C-BFP.

  Preferably, the nuclease is an isolated nuclease.

  Preferably, the nuclease enzyme is present in the aqueous solution in an amount of 0.01 ppm to 1000 ppm nuclease enzyme, or in an amount from 0.05 ppm or 0.1 ppm to 750 ppm or 500 ppm.

Galactanase Preferably, as an additional enzyme, the composition comprises galactanase. Particularly preferred is endo-β-1,6-galactanase extracellular polymer degrading enzyme. The term “endo-β-1,6-galactan” or “polypeptide having endo-β-1,6-galactoctonase activity” refers to 1,6-3-galactoligos having a degree of polymerization (DP) higher than 3. Endo-β-1,6-derived from sugars and from glycoside hydrolase family 30 which catalyzes the hydrolytic cleavage of 4-O-methylglucosyluronate groups or their acidic derivatives having a glucosyluronate group at the non-reducing end. It means galactoctanase (EC 3.2.1.164). For the purposes of this disclosure, endo-β-1,6-galactanase activity is determined in Assay I according to the procedure described in WO2015185689. Suitable examples from the class EC 3.2.1.164 are described in WO2015185689, for example the mature polypeptide SEQ ID NO: 2 described therein.

  Preferably, the galactanase enzyme is selected from glycoside hydrolase family 30.

  Preferably, the endo-β-1,6-galactanase is a microbial enzyme. The endo-β-1,6-galactanase may be of fungal or bacterial origin. Bacterial endo-β-1,6-galactanase may be most preferred. Fungal endo-β-1,6-galactaner may be most preferred.

  Bacterial endo-β-1,6-galactanase can be obtained from Streptomyces, for example, Streptomyces davawensis. A preferred endo-β-1,6-galactanase is Streptomyces davawensis JCM 4913 as defined in SEQ ID NO: 19 herein, or a variant thereof, eg, at least 40%, or 50%, or 60% thereto. Or 70%, or 75%, or 80%, or 85%, or 90%, or 95%, 96%, 97%, 98%, 99% or 100% identity. .

  Other bacterial endo-β-1,6-galactanases include those encoded by the DNA sequence of Streptomyces avermitilis MA-4680 having the amino acid sequence defined in SEQ ID NO: 20, or a mutant thereof, For example, at least 40%, or 50%, or 60%, or 70%, or 75%, or 80%, or 85%, or 90%, or 95%, 96%, 97%, 98%, Those having 99% or 100% identity can be mentioned.

  Fungal endo-β-1,6-galactanase can be obtained from Trichoderma, eg, Trichoderma harzianum. A preferred endo-β-1,6-galactanase is Trichoderma harzianum as defined herein in SEQ ID NO: 21, or a variant thereof, eg, at least 40%, or 50%, or 60%, or 70%, or 75%, or 80%, or 85%, or 90%, or 95%, 96%, 97%, 98%, 99% or 100% identity.

  Other fungal endo-β-1,6-galactanases include Ceratocystis fimbriata f. sp. Platani, Muscodor strobeliii WG-2009a, Oculimacula yallundae, Trichoderma virido GD36A, Thermomyces stellatus, DNA of Mycelophthora thermophilia, whose sequences are listed by Mycelophthora thermophilia.

  Preferably, the galactanase has an amino acid sequence having at least 60%, or at least 80%, or at least 90%, or at least 95% identity to the amino acid sequence set forth in SEQ ID NO: 19, SEQ ID NO: 20 or SEQ ID NO: 21. Have.

  Preferably, the galactanase is an isolated galactanase.

  Preferably, the galactanase enzyme is present in the composition at 0.001-1% by weight, based on the active protein in the composition, or 0.005-0.5% by weight, based on the weight of the composition, or It is present in an amount of 0.01 to 0.25% by weight. Preferably, the galactanase enzyme is present in the aqueous laundry solution in an amount of 0.01 ppm to 1000 ppm galactanase enzyme, or in an amount from 0.05 ppm or 0.1 ppm to 750 ppm or 500 ppm.

Mannanase Preferably, the composition comprises a mannanase enzyme. The mannanase enzyme is a mannan endo-1,4-β-mannosidase activity from glycoside hydrolase family 26 that catalyzes the hydrolysis of 1,4-3-D-mannosidic bonds in mannan, galactomannan and glucomannan (EC 3.2. 1.78). Other names of mannan endo-1,4-β-mannosidase are 1,4-3-D-mannanman nanohydrolase, endo-1,4-3-mannanase, endo-β-1,4-mannanase, β-mannanase B, 3-1, 4-mannan 4-mannanohydrolase, endo-3-mannanase, and β-mannanase. Preferred mannanases are members of the glycoside hydrolase family 26.

For the purposes of this disclosure, mannanase activity may be determined using a reducing endo-assay as described in the experimental section of WO2015040159.
Suitable examples from the classification EC 3.2.1.78 are described in WO2015040159, for example, the mature polypeptide SEQ ID NO: 2 described therein.

  Preferred mannanases are at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 60%, relative to the mature polypeptide SEQ ID NO: 22 from Ascobolus stitoideus. 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%, at least 99%, or 100% sequence identity.

  Preferred mannanases are 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 81%, relative to the mature polypeptide SEQ ID NO: 23 from Chaetomium virescens. 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%, at least 99%, or 100% sequence identity Is a mutant having

  Preferred mannanases are at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 75%, relative to the mature polypeptide SEQ ID NO: 24 from Preussia aemulans. 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%, at least 99%, or 100% sequence identity.

  Preferred mannanases are at least 65%, at least 66%, at least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 65%, relative to the mature polypeptide SEQ ID NO: 25 from Yunnania penicillata. 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, 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%, Kutomo 96%, at least 97%, at least 98%, a variant has at least 99%, or 100% sequence identity.

  Preferred mannanases are at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 75%, relative to the mature polypeptide SEQ ID NO: 26 from Myrothecium roridum. 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%, at least 99%, or 100% sequence identity.

  Preferably, the mannanase is an isolated mannanase.

  Preferably, the mannanase enzyme is present in the cleaning composition at 0.001-1% by weight, or 0.005-0.5% by weight, or 0.01-0.25%, based on the active protein in the composition. It is present in an amount of weight percent. Preferably, the mannanase enzyme is present in the aqueous laundry solution in an amount of 0.01 ppm to 1000 ppm of the mannanase enzyme, or in an amount of 0.05 ppm or 0.1 ppm to 750 ppm or 500 ppm.

Mannanase can also produce a biofilm breaking effect. Xanthan degrading enzyme The composition preferably comprises xanthan degrading enzyme. Xanthan gum is a polysaccharide secreted by the bacterium Xanthomonas campestris. Xanthan is composed of a pentasaccharide subunit, and a cellulose skeleton having a trisaccharide side chain composed of mannose- (β1,4) -glucuronic acid- (β1,2) -mannose is formed in the skeleton by α1,3 bonds. To form a cellulose skeleton alternately bonded to glucose residues. The cleaning composition preferably comprises a xanthan-degraded polypeptide having xanthan lyase activity and / or endo-β-1,4-glucanase activity. Xanthan lyase is an enzyme that cleaves the β-D-mannosyl α-β-D-1,4-glucuronosyl bond of xanthan, and is preferably xanthan lyase isolated from Paenibacillus alginoliticus XL-1. Preferred xanthanases are selected from glycosyl hydrolase family 5 (GH5).

Acetylglucosaminidase In a preferred composition, the composition comprises an acetylglucosaminidase enzyme, preferably E. coli. C. A β-N-acetylglucosaminidase enzyme from 3.2.1.52, preferably at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, relative to SEQ ID NO: 27; Alternatively, it may additionally comprise an enzyme having at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or at least or 100% identity.

Protease Preferably, the composition comprises one or more proteases. Suitable proteases include metalloproteases and serine proteases, including, for example, neutral or alkaline microbial serine proteases such as subtilisin (EC 3.4.21.62). Suitable proteases include those of animal, plant or microbial origin. In one aspect, such suitable proteases may be of microbial origin. Suitable proteases include chemically or genetically modified mutants of the aforementioned preferred proteases. In one aspect, a suitable protease may be a serine protease, such as an alkaline microbial protease or / and a trypsin-type protease. Examples of suitable neutral or alkaline proteases include:
(A) Subtilisin (EC 3.4.21.62), preferably, WO200407737, JP20105091989, JP2010509990, JP2015502439, JP2015143360, US Patent No. 6,312 , 936 (B1), 5,679,630, 4,760,025, 7,262,042 and WO 09/021867, German Patent Publication 102006022216 (A1). ), No. 102006022224 (A1), International Publication Nos. 2015009847, 2015089441, 20160166756, 2016166757, 20161699557, 201616069563, and 2016969569. Yes, B acillus sp. For example, B.I. lentus, B.L. alcoholophilus, B.A. subtilis, B .; amyloliquefaciens, B.A. pumilus and B. gibsoni and B.C. akibaii.
(B) trypsin, including the Fusarium protease described in WO 89/06270 and the chymotrypsin protease derived from Cellumonas described in 05/052161 and 05/052146; Trypsin-type or chymotrypsin-type proteases (porcine or bovine origin).
(C) metalloproteases, preferably Bacillus amyloliquefaciens described in WO07 / 044993A2, Bacillus, Brevibacillus, Thermomacromus, Thermobacillus, Thermobacillus, and Bacillus amyloliquefaciens described in WO07 / 044993A2. , Paenibacillus, Lysinibacillus or Streptomyces spp. , Krivella alluminosa described in WO2015193488, and Streptomyces and Lysobacter described in WO201675078.
(D) Bacillus sp. Described in WO 92/17577 (Novozymes A / S). TY145, a protease having at least 90% identity to a subtilase from NCIMB 40339, including variants of this Bacillus sp TY145 subtilase described in 20150247439 and 201606657.

  Preferred proteases include those derived from Bacillus gibsoni or Bacillus Lentus.

  Suitable commercially available protease enzymes include Alcalase (registered trademark), Savinase (registered trademark), Primase (registered trademark), Durazym (registered trademark), Polarzyme (registered trademark), and Kannase (registered trademark) according to Novozymes A / S (Denmark). (Registered trademark), Liquanase (registered trademark), Liquanase Ultra (registered trademark), Savinase Ultra (registered trademark), Ovozyme (registered trademark), Neutrase (registered trademark), Everlase (registered trademark), and Esperase (registered trademark), General Information Maxatase®, Maxacal®, Maxapem®, Properase® ), Purafect (registered trademark), Purafect Prime (registered trademark), Purafect Ox (registered trademark), FN3 (registered trademark), FN4 (registered trademark), Excellase (registered trademark), and Purafect OXP (registered trademark). What is sold, sold by Solvay Enzymes under the tradenames Opticlean® and Optimase®, available from Henkel / Kemira, ie, BLAP with mutations of S99D + S101R + S103A + V104I + G159S (US Pat. No. 5) , 352, 604, hereinafter referred to as BLAP), BLAP R (having S3T + V4I + V199M + V205I + L217D). BLAP), BLAP X (BLAP with S3T + V4I + V205I) and BLAP F49 (BLAP with S3T + V4I + A194P + V199M + V205I + L217D) (all from Henkel / Kemira), and KAP from Kao (mutations A230V + S9GusSusGusIusBlSusGusSusGusSil with a mutation from A230V + S9NusBlSusGusSusGusIusBlSusGusIusBlSusGusSusGusSusGusSusGusSusGusIusBlSusGusSusGusSusGusSusGusSusGusSusGusIusBusIusBusIusBusIusBusIusBusIusBlSusGusIusBusIusBlSusGusIus as well as KAP from Kao). Nos. 2009/149145, 2010/56653, 2010/56640, 2011/072117, U.S. Patent Publication No. 2011/0237487, International Publication No. 2011/140316, and 2012. / 151480, European Patent Nos. 2510092, 2566960 or Include those disclosed in JP 2705145.

Lipases Preferably, the composition comprises one or more comprising "first cycle lipase" such as those described in US Patent No. 6,939,702 (Bl) and US Patent Publication No. 2009/0217464. Lipase. A preferred lipase is a first washed lipase. In one embodiment of the invention, the composition comprises a first wash lipase. The first washed lipase comprises a lipase, a polypeptide having the following amino acid sequence: (a) having at least 90% identity to a wild-type lipase from Humicola lanuginosa strain DSM4109 ( b) comprising the substitution of a positively charged amino acid for an electrically neutral or negatively charged amino acid on the surface of the three-dimensional structure within 15A of E1 or Q249, compared to the wild-type lipase; And (c) those containing a peptide addition at the C-terminus and / or (d) those containing a peptide addition at the N-terminus and / or (e) those meeting the following restrictions: i) at position E210 of the wild-type lipase (Ii) including a negatively charged amino acid in the region corresponding to positions 90 to 101 of the wild-type lipase; and And (iii) contains a neutral or negative amino acid at a position corresponding to N94 of the wild-type lipase, and / or has a negative or neutral net charge at a region corresponding to positions 90 to 101 of the wild-type lipase. Having Preferred are variants of a wild-type lipase from Thermomyces lanuginosus that contain one or more of the T231R and N233R mutations. This wild-type sequence is 269 amino acids (amino acids 23 to 291) of Swissprot accession number Swiss-Prot O59952 (from Thermomyces lanuginosus (Humicola lanuginosa)). Preferred lipases include those sold under the trade names Lipex®, Lipolex®, and Lipoclean®. Other suitable lipases include those described in European Patent Application No. 12001034.3 or European Patent No. 2623586.

Endoglucanases Other preferred enzymes include endoglucanases derived from microorganisms that exhibit endo-β-1,4-glucanase activity (EC 3.2.1.4), and are described in US Pat. No. 403 (B2), wherein the microbial polypeptide is endogenous to a member of the genus Bacillus having at least 90%, 94%, 97%, and even 99% identity to the amino acid sequence of SEQ ID NO: 2 and Contains mixtures. Suitable endoglucanases are sold under the trade names Celluclean® and Whitezyme® (Novozymes A / S (Bagsvaerd, Denmark).

Pectate lyase Other preferred enzymes include Pectawash®, Pectaway®, pectate lyase sold as Xpect®, and Mannaway® (all Novozymes A). / S (Bagsvaerd, Denmark)) and Mannanase sold as Purabrite (registered trademark) (Genencor International Inc. (Palo Alto, California)).

Surfactant system The cleaning composition may include a surfactant system. The cleaning composition comprises from about 1% to about 80%, or from 1% to about 60%, preferably from about 5% to about 50%, more preferably from about 8% to about 60% by weight of the cleaning composition. It may contain 40% by weight of the surfactant system.

  Surfactants suitable for use in the surfactant system may be derived from natural and / or renewable resources.

  The surfactant system may include an anionic surfactant, more preferably an anionic surfactant selected from the group consisting of alkyl benzene sulfonates, alkyl sulfates, alkyl alkoxy sulfates. Alkyl ethoxy sulfates, paraffin sulfonates, and mixtures thereof may be preferred, but alkyl benzene sulfonates are particularly preferred. The surfactant system may further include a surfactant selected from the group consisting of a nonionic surfactant, a cationic surfactant, an amphoteric surfactant, a zwitterionic surfactant, and mixtures thereof. The surfactant system preferably comprises a nonionic surfactant, for example, an ethoxylated nonionic surfactant. The surfactant system may include an amphoteric surfactant, for example, an amine oxide surfactant such as an alkyl dimethyl amine oxide. The surfactant system may include a zwitterionic surfactant such as betaine.

  The most preferred surfactant system for the detergent compositions of the present invention comprises from about 1% to about 40%, preferably from about 6% to 35%, more preferably from about 8% to about 30% by weight of the total composition. % By weight of an anionic surfactant, preferably alkyl benzene sulphonate. Preferred surfactant systems optionally include, in addition, an alkyl alkoxy sulfate surfactant, more preferably an alkyl ethoxy sulfate, optionally from 0.5% to 15% by weight of the composition. , Preferably 1% to 12%, more preferably 2% to 10% by weight of amphoteric and / or amphoteric surfactants, more preferably amphoteric, even more preferably amine oxide surfactants, especially It may be contained in combination with alkyldimethylamine oxide.

  Most preferably, the surfactant system comprises an anionic surfactant and a nonionic surfactant, and preferably, the weight ratio of anionic surfactant to nonionic surfactant is from 25: 1 to 1: 2.

Anionic surfactant The anionic surfactant may be in salt or acid form and is typically water-soluble sodium, potassium, ammonium, magnesium or mono-, di- or tri-C2-C3 alkanolammonium. It may be in the form of a salt, and the sodium cation is the usual one chosen.

Sulfonate Surfactants Suitable anionic sulfonate surfactants for use herein include water-soluble salts of C8-C18 alkyl or hydroxyalkyl sulfonates, C11-C18 alkyl benzene sulfonates (LAS), WO 99/05243. No. 99/05242, No. 99/05244, No. 99/05082, No. 99/05084, No. 99/05241, No. 99/07656, No. 00/23549 And modified alkylbenzene sulfonates (MLAS), methyl ester sulfonates (MES), and α-olefin sulfonates (AOS) described in WO 00/23548. These also include paraffin sulfonates, which can be monosulfonates and / or disulfonates, obtained by sulfonating paraffins of 10 to 20 carbon atoms. Sulfonate surfactants may also include alkyl glyceryl sulfonate surfactants.

Sulphated anionic surfactant Preferably, the sulphated anionic surfactant is alkoxylated, more preferably from about 0.2 to about 4, even more preferably from about 0.3 to about 3, more preferably More preferred are alkoxylated branched sulphated anionic surfactants having a degree of alkoxylation of about 0.4 to about 1.5, especially about 0.4 to about 1. Preferably, the alkoxy group is ethoxy. When the sulphated anionic surfactant is a mixture of sulphated anionic surfactants, the degree of alkoxylation is the weight average degree of alkoxylation of all components of the mixture (weight average degree of alkoxylation). The calculation of the weight average degree of alkoxylation must also include the weight of the sulfated anionic surfactant component having no alkoxylated groups.

Weight average degree of alkoxylation = (x1 ^* degree of alkoxylation of surfactant 1 + x2 ^* degree of alkoxylation of surfactant 2 + ...) / (x1 + x2 + ...)
[Where x1, x2,. . . Is the weight in grams of each sulphated anionic surfactant in the mixture, and the degree of alkoxylation is the number of alkoxy groups on each sulphated anionic surfactant].

  Preferably, the branching group is an alkyl. Typically, the alkyl is selected from methyl, ethyl, propyl, butyl, pentyl, cyclic alkyl groups and mixtures thereof. One or more alkyl branches may be present in the hydrocarbyl backbone of the starting alcohol used to make the sulfated anionic surfactant used in the detergents of the present invention. Most preferably, the branched sulfated anionic surfactant is selected from alkyl sulfates, alkyl ethoxy sulfates, and mixtures thereof.

  The branched sulphated anionic surfactant may be a single anionic surfactant or a mixture of anionic surfactants. In the case of a single surfactant, the percentage of branching refers to the weight percentage of hydrocarbyl chains that are branched in the alcohol from which the surfactant is derived.

In the case of surfactant mixtures, the percentage of branches is weight average and has the following formula:
Weight average of branches (%) = [(x1 ^* weight% of branched alcohol 1 in alcohol 1 + x2 ^* weight% of branched alcohol 2 in alcohol 2 + ...) / (x1 + x2 + ... ..]] ^* 100
[Where x1, x2,. . . Is the weight in grams of each alcohol in the total alcohol mixture of alcohols used as starting materials for the anionic surfactants of the detergents of the present invention. The calculation of the weight average degree of branching must also include the weight of the anionic surfactant component without branching groups.

  Sulfate surfactants suitable for use herein include water soluble salts of C8-C18 alkyl or hydroxyalkyl, sulfate and / or ether sulfates. Suitable counterions include alkali metal cations or ammonium or substituted ammonium, with sodium being preferred.

  Sulfate surfactants include C8-C18 primary branched and random alkyl sulfates (AS), C8-C18 secondary (2,3) alkyl sulfates, C8-C18 alkyl alkoxy sulfates (AExS) ( Wherein x is preferably from 1 to 30, and the alkoxy group can be selected from ethoxy, propoxy, butoxy, or even higher alkoxy groups, and mixtures thereof.

  Alkyl sulfates and alkyl alkoxy sulfates are commercially available in various chain lengths, degrees of ethoxylation and degree of branching. Commercially available sulfates include Neodol alcohol from Shell company, Lial-Isalcheml and Safol from Sasol company, and those based on natural alcohol from Procter & Gamble Chemicals company.

  Preferred alkyl sulfates are those in which the anionic surfactant has a degree of ethoxylation of about 0.2 to about 3, more preferably about 0.3 to about 2, even more preferably about 0.4 to about 1.5, especially , About 0.4 to about 1 alkyl ethoxy sulfate. These are also preferred anionic surfactants having a degree of branching of about 5% to about 40%, even more preferably about 10% to 35%, especially about 20% to 30%.

Nonionic surfactant Preferably, the surfactant system comprises from 0.1% to 40%, preferably from 0.2% to 20%, most preferably from 0.5% to 10% by weight of the composition. % Nonionic surfactant. Suitable nonionic surfactants include the condensation products of aliphatic alcohols with 1 to 25 moles of ethylene oxide. The alkyl chain of the aliphatic alcohol may be either linear or branched, primary or secondary, and generally may contain from 8 to 22 carbon atoms . Particularly preferred are alcohols having alkyl groups containing 10 to 18 carbon atoms, preferably 10 to 15 carbon atoms, and 2 to 18 moles, preferably 2 to 15 moles, more preferably 2 moles per mole of alcohol. Are condensation products with 5 to 12 moles of ethylene oxide. Highly preferred nonionic surfactants are the condensation products of Guerbet alcohol with 2 to 18, preferably 2 to 15 and more preferably 5 to 12 moles of ethylene oxide per mole of alcohol.

  Other nonionic surfactants suitable for use herein include fatty alcohol polyglycol ethers, alkyl polyglucosides, and fatty acid glucamide.

Amphoteric surfactant The surfactant system can include an amphoteric surfactant such as an amine oxide. Preferred amine oxides are alkyldimethylamine oxides or alkylamidopropyldimethylamine oxides, more preferably alkyldimethylamine oxides, especially cocodimethylamine oxide. The amine oxide can have a straight or medium chain branched alkyl moiety. Typical linear amine oxides contain one C1-18 alkyl moiety of R1 and two R2 and R3 moieties selected from the group consisting of C1-3 alkyl groups and C1-3 hydroxyalkyl groups. Water-soluble amine oxides. Preferably, the amine oxide is of the formula R1-N (R2) (R3) O wherein R1 is C8-18 alkyl and R2 and R3 are methyl, ethyl, propyl, isopropyl, 2-hydroxyethyl, -Hydroxypropyl and 3-hydroxypropyl]. Examples of the linear amine oxy-based surfactant include linear C10 to C18 alkyldimethylamine oxide and linear C8 to C12 alkoxyethyldihydroxyethylamine oxide. Preferred amine oxides include linear C10, linear C10-C12, and linear C12-C14 alkyl dimethylamine oxide. As used herein, "mid-branched" means that the amine oxide has one alkyl moiety having n1 carbon atoms and one alkyl moiety in the alkyl moiety. It means that the branch has n2 carbon atoms. The alkyl branch is located on the alpha carbon of the nitrogen of the alkyl moiety. This type of branching in the amine oxide is also known in the art as an internal amine oxide. The sum of n1 and n2 is 10 to 24 carbon atoms, preferably 12 to 20, more preferably 10 to 16 carbon atoms. The number of carbon atoms in one alkyl moiety (n1) must be approximately the same as the number of carbon atoms in one alkyl branch (n2) so that one alkyl moiety and one alkyl branch are symmetric. . As used herein, "symmetric" refers to | n1- at at least 50%, more preferably at least 75% to 100%, by weight of the medium-chain branched amine oxide used herein. n2 | is 5 or less, preferably 4, most preferably 0 to 4 carbon atoms.

  The amine oxide may further comprise two moieties independently selected from a C1-3 alkyl, a C1-3 hydroxyalkyl group, or a polyethylene oxide group containing on average about 1 to about 3 ethylene oxide groups. Good. Preferably, the two moieties are selected from C1-3 alkyl, more preferably both are selected as C1 alkyl.

Zwitterionic surfactants Other suitable surfactants include betaines such as alkyl betaines, alkyl amide betaines, amidazolinium betaines, sulfobetaines (INCI sultaines) and phosphobetaines, preferably of the formula (I):
^{_{R 1 - [CO-X (}} CH 2) n] x -N + (R 2) (R 3) - (CH 2) m - [CH (OH) -CH 2] y -Y- (I)
[Where,
R ¹ is a saturated or unsaturated C6-22 alkyl residue, preferably a C8-18 alkyl residue, especially a saturated C10-16 alkyl residue, for example a saturated C12-14 alkyl residue;
X is, NH, is ^NR 4, O or S with C1~4 alkyl residues ^{R 4,}
n is a number from 1 to 10, preferably 2 to 5, especially 3,
x is 0 or 1, preferably 1,
R ² and R ³ are independently a C1-4 alkyl residue which may be hydroxy-substituted such as hydroxyethyl, preferably methyl;
m is a number from 1 to 4, especially 1, 2 or 3;
y is 0 or 1;
Y is COO, SO 3, OPO (OR ⁵ ) O or P (O) (OR ⁵ ) O, wherein R ⁵ is a hydrogen atom H or a C 1-4 alkyl residue.

Preferred betaines are alkyl betaines of formula (Ia), alkylamidopropyl betaines of formula (Ib), sulfobetaines of formula (Ic), and amide sulfobetaines of formula (Id);
R ¹ -N ⁺ (CH ₃ ) ₂ —CH ₂ COO ⁻ (Ia)
R ¹ —CO—NH (CH ₂ ) ₃ —N ⁺ (CH ₃ ) ₂ —CH ₂ COO ⁻ (Ib)
R ¹ -N ⁺ (CH ₃ ) ₂ —CH ₂ CH (OH) CH ₂ SO ₃ − (Ic)
_{^{R 1 -CO-NH- (CH 2}} ) 3 -N + (CH 3) 2 -CH 2 CH (OH) CH 2 SO 3 - (Id) [ wherein, ^{R 1} 1 is the same meaning as in formula I There is]. A particularly preferred betaine is carbobetaine [wherein Y ⁻ = COO ⁻ ], especially carbobetaines of formulas (Ia) and (Ib), with alkylamide betaines of formula (Ib) being more preferred.

  Examples of suitable betaines and sulfobetaines are almondamidopropyl betaine, apricotamidopropyl betaine, avocadoamidopropyl betaine, babasamidopropyl betaine, behenamidopropyl betaine, behenylbetaine, betaine, canolamidpropyl betaine, capryl / capramide Propyl betaine, carnitine, cetyl betaine, cocamidoethyl betaine, cocamidopropyl betaine, cocamidopropyl hydroxysultaine, cocobetaine, cocohydroxysultaine, coco / oleamidopropyl betaine, cocosultaine, decylbetaine, dihydroxyethyl oleyl glycinate , Dihydroxyethyl soybean glycinate, dihydroxyethyl stearyl glycinate, dihydroxyethyl tallow gly PG-betaine propyl dimethicone, erucamidopropyl hydroxysultaine, hydrogenated tallow betaine, isostearamidopropyl betaine, lauramidopropyl betaine, lauryl betaine, lauryl hydroxysultaine, lauryl sultaine, milkamidopropyl betaine, Minkamidopropyl betaine, myristamidopropyl betaine, myristyl betaine, oleamidopropyl betaine, oleamidopropyl hydroxysultaine, oleyl betaine, oliveamidopropyl betaine, cocoamidopropyl betaine, palmitamidopropyl betaine, palmitoyl carnitine, coconut amide Propyl betaine, polytetrafluoroethylene acetoxypropyl betaine, ricinoleamide propyl betaine , Sesamidopropyl betaine, soyamidopropyl betaine, stearamidopropyl betaine, stearyl betaine, tallowamidopropyl betaine, tallowamidopropyl hydroxysultaine, tallow betaine, talodihydroxyethyl betaine, undecylenamidopropyl betaine, and wheat germ amidopropyl Betaine [expressed according to INCI]. For example, a preferred betaine is cocoamidopropyl betaine.

Fatty acids, especially when in liquid form, preferably the detergent composition comprises from 1.5% to 20%, more preferably from 2% to 15%, even more preferably from 3% to 10% by weight of the liquid detergent composition. %, Most preferably 4% to 8% by weight of a soap, preferably a fatty acid salt, more preferably an amine neutralized fatty acid salt, preferably the amine is an alkanolamine, more preferably It is selected from ethanolamine, diethanolamine, triethanolamine, or a mixture thereof, and is more preferably monoethanolamine.

Perfume Preferred compositions of the present invention include a perfume. Typically, the composition comprises a fragrance comprising one or more fragrance ingredients selected from the group as described in WO 08/87497. However, any fragrance useful in detergents may be used. The preferred method of incorporating perfume into the compositions of the present invention is via encapsulated perfume particles containing a water-soluble hydroxy compound or either melamine-formaldehyde or modified polyvinyl alcohol. In one aspect, the encapsulant comprises: (a) at least a partially water-soluble solid matrix comprising one or more water-soluble hydroxy compounds, preferably starch, and (b) a perfume oil encapsulated by the solid matrix. Including. In a further aspect, the fragrance may be pre-complexed with a polyamine, preferably polyethyleneimine, to form a Schiff base.

Polymer The detergent composition may include one or more polymers, for example, for cleaning and / or care. Examples are optionally modified carboxymethylcellulose, poly (ethylene glycol), poly (vinyl alcohol), polycarboxylates such as polyacrylates, maleic / acrylic acid copolymers and lauryl methacrylate / acrylic acid copolymers and carboxylate polymers It is.

  Suitable carboxylate polymers include maleate / acrylate random copolymers or polyacrylate homopolymers. The carboxylate polymer may be a polyacrylate homopolymer having a molecular weight of 4,000 to 9,000 Da or 6,000 to 9,000 Da. Another suitable carboxylate polymer is a copolymer of maleic acid and acrylic acid, which may have a molecular weight ranging from 4,000 Da to 90,000 Da.

  Other suitable carboxylate polymers include (i) structural units derived from 50% to less than 98% by weight of one or more monomers, including carboxyl groups, and (ii) one or more monomers, including a sulfonate moiety. From 1% to less than 49% by weight of structural units derived from: and (iii) formulas (I) and (II):

［式（Ｉ）中、Ｒ_０は、水素原子又はＣＨ_３基を表し、Ｒは、ＣＨ_２基、ＣＨ_２ＣＨ_２基又は単結合を表し、Ｘは、０〜５の数を表し、ただし、Ｒが単結合である場合、Ｘは１〜５の数を表し、Ｒ_１は、水素原子又はＣ_１〜Ｃ_２０有機基である］、

[In the formula (I), R ₀ represents a hydrogen atom or a CH ₃ group, R represents a CH ₂ group, a CH ₂ CH ₂ group or a single bond, and X represents a number of 0 to 5, provided that , R is a single bond, X represents a number of 1 to 5, and R ₁ is a hydrogen atom or a C ₁ -C ₂₀ organic group],

［式（ＩＩ）中、Ｒ_０は、水素原子又はＣＨ_３基を表し、Ｒは、ＣＨ_２基、ＣＨ_２ＣＨ_２基又は単結合を表し、Ｘは、０〜５の数を表し、Ｒ_１は、水素原子又はＣ_１〜Ｃ_２０有機基である］により表されるエーテル結合含有モノマーから選択される１つ以上のモノマーから誘導される１重量％〜４９重量％の構造単位と、を含む、コポリマーである。

[In the formula (II), R ₀ represents a hydrogen atom or a CH ₃ group, R represents a CH ₂ group, a CH ₂ CH ₂ group or a single bond, X represents a number of 0 to 5, R ₁ is a hydrogen atom or a C ₁ -C ₂₀ organic group], and 1% to 49% by weight of a structural unit derived from one or more monomers selected from ether bond-containing monomers represented by And copolymers.

The composition has the following general structure: bis _{((C 2 H 5 O)} (C 2 H 4 O) n) (CH 3) -N + -C x H 2x -N + - (CH 3) - bis _{((C 2 H 5 O)} (C 2 H 4 O) n) [ wherein, a n = 20 to 30, x = 3 to 8] compound having, or a sulphated or sulphonated variants And one or more amphiphilic cleaning polymers. In one aspect, the polymer is sulphated or sulphonated to obtain a zwitter soil suspended polymer.

  The composition preferably includes an amphiphilic alkoxylated grease cleaning polymer that is balanced in hydrophilicity and properties to remove grease particles from fabrics and surfaces. Preferred amphiphilic alkoxylated grease cleaning polymers comprise a core structure and a plurality of alkoxylate groups attached to the core structure. These may preferably include alkoxylated polyalkyleneimines having an inner polyethylene oxide block and an outer polypropylene oxide block. Typically, they can be incorporated into the compositions of the invention in amounts of 0.005 to 10% by weight, generally 0.5 to 8% by weight.

Alkoxylated polycarboxylates, such as those prepared from polyacrylates, are useful herein to provide additional grease removal performance. Such materials are described in WO 91/08281 and WO 90/01815. Chemically, these materials include polyacrylates having one ethoxy side chain for every 7-8 acrylate units. The side chains have the formula _{- (CH 2 CH 2 O)} m (CH 2) n CH 3 [ wherein, m is 2 to 3, n is 6 to 12] are of. The side chains are esterified to a polyacrylate "backbone" to provide a "comb" polymer type structure. Molecular weights can vary, but typically range from about 2000 to about 50,000. Such alkoxylated polycarboxylates can comprise from about 0.05% to about 10% by weight of the compositions herein.

  The present compositions may include polyethylene glycol polymers, which may be particularly preferred in compositions that include a mixed surfactant system. Suitable polyethylene glycol polymers include (i) a hydrophilic backbone comprising polyethylene glycol, and (ii) C4-C25 alkyl groups, polypropylene, polybutylene, vinyl esters of saturated C1-C6 monocarboxylic acids, acrylic acid or methacrylic acid. Random graft copolymers comprising side chains selected from the group consisting of C1-C6 alkyl esters, and mixtures thereof. Suitable polyethylene glycol polymers have a polyethylene glycol backbone with randomly grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone can range from 2,000 Da to 20,000 Da, or 4,000 Da to 8,000 Da. The molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can range from 1: 1 to 1: 5 or 1: 1.2 to 1: 2. The average number of graft sites per ethylene oxide unit may be less than 1, or less than 0.8, and the average number of graft sites per ethylene oxide unit may range from 0.5 to 0.9. Or the average number of graft sites per ethylene oxide unit may range from 0.1 to 0.5, or 0.2 to 0.4. A preferred polyethylene glycol polymer is Sokalan HP22.

  Typically, these polymers, when present, are each incorporated into the compositions of the present invention in an amount of 0.005 to 10% by weight, more typically 0.05 to 8% by weight.

  Preferably, the composition comprises one or more carboxylate polymers, such as a maleate / acrylate random copolymer or a polyacrylate homopolymer. In one aspect, the carboxylate polymer is a polyacrylate homopolymer having a molecular weight of 4,000 Da to 9,000 Da or 6,000 Da to 9,000 Da. Typically, they are incorporated into the compositions of the present invention in amounts of 0.005 to 10% or 0.05 to 8% by weight.

  Preferably, the compositions of the present invention include one or more soil release polymers.

  Suitable soil release polymers are polyester soil release polymers such as Repel-o-tex polymers (eg, Repel-o-tex SF, SF-2 and SRP6 supplied by Rhodia). Other suitable soil release polymers include Texcare polymers, including Texcare SRA100, SRA300, SRN100, SRN170, SRN240, SRN260, SRN300 and SRN325 supplied by Clariant. Other suitable soil release polymers are Marloquest polymers such as Marloquest SL supplied by Sasol.

  Preferably, the composition comprises one or more cellulosic polymers, including those selected from alkyl cellulose, alkyl alkoxyalkyl cellulose, carboxyalkyl cellulose, alkyl carboxyalkyl cellulose. Preferred cellulosic polymers are selected from the group comprising carboxymethylcellulose, methylcellulose, methylhydroxyethylcellulose, methylcarboxymethylcellulose, and mixtures thereof. In one aspect, the carboxymethyl cellulose has a degree of carboxymethyl substitution of 0.5 to 0.9 and a molecular weight of 100,000 Da to 300,000 Da.

  The composition preferably comprises a cation-modified polysaccharide polymer. Preferably, the cationic polysaccharide polymer is selected from cationically modified hydroxyethylcellulose, cationically modified hydroxypropylcellulose, cationically hydrophobically modified hydroxyethylcellulose, cationically hydrophobically modified hydroxypropylcellulose, or a mixture thereof, more preferably, cationically modified hydroxyethylcellulose, It is selected from cationic hydrophobically modified hydroxyethyl cellulose or mixtures thereof.

Amine The cleaning compositions described herein may include an amine. The cleaning composition comprises about 0.1% to about 10%, about 0.2% to about 5%, about 0.5% to about 4%, about 0.1% by weight of the composition. From about 4% to about 4%, or from about 0.1% to about 2% by weight of the amine. The amine can be subjected to protonation depending on the pH of the washing medium in which it is used. Non-limiting examples of amines include, but are not limited to, ether amines, cyclic amines, polyamines, oligoamines (eg, triamine, diamine, pentaamine, tetraamine), or combinations thereof. The compositions described herein may include an amine selected from the group consisting of oligoamines, ether amines, cyclic amines, and combinations thereof. In some aspects, the amine is not an alkanolamine. In some aspects, the amine is not a polyalkyleneimine. Examples of suitable oligoamines include tetraethylenepentamine, triethylenetetraamine, diethylenetriamine, and mixtures thereof. Etheramines and cyclic amines may be particularly preferred.

Fabric Shading Dye The composition may include a fabric shading agent. Suitable fabric shading agents include dyes, dye-clay complexes, and pigments. Suitable dyes include small molecule dyes and polymer dyes. Suitable small molecule dyes include Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or a color index (CI) classification of a mixture thereof. And small molecule dyes selected from the group consisting of dyes classified as Preferred dyes include alkoxylated azothiophene, Solvent Violet 13, Acid Violet 50 and Direct Violet 9. Particularly preferred dyes are polymeric dyes, especially those containing polyalkoxy groups, most preferably polyethoxy groups, for example,

［式中、指数ｘ及びｙは、独立して、１〜１０から選択される］である。

Wherein the indices x and y are independently selected from 1 to 10.

Migration Inhibitors Suitable migration inhibitors include polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone, polyvinyloxazolidone, polyvinylimidazole, and mixtures thereof. Preferred are poly (vinylpyrrolidone), poly (vinylpyridine betaine), poly (vinylpyridine N-oxide), poly (vinylpyrrolidone-vinylimidazole), and mixtures thereof. Suitable commercially available migration inhibitors include PVP-K15 and K30 (Ashland), Sokalan® HP165, HP50, HP53, HP59, HP56K, HP56, HP66 (BASF), Chromabond® S-400. , S403E, and S-100 (Ashland).

Chelating agent The composition may include, for example, a chelating agent selected from a phosphonic acid chelating agent, a sulfonic acid chelating agent, a succinic acid chelating agent and an acetic acid chelating agent, or a mixture thereof. Suitable examples include HEDP, DTPA, EDTA, MGDA, GLDA, EDDS, and 4,5-dihydroxy-1,3-benzenedisulfonic acid and salts thereof.

The present disclosure relates to a method of making the compositions described herein. The compositions of the present invention may be in solid (eg, granules or tablets) or liquid form. It may be preferred that the composition is in a liquid form. The composition may be manufactured by any process selected by the formulator, including a batch process, a continuous loop process, or a combination thereof.

When in liquid form, the composition of the invention may be aqueous (typically more than 2% by weight, or even 5 or 10% by weight total water content, up to 90 or up to 80% by weight or 70% by weight). % By weight) or non-aqueous (typically less than 2% by weight total water content). Typically, the compositions of the present invention will be in the form of an aqueous solution or homogeneous dispersion or suspension of the optical brightener, DTI, and optionally further additive materials, and some of these components May be in the form of a normal solid, and may contain the usual liquid components of the composition of the present invention (such as alcohol ethoxylate nonionic liquid, aqueous liquid carrier, and any other optional components of the usual liquid). It is a combined component. Such a solution, dispersion or suspension has acceptable phase stability. When in the form of a liquid, detergent of the present invention, preferably, 1 to 1500 centipoise at 20s-1 and 21 ℃ (1~1500mPa ^* s), more preferably 100 to 1000 centipoises (100~1000mPa ^* s), Most preferably it has a viscosity of 200-500 centipoise (200-500 mPa ^* s). The viscosity can be measured by a conventional method. Viscosity may be measured using an AR550 rheometer from TA instruments using a plate steel spindle with a diameter of 40 mm and a gap size of 500 μm. A high shear viscosity at 20 s-1 and a low shear viscosity at 0.05-1 can be obtained from a log shear rate sweep from 0.1-1 to 25-1 at 21C for 3 minutes. The preferred rheology described herein can be obtained by using an internal structurant with a detergent component or by using an external rheology modifier. More preferably, the detergent, such as a detergent liquid composition, has a high shear rate viscosity of about 100 centipoise to 1500 centipoise, more preferably 100 to 1000 cps. Unit dose detergents, such as detergent liquid compositions, have a high shear rate viscosity of 400-1000 cps. Detergents, such as laundry softening compositions, typically have a high shear rate viscosity of 10-1000, more preferably 10-800 cps, most preferably 10-500 cps. The dishwashing composition has a high shear rate viscosity of 300 to 4000 cps, more preferably 300 to 1000 cps.

  The cleaning and / or treatment composition in liquid form herein can be combined with the components in any convenient order and the resulting combination of components can be mixed, eg, stirred, to produce a phase stable liquid detergent composition. Can be prepared by forming In the process of preparing such compositions, at least a majority, or even substantially all, of the liquid components, such as, for example, nonionic surfactants, non-surfactant liquid carriers, and other optional liquid components, are included. A containing liquid matrix is formed and the liquid components are well mixed by applying shear agitation to the liquid combination. For example, high speed stirring with a mechanical stirrer can usually be used. While maintaining shear agitation, substantially all of the optional anionic surfactant and components in solid form can be added. Stirring of the mixture may be continued, if necessary, increased at that point, to form a solution or homogeneous dispersion of the insoluble solid particles in the liquid phase. After some or all of the solid form material has been added to the stirred mixture, particles of any enzymatic material to be included, such as enzyme granules, are incorporated. As a variation on the composition preparation procedure described above, one or more of the solid components may be added to the stirred mixture as a solution or slurry of particles pre-mixed with one or more minor portions of the liquid component. After all of the composition components have been added, stirring of the mixture is continued for a time sufficient to form a composition having the required viscosity and phase stability properties. In many cases, this involves stirring for about 30 to 60 minutes.

  The additive components in the compositions of the present invention, with or without an intermediate purification step, can be incorporated into the compositions as synthetic products that produce such components. If no purification step is present, the mixture used will generally be the desired component or mixture thereof (the proportions given herein relate to the weight percent of the components themselves, unless otherwise specified), It contains unreacted starting materials and impurities formed by side reactions and / or incomplete reactions. For example, for ethoxylated or substituted components, the mixture may contain different degrees of ethoxylation / substitution.

Methods of Use The present disclosure relates to methods for cleaning surfaces such as textile products using the cleaning compositions of the present disclosure. Generally, the method comprises, in a washing step, mixing the cleaning composition described herein with water to form an aqueous liquid, and contacting the aqueous liquid with a surface, preferably a textile product. The target surface may include oily or body soil.

  The present invention also provides an amylase enzyme for enhancing stain removal, preferably oily stain removal from a surface, preferably a textile surface, or body soil removal, and / or for classifying reduced odor, and an endo- an enzyme having glycoside hydrolase activity, which belongs to the enzyme of α-1,4-polygalactosaminidase (EC 3.2.1.109). Preferably, the glycoside hydrolase enzyme has at least 60%, or 65%, or 70%, or 75%, or 80%, or 85%, or 90%, or 95%, up to 100% relative to SEQ ID NO: 1. Mutants having the same identity.

  The compositions of the present invention, typically prepared as described above, can be used to form aqueous (washing / treating) liquors for use in washing / treating fabrics and / or hard surfaces. Generally, an effective amount of such a composition is added to water, for example, in a conventional automatic fabric washer, to form such an aqueous liquid. The aqueous liquid thus formed is then brought into contact, typically under stirring, with the fabric to be washed / treated. An effective amount of a detergent composition herein that is added to water to form an aqueous liquid is an amount sufficient to form about 500 to 25,000 ppm or 500 to 15,000 ppm of the composition in the aqueous liquid. About 1,000 to 3,000 ppm of the detergent composition herein, which may be included, is provided in the aqueous liquid.

  Typically, to form an aqueous liquid, the concentration of the anionic surfactant in the cleaning liquid is more than 0.1 g / L to 5 g / L, or 1 g / L or more and 4.5 g / L or less. 0 g / L or less, or 3.5 g / L or less, or 3.0 g / L or less, or 2.5 g / L or less, or even 2.0 g / L or less, or even 1.5 g / L or less. By contacting the cleaning composition in such an amount with the cleaning water. The method of washing the fabric or woven product may be performed in a top-loading or front-loading automatic washing machine, or may be used for hand-washing laundry applications. In these applications, the formed aqueous liquid and the concentration of the cleaning composition in the cleaning liquid will be that of the main cleaning cycle. When determining the volume of the aqueous liquid does not include any water input during any optional rinsing steps.

  The aqueous liquid may contain up to 40 L of water, or up to 30 L, or up to 20 L, or up to 10 L, or up to 8 L, or even up to 6 L of water. The aqueous liquid may contain more than 0 L to 15 L, or 2 to 12 L, or even 8 L or less of water. Typically, 0.01 kg to 2 kg of fabric per liter of aqueous liquid is charged to the aqueous liquid. Typically, 0.01 kg or more per liter of aqueous liquid, or 0.05 kg or more, or 0.07 kg or more, or 0.10 kg or more, or 0.15 kg or more, or 0.20 kg or more, or 0.25 kg or more The fabric is poured into the aqueous liquid. Optionally, contacting no more than 50 g, or no more than 45 g, or no more than 40 g, or no more than 35 g, or no more than 30 g, or no more than 25 g, or even no more than 15 g, or even no more than 10 g of the composition to water. To form an aqueous liquid. Such compositions are typically used at a concentration of about 500 ppm to about 15,000 ppm in the solution. The water temperature is typically in the range of about 5 ° C. to about 90 ° C., for example 20 ° C. to 60 ° C., preferably up to 40 ° C. or 30 ° C., and when washing the fabric, the ratio of water to fabric is: Typically from about 1: 1 to about 30: 1. Typically, the aqueous liquid containing the cleaning composition of the present invention has a pH of 3 to 11.5, typically 7 to 11, more usually 8 to 10.5.

  In one aspect, the method optionally comprises washing and / or rinsing the surface or fabric; contacting the surface or fabric with any of the compositions disclosed herein; Washing and / or rinsing the surface or fabric, and optionally drying.

  Drying of such surfaces or fabrics, whether mechanical or outdoor, can be performed by any one of the common means used in either domestic or industrial settings. . The fabric may include any fabric that can be laundered under general consumer or commercial conditions, and the present invention is particularly suitable for synthetic textile products such as polyester and nylon, especially synthetic and cellulose. It is suitable for treating mixed fabrics and / or fibers containing system fabrics and / or fibers. Examples of synthetic fabrics are polyester, nylon, which can be present in blended fabrics with cellulosic fibers, such as polycotton fabrics.

  The following are illustrative examples of cleaning compositions according to the present disclosure and are not intended to be limiting.

Examples 1-18: unit dose compositions.
These examples provide various formulations for unit dose laundry detergents and include dual compartment unit dose products, including one powder compartment and one liquid compartment. The film used to encapsulate the composition is PVA. Each example is prepared by combining a liquid compartment composition selected from compositions AE with a powder compartment composition selected from compositions FK.

  Based on cleaning and / or treatment composition / compartment weight. Enzyme concentrations are reported as raw materials.

Examples 19 to 24
Granular laundry detergent compositions for hand washing or washing machines, typically for top-loading washing machines.

Examples 25 to 30
Typically, a granular laundry detergent composition for a front-loading automatic washing machine.

  Examples 31-37: Strong liquid laundry detergent compositions.

  Based on the total weight of the cleaning and / or treatment composition. Unless otherwise stated, enzyme concentrations are reported as raw materials.

AE1.8S an average ethoxylation degree of _{C 12 to 15} alkyl ethoxysulfate 1.8.
AE3S is an average ethoxylation degree of _{C 12 to 15} alkyl ethoxysulfate 3.0.
AE7 is an average ethoxylation degree of _{C 12 to 13} alcohol ethoxylate 7.
AE8 is a _C12-13 alcohol ethoxylate with an average degree of ethoxylation of 8.
AE9 an average ethoxylation degree of _{C 12 to 13} alcohol ethoxylate 9.
Alkoxylated polyaryl / polyalkylphenols are alkoxylated polyaryl / polyalkylphenols such as Emulsogen® TS160, Hostapal®
BV conc. , Sapogenat (R) T110 or Sapogenat (R) T139, all available from Clariant.
Amylase 1 is Stainzyme® (15 mg activity / g).
Amylase 2 is Natalase® (29 mg activity / g).
Amylase 3 is Stainzyme Plus® (20 mg activity / g).
AS is a _C12-14 alkyl sulfate.
Cellulase 2 is Celluclean® (15.6 mg activity / g).
Xyloglucanase is Whitezyme® (20 mg activity / g).
Chelating agent 1 is diethylenetriaminepentaacetic acid.
Chelating agent 2 is 1-hydroxyethane 1,1-diphosphonic acid.
The chelating agent 3 is ethylenediamine-N, N′-disuccinic acid, a sodium salt of the (S, S) isomer (EDDS).
Dispersin B is a glycoside hydrolase (reported as 1000 mg activity / g).
DTI1 is poly (4-vinylpyridine-1-oxide) (Chromabond S-403E®).
DTI2 is poly (1-vinylpyrrolidone-co-1-vinylimidazole) (such as Sokalan HP56®).
Dye control agents are, for example, Superex® O.D. IN (M1), Nylofix (registered trademark) P (M2), Nylofixan (registered trademark) PM (M3), or Nylofixan (registered trademark) HF (M4).
HSAS is a medium chain branched alkyl sulfate disclosed in U.S. Patent Nos. 6,020,303 and 6,060,443.
LAS _is a linear alkylbenzene sulfonate having an average aliphatic carbon chain length of _C 9 ~C ₁₅ (HLAS is an acid form).
Lipase is Lipex® (18 mg activity / g).
Mannanase is Mannaway® (25 mg activity / g).
The nuclease is the phosphodiesterase of SEQ ID NO: 2-6, preferably any of SEQ ID NO: 2, 3, or 4, which has been reported as an active protein.
Optical brightener 1 is disodium 4,4'-bis {[4-anilino-6-morpholino-s-triazin-2-yl] -amino} -2, -2'-stilbene disulfonate.
Optical brightener 2 is disodium 4,4'-bis- (2-sulfostyryl) biphenyl (sodium salt).
Optical brightener 3 is Optiblanc SPL10 (registered trademark) (3V Sigma).
Perfume capsules are core-shell melamine formaldehyde perfume microcapsules.
The photobleach is a sulfonated zinc phthalocyanine.
The polishing enzyme is para-nitrobenzyl esterase, reported as 1000 mg activity / g.
The polyetheramine is as described in the present disclosure.
Polymer 1 bis _{((C 2 H 5 O)} (C 2 H 4 O) n) (CH 3) -N + -C x H 2x -N + - (CH 3) - bis _((C 2 _{H 5 O) (C 2 H 4 O} ) n) [ wherein, n = 20 to 30, an x = 3 to 8], or its sulfated or sulfonated variant.
Polymer 2 is ethoxylated (EO ₁₅ ) tetraethylenepentamine.
Polymer 3 is an ethoxylated polyethyleneimine.
Polymer 4 is an ethoxylated hexamethylenediamine.
Polymer 5 is Acusol 305 provided by Rohm & Haas.
Polymer 6 is a polyethylene glycol polymer grafted with vinyl acetate side chains, provided by BASF.
Protease 1 is Purafect Prime® (40.6 mg activity / g).
Protease 2 is Savinase® (32.89 mg activity / g).
Protease 3 is Purafect® (84 mg activity / g).
The quaternary ammonium is _C12-14 dimethylhydroxyethylammonium chloride.
S-ACMC is Reactive Blue 19 azo-CM-cellulose provided by Megazyme.
The soil release agent is Repel-o-tex® SF2, supplied by Solvay.
The structurant is hydrogenated castor oil.
Violet DD is a thiophene azo polymer toning dye provided by Milliken.

  The dimensions and values disclosed herein are not to be understood as being strictly limited to the exact numerical values recited. Instead, unless otherwise indicated, each such dimension is intended to mean both the recited value and a functionally equivalent range surrounding that value. For example, a dimension disclosed as "40 mm" is intended to mean "about 40 mm".

Claims (15)

  A cleaning composition comprising an amylase enzyme and an enzyme having glycoside hydrolase activity and selected from enzymes of the class of endo-α-1,4-polygalactosaminidase (EC 3.2.1.109).   The cleaning composition according to claim 1, wherein the glycoside hydrolase enzyme having glycoside hydrolase activity is a variant having at least 60%, preferably at least 70%, more preferably at least 80% identity to SEQ ID NO: 1. object.   The cleaning composition according to claim 1, wherein the glycoside hydrolase is derived from GH family 114. 4.   The cleaning composition according to any one of claims 1 to 3, wherein the glycoside hydrolase comprises PelAh.   The cleaning composition according to any one of claims 1 to 4, wherein the glycoside hydrolase enzyme can be obtained from Pseudomonas, preferably Pseudomonas aeruginosa.   The cleaning composition according to any one of claims 1 to 5, wherein the glycoside hydrolase enzyme is an isolated glycoside hydrolase.   The cleaning composition according to any one of claims 1 to 6, further comprising an additional enzyme selected from galactanase, mannanase, nuclease, and mixtures thereof.   The cleaning composition according to claim 7, further comprising a nuclease enzyme, preferably a deoxyribonuclease enzyme.   The method according to any one of claims 1 to 8, further comprising one, preferably two or three or more additional enzymes selected from lipases, proteases, pectate lyases, cellulases, cutinases, and mixtures thereof. A cleaning composition as described.   E. FIG. C. 10. The method according to any one of claims 1 to 9, further comprising a β-N-acetylglucosaminidase enzyme from 3.2.1.52, preferably an enzyme having at least 70% identity to SEQ ID NO: 12. A cleaning composition as described.   11. The method according to any of the preceding claims, further comprising 1% to 80%, preferably 5 to 80% by weight of the cleaning composition, of a surfactant system, preferably comprising an anionic surfactant. A cleaning composition as described.   The surfactant system according to claim 11, wherein the surfactant system additionally comprises a nonionic surfactant, preferably the weight ratio of anionic surfactant to nonionic surfactant is 25: 1 to 1: 2. Cleaning composition.   The anionic surfactant is selected from alkyl benzene sulfonates and (optionally alkoxylated) alkyl sulfates, and mixtures thereof, preferably an anionic surfactant comprising at least 50% by weight of the alkyl benzene sulfonate surfactant. A cleaning composition according to claim 11 or claim 12.   A method for cleaning a surface, preferably a textile product, comprising mixing the cleaning composition according to any one of claims 1 to 13 with water to form an aqueous liquid, and in a washing step. Contacting the surface, preferably a textile product, with the aqueous liquid, preferably wherein the glycoside hydrolase enzyme comprises 0.01 ppm to 1000 ppm of the enzyme in the aqueous liquid, based on active protein. The method is present in an amount or in an amount from 0.05 ppm or 0.1 ppm to 750 ppm or 500 ppm.   It has an amylase enzyme and a glycoside hydrolase activity to enhance stain removal from surfaces, preferably textile surfaces, especially oily stain removal, to enhance body soil removal and / or to reduce malodor from said surfaces. And an enzyme belonging to the class of the endo-α-1,4-polygalactosaminidase (EC 3.2.1.109).