EP3339419A1 - Laundry detergent composition - Google Patents

Laundry detergent composition Download PDF

Info

Publication number
EP3339419A1
EP3339419A1 EP17173007.0A EP17173007A EP3339419A1 EP 3339419 A1 EP3339419 A1 EP 3339419A1 EP 17173007 A EP17173007 A EP 17173007A EP 3339419 A1 EP3339419 A1 EP 3339419A1
Authority
EP
European Patent Office
Prior art keywords
composition
selected
preceding
particularly
composition according
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP17173007.0A
Other languages
German (de)
French (fr)
Inventor
Neil Joseph Lant
Alan Thomas Brooker
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Procter and Gamble Co
Original Assignee
Procter and Gamble Co
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
Priority to EP16206503 priority Critical
Application filed by Procter and Gamble Co filed Critical Procter and Gamble Co
Priority claimed from PCT/CN2017/117073 external-priority patent/WO2018113644A1/en
Priority claimed from PCT/US2017/067156 external-priority patent/WO2018118824A1/en
Priority claimed from PCT/CN2017/117072 external-priority patent/WO2018113643A1/en
Priority claimed from PCT/US2017/067157 external-priority patent/WO2018118825A1/en
Priority claimed from PCT/CN2017/117078 external-priority patent/WO2018113646A1/en
Priority claimed from PCT/CN2017/117074 external-priority patent/WO2018113645A1/en
Publication of EP3339419A1 publication Critical patent/EP3339419A1/en
Application status is Withdrawn legal-status Critical

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D17/00Detergent materials characterised by their shape or physical properties
    • C11D17/0039Coated compositions or coated components in the compositions, (micro)capsules
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02Anionic compounds
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/66Non-ionic compounds
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/66Non-ionic compounds
    • C11D1/83Mixtures of non-ionic with anionic compounds
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/0005Other compounding ingredients characterised by their effect
    • C11D3/0021Dye-stain or dye-transfer inhibiting compositions
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/02Inorganic compounds ; Elemental compounds
    • C11D3/04Water-soluble compounds
    • C11D3/10Carbonates ; Bicarbonates
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/20Organic compounds containing oxygen
    • C11D3/2075Carboxylic acids-salts thereof
    • C11D3/2086Hydroxy carboxylic acids-salts thereof
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/37Polymers
    • C11D3/3746Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3769(Co)polymerised monomers containing nitrogen, e.g. carbonamides, nitriles, amines
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/37Polymers
    • C11D3/3746Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3769(Co)polymerised monomers containing nitrogen, e.g. carbonamides, nitriles, amines
    • C11D3/3776Heterocyclic compounds, e.g. lactam
    • CCHEMISTRY; METALLURGY
    • C11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/38Products with no well-defined composition, e.g. natural products
    • C11D3/386Preparations containing enzymes, e.g. protease, amylase

Abstract

The present invention relates to a solid laundry detergent composition comprising:
(a) from 20wt% to 39wt% detersive surfactant selected from anionic detersive surfactant and/or non-ionic detersive surfactant;
(b) from 10wt% to 40wt% inorganic salts selected from sodium carbonate, sodium sesquicarbonate, sodium bicarbonate and any mixtures thereof;
(c) optionally, from 10wt% to 40wt% citric acid and/or salts thereof;
(d) from 0.01wt% to 20wt% dye transfer inhibitor (DTI) polymer selected from polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones, polyvinylimidazoles, and any combination thereof,
wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a pH in the range of from 7.6 to 10.0;
wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a reserve alkalinity to pH 7.5 of greater than 3.0,
wherein the composition is in the form of a coated laundry detergent particle that is curved and has perpendicular dimensions x, y and z,
wherein x is from 0.5mm to 2.0mm,
wherein y is from 2.0mm to 8.0mm, and
wherein z is from 2.0mm to 8.0mm,
wherein the coating comprises the inorganic salt (b), and wherein the core comprises the detersive surfactant (a).

Description

    FIELD OF THE INVENTION
  • The present invention relates to laundry detergent compositions, especially laundry detergent powders having a low pH profile that also comprise carbonate salt. The laundry detergent compositions of the present invention provide good cleaning performance and good colour care performance.
  • BACKGROUND OF THE INVENTION
  • Laundry detergent powders are typically formulated at quite high alkaline pH, for example a pH in the range of 10.5 to 12.0. Cleaning and colour care chemistries that are incorporated into laundry detergent powders are typically designed to provide good cleaning performance, and oftentimes even optimized cleaning performance, at this pH range.
  • Recently, laundry detergent powder manufacturers are designing products that are formulated to a much lower pH range, such as from 7.6 to 10.0. Such laundry detergent powders provide good fabric care performance. However, the cleaning performance and colour care performance of these lower pH laundry powder formulations needs to be carefully considered. Cleaning chemistries and colour care chemistries that provide good cleaning performance and good colour care performance at high pH wash conditions do not always provide good cleaning performance and colour care performance at low pH wash conditions. Consequently, the cleaning performance and colour care performance of low pH laundry detergent powders is reduced.
  • In addition, one of the main formulation chassis approaches to lowering the pH profile of a laundry detergent powder is to lower, or even remove, carbonate salt from the product. The presence of carbonate anion in the wash impacts the cleaning performance of some cleaning chemistries and the colour care performance of some colour care chemistries typically formulated in the laundry detergent powder. Consequently, the removal of carbonate salt leads to a formulation strategy of using cleaning chemistries and colour care chemistries that provide good cleaning performance and good colour care performance at both a low pH wash condition and also a low carbonate anion wash level.
  • However, the present invention differs from this recent low pH laundry powder formulation approach in that the present invention seeks to provide a low pH laundry detergent powder that has a low pH profile, and that provides good cleaning performance and good colour care performance, and that also comprises carbonate salt. This requires a formulation approach of including of cleaning technologies and colour care technologies that provide good cleaning performance and good colour care performance at low wash pH and that also provide good cleaning performance and good colour care performance in the presence of carbonate salt. The presence of carbonate salt in the product aids the performance of the product, for example by providing precipitating builder performance or by providing effervescence performance which leads to improved dispensing/dissolution performance, especially in cold and quick wash cycles.
  • In addition, when these products are in a coated lenticular form, due to the particle architecture of this product form, the cleaning performance and colour care performance of the product needs to be improved, especially in stressed washed conditions such as cold and quick wash cycles. The present invention addresses this problem.
  • SUMMARY OF THE INVENTION
  • The present invention provides a solid laundry detergent composition comprising:
  1. (a) from 20wt% to 39wt% detersive surfactant selected from anionic detersive surfactant and/or non-ionic detersive surfactant;
  2. (b) from 10wt% to 40wt% inorganic salts selected from sodium carbonate, sodium sesquicarbonate, sodium bicarbonate and any mixtures thereof;
  3. (c) optionally, from 10wt% to 40wt% citric acid and/or salts thereof;
  4. (d) from 0.01wt% to 20wt% dye transfer inhibitor (DTI) polymer selected from polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones, polyvinylimidazoles, and any combination thereof,
wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a pH in the range of from 7.6 to 10.0;
wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a reserve alkalinity to pH 7.5 of greater than 3.0,
wherein the composition is in the form of a coated laundry detergent particle that is curved and has perpendicular dimensions x, y and z,
wherein x is from 0.5mm to 2.0mm,
wherein y is from 2.0mm to 8.0mm, and
wherein z is from 2.0mm to 8.0mm,
wherein the coating comprises the inorganic salt (b), and wherein the core comprises the detersive surfactant (a). DETAILED DESCRIPTION OF THE INVENTION
  • Solid laundry detergent composition: The solid laundry detergent composition comprises:
    1. (a) from 20wt% to 39wt% detersive surfactant selected from anionic detersive surfactant and/or non-ionic detersive surfactant;
    2. (b) from 10wt% to 40wt% inorganic salts selected from sodium carbonate, sodium sesquicarbonate, sodium bicarbonate and any mixtures thereof;
    3. (c) optionally, from 10wt% to 40wt% citric acid and/or salts thereof;
    4. (d) from 0.01wt% to 20wt% dye transfer inhibitor (DTI) polymer selected from polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones, polyvinylimidazoles, and any combination thereof,
    wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a pH in the range of from 7.6 to 10.0;
    wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a reserve alkalinity to pH 7.5 of greater than 3.0,
    wherein the composition is in the form of a coated laundry detergent particle that is curved and has perpendicular dimensions x, y and z,
    wherein x is from 0.5mm to 2.0mm,
    wherein y is from 2.0mm to 8.0mm, and
    wherein z is from 2.0mm to 8.0mm,
    wherein the coating comprises the inorganic salt (b), and wherein the core comprises the detersive surfactant (a).
  • The coated laundry detergent particle may be lenticular (e.g. shaped like a whole dried lentil), an oblate ellipsoid, and where z and y are the equatorial diameters and x is the polar diameter; preferably y = z.
  • Typically, when x = 2mm, then at least one of z or y = >2mm, and preferably >3mm.The dimensions x, y and z can be measured using image analysis. Suitable equipment for image analysis includes a Leica Binocular Microscope (Leica MZ16A) with motorised and indexed mount, using a digital camera (Leica IC30) to capture the images, the images would be processed within the LEICA Application Software (LAS) platform using the optional Montage MultiFocus and Analysis modules.
  • The X and y axial size can be determined by pixel count analysis of the Feret diameters with the maximum and minimum Feret Diameters representing the X and Y axial lengths.
  • The Z axial length can be determined via the use of focus stacking (i.e. z-stacked images) which is a digital image processing technique which combines multiple images taken at different known focus distances to give a resulting image with a greater depth of field (DOF) than any of the individual source images.
  • A suitable method for making the detergent particle is described in WO2010/122050 .
  • The coated laundry detergent particle may be shaped as a disc. Preferably the coated laundry detergent particle does not have hole; that is to say, the coated laundry detergent particle does not have a conduit that passes through the core: i.e. the coated detergent particle has a topologic genus of zero.
  • The composition may comprise from 0.05wt% to 4.0wt% soil release polymer.
  • The composition may comprise from 0.1wt% to 3.0wt% carboxymethylcellulose (CMC).
  • The composition may comprise from 0.1wt% to 5.0wt% calcite.
  • The composition may comprise from 1wt% to 10wt% carboxylate polymer.
  • The composition may comprise less than 10wt% total level of silicates and aluminosilicates.
  • The composition may comprise from 0.001wt% to 0.5wt% hueing dye.
  • The composition may comprise from 0.001wt% to 0.5wt% organic pigment and/or inorganic pigment.
  • The composition may comprise from 0.2 wt% to 10wt% chelant, preferably phosphonate chelant.
  • The composition preferably comprises from 10wt% to 40wt% sodium carbonate.
  • Dye transfer inhibitor polymer: The composition comprises from 0.01wt% to 20wt%, preferably from 0.5wt% to 5wt%, more preferably from 0.2wt% to 2wt% dye transfer inhibitor (DTI) polymer selected from polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones, polyvinylimidazoles, and any combination thereof. Suitable DTI polymers include the Sokalan® HP product range from BASF (e.g. Sokalan® HP165, HP22, HP25, HP50, HP53, HP56, HP56K), the Chromabond® range from Ashland (e.g. Chromabond® S100 and S350), and the Reilline® range from Vertellus (e.g. Reilline® 350, 4035, 4140).
  • Detersive surfactant: A suitable detersive surfactant system typically comprises at least 5% alcohol ether carboxylate as a percentage of the total detersive surfactant system.
  • A suitable detersive surfactant system typically comprises at least 5% alcohol ethoxylate having an average degree of ethoxylation in the range of from 10 to 50 as a percentage of the total detersive surfactant system.
  • Preferably, the detersive surfactant comprises C8-C24 alkyl ethoxylated alcohol having an average degree of ethoxylation of from 20 to 50, and preferably the compositon comprises from 1wt% to 10wt% C8-C24 alkyl ethoxylated alcohol having an average degree of ethoxylation of from 20 to 50. A suitable highly ethoxylated alcohol is Lutensol® AO30 from BASF and/or Slovasol® 2430 from Sasol.
  • Anionic detersive surfactant: Suitable anionic detersive surfactants include sulphonate and sulphate detersive surfactants.
  • Suitable sulphonate detersive surfactants include methyl ester sulphonates, alpha olefin sulphonates, alkyl benzene sulphonates, especially alkyl benzene sulphonates, preferably C10-13 alkyl benzene sulphonate. Suitable alkyl benzene sulphonate (LAS) is obtainable, preferably obtained, by sulphonating commercially available linear alkyl benzene (LAB); suitable LAB includes low 2-phenyl LAB, other suitable LAB include high 2-phenyl LAB, such as those supplied by Sasol under the tradename Hyblene®.
  • Suitable sulphate detersive surfactants include alkyl sulphate, preferably C8-18 alkyl sulphate, or predominantly C12 alkyl sulphate.
  • A preferred sulphate detersive surfactant is alkyl alkoxylated sulphate, preferably alkyl ethoxylated sulphate, preferably a C8-18 alkyl alkoxylated sulphate, preferably a C8-18 alkyl ethoxylated sulphate, preferably the alkyl alkoxylated sulphate has an average degree of alkoxylation of from 0.5 to 20, preferably from 0.5 to 10, preferably the alkyl alkoxylated sulphate is a C8-18 alkyl ethoxylated sulphate having an average degree of ethoxylation of from 0.5 to 10, preferably from 0.5 to 5, more preferably from 0.5 to 3 and most preferably from 0.5 to 1.5.
  • The alkyl sulphate, alkyl alkoxylated sulphate and alkyl benzene sulphonates may be linear or branched, substituted or un-substituted, and may be derived from petrochemical material or biomaterial.
  • Other suitable anionic detersive surfactants include alkyl ether carboxylates.
  • Suitable anionic detersive surfactants may be in salt form, suitable counter-ions include sodium, calcium, magnesium, amino alcohols, and any combination thereof. A preferred counterion is sodium.
    Alkyl ether carboxylic acid: A suitable alkyl ether carboxylic acid has the following structure:

             R-(OCH2CH2)n-OCH2-COOH

    wherein,
    • R is selected from saturated and mono-unsaturated C10 to C26 linear or branched alkyl chains, preferably C12 to C24 linear or branched alkyl chains, most preferably a C16 to C20 linear alkyl chain;
    • n is selected from 5 to 20, preferably 7 to 13, more preferably 8 to 12, most preferably 9.5 to 10.5; and
    • The alkyl ether carboxylic acid may be present from 0.5 to 20 wt%, preferably from 2 to 14 wt%, most preferably from 2.5 to 5 wt%. It may be present in acid or salt form, most preferably as its sodium salt.
  • Suitable materials are sold under the AKYPO® (Kao) and Empicol® C (Huntsman) brand names.
  • Non-ionic detersive surfactant: Suitable non-ionic detersive surfactants are selected from the group consisting of: C8-C18 alkyl ethoxylates, such as, NEODOL® non-ionic surfactants from Shell; C6-C12 alkyl phenol alkoxylates wherein preferably the alkoxylate units are ethyleneoxy units, propyleneoxy units or a mixture thereof; C12-C18 alcohol and C6-C12 alkyl phenol condensates with ethylene oxide/propylene oxide block polymers such as Pluronic® from BASF; alkylpolysaccharides, preferably alkylpolyglycosides; methyl ester ethoxylates; polyhydroxy fatty acid amides; ether capped poly(oxyalkylated) alcohol surfactants; and mixtures thereof.
  • Suitable non-ionic detersive surfactants are alkylpolyglucoside and/or an alkyl alkoxylated alcohol.
  • Suitable non-ionic detersive surfactants include alkyl alkoxylated alcohols, preferably C8-18 alkyl alkoxylated alcohol, preferably a C8-18 alkyl ethoxylated alcohol, preferably the alkyl alkoxylated alcohol has an average degree of alkoxylation of from 1 to 50, preferably from 1 to 30, or from 1 to 20, or from 1 to 10, preferably the alkyl alkoxylated alcohol is a C8-18 alkyl ethoxylated alcohol having an average degree of ethoxylation of from 1 to 10, preferably from 1 to 7, more preferably from 1 to 5 and most preferably from 3 to 7. The alkyl alkoxylated alcohol can be linear or branched, and substituted or un-substituted.
  • Suitable nonionic detersive surfactants include secondary alcohol-based detersive surfactants.
  • Amino acid derivative complexing agent: A suitable amino acid derivative complexing agent is selected from one or more of the following, in any stereoisomer or mixture of stereoisomer form:
    1. (i) methylglycinediacetic acid and salts thereof (MGDA)
      Figure imgb0001
    2. (ii) L-glutamic acid, N,N-diacetic acid and salts thereof (GLDA)
      Figure imgb0002
      and
    3. (iii) L-aspartic acid N,N-diacetic acid and salts thereof (ASDA)
      Figure imgb0003
  • Preferbly, the composition comprises from 0.1wt% to 10wt% methylglycinediacetic acid and salts thereof (MGDA)
    Figure imgb0004
  • It may be preferred to formulate the amino acid derivative complexing agent in acid form. Alternatively, it may be preferred to formulate the amino acid derivative complexing agent in salt form, especially preferred is the sodium salt form.
  • Suitable MGDA salts are produced by BASF. Suitable GLDA salts are produced by Akzo Nobel and Showa Denko. Suitable ASDA salts are produced by Mitsubishi Rayon.
  • Alkoxylated polyaryl/polyalkyl phenol: A suitable alkoxylated polyaryl/polyalkyl phenol has the following structure:
    Figure imgb0005
    wherein R1 is selected from linear of branched C3-C15 alkyl groups and aryl groups, X is selected from ethoxy or propoxy groups, n is from 2 to 70, T is selected from H, SO3 -, COO- and PO3 2-
  • The alkoxylated polyaryl or alkoxylated polyalkyl phenol is preferably selected from groups (i) to (iv):
    1. (i) Uncharged alkoxylated tristyrylphenols of the following structure:
      Figure imgb0006
      wherein n is selected from 2 to 70, more preferably n is selected from 10 to 54, most preferably n = 16 or 20.
    2. (ii) Anionic alkoxylated tristyrylphenols of the following structure
      Figure imgb0007
      wherein R is selected from SO3 -, COO- and PO3 2-, preferably selected from SO3 - and COO-, wherein n is selected from 2 to 54.
    3. (iii) Uncharged alkoxylated tri(n-butyl)phenols of the following structure:
      Figure imgb0008
      wherein n is selected from 2 to 50
    4. (iv) Anionic alkoxylated tri(n-butyl)phenols of the following structure:
      Figure imgb0009
      wherein R is selected from SO3 -, COO- and PO3 2-, preferably selected from SO3 - and COO-, wherein n is selected from 6 to 50.
  • Such compounds are available from industrial suppliers, for example Solvay under the Soprophor trade name, from Clariant under the Emulsogen trade name, Aoki Oil Industrial Co. under the Blaunon trade name, from Stepan under the Makon trade name, and from TOTO Chemical Industry Co. under the Sorpol trade name. Specific examples of suitable compounds are Emulsogen® TS160, Hostapal® BV conc., Sapogenat® T110 or Sapogenat® T139, all from Clariant.
  • The alkoxylated polyaryl/polyalkyl phenol may be present at levels of 0.5-20wt%, preferably 1-15wt%, most preferably 3-10wt%.
  • Amylase variant: A suitable amylase variant comprises:
    1. (a) a deletion and/or a substitution at two or more positions corresponding to positions R181, G182, H183 and G184 of the mature polypeptide of SEQ ID NO: 1 , and
    2. (b) a substitution at one or more positions said substitutions selected from the group consisting of:
      • I206Y;F;Q;P;R;V;C;G;A;C;D;E;H;K;L;M;N;S;T, particularly I206Y;F;C;L;H;S,
      • N195F;Y;H;K;L,
      • L63Q;P;R;V;F;C;G;A;C;D;E;H;K;I;M;N;S;T;Y, particularly L63V,
      • A113M;R;W;I;L,
      • M116F;Y;I;W;L,
      • R118P;Q;V;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly R118P;Q;V;F;C;G,
      • N128C;
      • Q129P;R;V;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly Q129E,
      • G133N,
      • A139Q;P;R;V;F;C;G;C;D;E;H;I;K;L;M;N;S;T;Y, particularly A139T,
      • R142H;V;L;Q;I,
      • A186E;N;Q;S,
      • E190P;R;V;F;C;G;A;C;D;Q;H;I;K;L;M;N;S;T;Y, particularly E190P,
      • A204Q;P;R;V;F;C;G;C;D;E;H;I;K;L;M;N;S;T;Y, particularly A204T,
      • H210M;D;C;A;Q;S;F;N;E;T,
      • P211Q;R;V;F;C;G;A;C;D;E;H;1;K;L;M;N;S;T;Y,particularly P211L;M;S;Q;G;V;W;A;H;T;R;
      • E212T;R;S;V;L;Y;R;T;G;
      • V213Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly V213T;A;G;S;C;L;P,
      • V214Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly V214T;I,
      • L217M;Q;V;I;H, particularly L217V,
      • Y243Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;V, particularly Y243F,
      • S244Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;Y;T;V, particularly S244Q,
      • T246Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;Y;S;V, particularly T246Q;M,
      • N260E, Q280S, N311R, F343W, D418C, S419M, S420Q;R and Y482W,
      • where the positions correspond to the positions of SEQ ID NO 1 and wherein the amylase variant has at least 95%, such as at least 96%, or at least 97%, or at least 98%, or at least 99% but less than 100% sequence identity to the polypeptide having the amino acid sequence of SEQ ID NO: 1 and wherein the variant has alpha-amylase activity.
  • One preferred amylase variant comprises a sequence corresponding to SEQ ID NO: 1 with the following mutations: H183*+G184*+I405L+A421H+A422P+A428T.
  • A suitable amylase is commercially available from Novozymes under the Amplify® brand name, for example as a liquid raw material as Amplify® 12L.
  • Metalloprotease: Metalloproteases can be derived from animals, plants, bacteria or fungi. Suitable metalloprotease can be selected from the group of neutral metalloproteases and Myxobacter metalloproteases. Suitable metalloproteases can include collagenases, hemorrhagic toxins from snake venoms and thermolysin from bacteria.
  • Preferred thermolysin enzyme variants include an M4 peptidase, more preferably the thermolysin enzyme variant is a member of the PepSY~Peptidase_M4~Peptidase_M4_C family.
  • Suitable metalloprotease variants can have at least 50% identity to the thermolysin set forth in SEQ ID NO: 3. In some embodiments, the thermolysin enzyme variant is from a genus selected from the group consisting of Bacillus, Geobacillus, Alicyclobacillus, Lactobacillus, Exiguobacterium, Brevibacillus, Paenibacillus, Herpetosiphon, Oceanobacillus, Shewanella, Clostridium, Staphylococcus,Flavobacterium, Stigmatella, Myxococcus, Vibrio, Methanosarcina, Chryseobacterium, Streptomyces,Kribbella, Janibacter, Nocardioides, Xanthamonas, Micromonospora, Burkholderia, Dehalococcoides, Croceibacter, Kordia, Microscilla, Thermoactinomyces, Chloroflexus, Listeria, PLesiocystis, Haliscomenobacter, Cytophaga, Hahella, Arthrobacter, Brachybacterium, Clavibacter, Microbacterium, Intrasporangium, Frankia, Meiothermus, Pseudomonas, Ricinus, Catenulispora, Anabaena, Nostoc, Halomonas, Chromohalobacter, Bordetella, Variovorax, Dickeya, Pectobacterium, Citrobacter, Enterobacter, Salmonella, Erwinia, Pantoea, Rahnella, Serratia, Geodermatophilus, Gemmata, Xenorhabdus, Photorhabdus, Aspergillus, Neosartorya, Pyrenophora, Saccharopolyspora, Nectria, Gibberella, Metarhizium, Waddlia, Cyanothece, Cellulphaga, Providencia, Bradyrhizobium,Agrobacterium, Mucilaginibacter, Serratia, Sorangium, Streptosporangium, Renibacterium, Aeromonas,Reinekea, Chromobacterium, Moritella, Haliangium, Kangiella, Marinomonas, Vibrionales, Listonella, Salinivibrio, Photobacterium, Alteromonadales, Legionella, Teredinibacter, Reinekea, Hydrogenivirga and Pseudoalteromonas. In some embodiments, the thermolysin enzyme variant is from a genus selected from the group consisting of Bacillus, Geobacillus, Alicyclobacillus, Lactobacillus, Exiguobacterium, Brevibacillus, Paenibacillus, Herpetosiphon, Oceanobacillus, Shewanella, Clostridium, Staphylococcus, Flavobacterium, Stigmatella, Myxococcus, Vibrio, Methanosarcina, Chryseobacterium, and Pseudoalteromonas.
  • Preferably the thermolysin enzyme is from the genus Bacillus.
  • Preferred metalloproteases include thermolysin, matrix metalloproteinases and those metalloproteases derived from Bacillus subtilis, Bacillus thermoproteolyticus, Geobacillus stearothermophilus or Geobacillus sp., or Bacillus amyloliquefaciens, as described in US PA 2008/0293610A1 .
  • A specially preferred metalloprotease belongs to the family EC3.4.24.27.
  • Further suitable metalloproteases are the thermolysin variants described in WO2014/71410 .
  • In one aspect the metalloprotease is a variant of a parent protease, said parent protease having at least 60%, or 80%, or 85% or 90% or 95% or 96% or 97% or 98% or 99% or even 100% identity to SEQ ID NO:3 including those with substitutions at one or more of the following sets of positions versus SEQ ID NO:3:
    1. (a) 2, 26, 47, 53, 87, 91,96, 108, 118, 154, 179, 197, 198, 199, 209, 211, 217, 219, 225, 232, 256, 257, 259, 261, 265, 267, 272,276, 277, 286, 289, 290, 293, 295, 298, 299, 300, 301, 303,305,308,311 and 316;
    2. (b) 1, 4, 17, 25, 40, 45, 56, 58, 61, 74, 86, 97, 101, 109, 149, 150 , 158, 159, 172, 181, 214, 216, 218, 221, 222, 224, 250, 253, 254, 258, 263, 264, 266, 268, 271, 273, 275, 278, 279, 280, 282, 283, 287, 288, 291, 297, 302, 304, 307 and 312;
    3. (c) 5, 9, 11, 19, 27, 31, 33, 37, 46, 64, 73, 76, 79, 80, 85, 89, 95, 98, 99, 107, 127, 129, 131, 137, 141, 145, 148, 151, 152, 155, 156, 160, 161, 164, 168 , 171, 176, 180, 182, 187, 188, 205, 206, 207, 210, 212, 213, 220, 227, 234 , 235, 236, 237, 242, 244, 246, 248, 249, 252, 255, 270, 274, 284, 294, 296, 306, 309, 310, 313, 314 and 315;
    4. (d) 3, 6, 7, 20, 23, 24, 44, 48, 50, 57, 63, 72, 75, 81, 92, 93, 94, 100, 102, 103, 104, 110, 117, 120, 134, 135, 136, 140, 144, 153, 173, 174, 175, 178, 183, 185, 189, 193, 201, 223, 230, 238, 239, 241, 247, 251, 260, 262, 269, and 285;
    5. (e) 17, 19, 24, 25, 31, 33, 40, 48, 73, 79, 80, 81, 85, 86, 89, 94, 109, 117, 140, 141, 150, 152, 153, 158, 159, 160, 161, 168, 171, 174, 175, 176, 178, 180, 181, 182, 183, 189, 205, 206, 207, 210, 212, 213, 214, 218, 223, 224,227, 235, 236, 237, 238, 239, 241, 244, 246, 248, 249, 250, 251, 252, 253, 254, 255, 258, 259, 260, 261, 262, 266, 268, 269, 270, 271, 272, 273, 274, 276, 278, 279, 280, 282, 283, 294, 295, 296, 297, 300, 302, 306, 310 and 312;
    6. (f) 1, 2, 127, 128, 180, 181, 195, 196, 197, 198, 199, 211, 223, 224, 298, 299, 300, and 316 all relative to SEQ ID NO:3.
  • In a further aspect the metalloprotease protease is a variant of a parent protease, said parent protease having at least 60%, or 80%, or 85% or 90% or 95% or 96% or 97% or 98% or 99% or even 100% identity to SEQ ID NO:3 including those with substitutions at one or more of the following sets of positions versus SEQ ID NO:3:
    1. (a) I001L, T002A, T002C, T002I, T002K, T002M, T004K, T004L, T004M, T004Y, Q017L, N037K, F040K, F040L, K045A, K045G, K045M, T049E, T049M, T049Y, L050P, S053C, S053L, A056M, A058E, A058L, Q061L, F063C, A064D, A064E, S065A, S065D, S065E, S065P, S065Y, V087C, V087K, V087L, V087M, V087N, V087Q, V087W, V087Y, N096K, N096L, N096Y, R101H, Q108L, Q108M, G109E, G109M, G109R, G109W, S118A, S118D, S118M, S118Q, S118R, S118T, SI 18V, Q128A, Q128L, Q128Y, I131L, I137L, T149N, G154A, G154H, G154K, G154M, G154Y, L155M, I164A, N181S, G196A, G196W, I197C, S198A, S198K, G199A, G199Y, A209C, A209M, H216A, Y217C, Y217L, T222K, N227A, I244L, Q246D, V256N, L263A, L263M, T272K, Q273N, Y274M, P277A, P277D, P277Y, L284A, L284M, L284Y, A286K, A286L, A286M, A286N, A286Y, A287C, A288L, A288M, V289A, S291A, S291T, T293A, T293I, T293K, T293L, T293M, T293Y, L295A, L295K, L295M, L295W, Y296M, G297N, S298A, S298G, S298K, S298M, S298R, T299A, T299K, S300D, S300N, Q301K, E302A, V303A, V303P, V303Y, A304E, A304K, A304Y, S305A, S305K, S305M, V306L, V306T, A309C, F310M, D311A, D311K, D311L, D311M, D311V, D311W,D311Y, and A312C;
    2. (b) T002Q, T004V, V007I, V009I, R01 IK, I020L, I020V, S025A, S025C, S025K, S025M, S025R, T026C, T026D, Y027C, Y027L, N037L, F040A, A044C, K045F, K045H, K045Q, K045Y, Y046C, R047D, R047E, R047G, R047L, R047M, R047Q, R047T, T049L, T049N, T049Q, T049V, S053A, S053N, S053V, A056E, Q061C, Q061I, A064T, S065L, S065T, S065W, A073F, A073L, A073M, A073W, H074C, H074F, H074M, H074N, H074Q, H074W, T080L, T080N, K085S, N086D, V087R, V087T, L091A, L091N, L091R, L091W, L091Y, S092L, Y093C, N096G, N096H, N096Q, N096R, N096S, N096W, N097E, N097M, A099R, A099S, R101C, R101L, R101S, S102N, S107G, Q108I, Q108K, Q108N, G109S, S118E, M120L, Q128I, Q128K, T129L, T129M, I131W, S134P, G136S, I137E, I137T, I137V, V140D, V148A, V148Q, T149D, T149S, T152G, G154C, G154N, L155I, N159S, N159Y, I164C, I168L, I171G, Y179F, A180S, G189A, Y193F, G196H, G196L, G196Y, I197F, S198M, S198N, S198R, S198W, S201A, A209G, A209I, A209K, A209P, A209R, A209Y, Y211E, Y211R, P214A, P214R, Y217A, Y217F, Y217M, Y217N, K219A, K219E, K219R, K219S, R220A, Y221A, Y221F, Y221G, Y221M, T222A, T222M, Q225C, Q225E, Q225K, Q225L, Q225S, I232L, I232R, I232S, I232T, I232V, I232Y, S234A, S234C, G235A, I236C, I244A, I244M, Q246C, V256S, G257K, G257R, I258A, I258C, I258K, I258Q, I258V, G259N, G259S, G259T, L263H, L263K, L263N, L263V, G264A, G264N, G264P, G264Q, G264S, G264T, K265N, I266C, I266M, I266T, I266V, F267A, F267C, F267H, F267I, F267K, F267L, F267M, F267T, F267Y, R269K, A270G, L271H, T272A, Q273E, Q273G, L275C, L275Q, L275S, L275T, T276A, T276L, T276V, T276Y, P277E, P277F, P277G, P277H, P277N, P277R, P277V, P277W, S279G, R285Y, A286C, A286Q, A286R, A286T, A288N, V289L, V289M, V289Y, Q290A, Q290H, Q290N, S291V, T293N, T293V, T293W, D294N, L295F, L295G, Y296W, G297D, S298E, S298N, S298P, T299N, S300A, S300G, S300T, Q301M, Q301S, Q301T, Q301V, E302D, E302Q, V303G, V303K, V303L, V303R, V303W, A304R, A304S, A304T, A304W, S305H, S305T, S305V, V306I, Q308A, Q308L, F310C, F310W, D311F, D311G, D311I, D311Q, D311S, D311T, V313C, G314Q, V315L, V315T, K316A, and K316M;
    3. (c) I001K, I001M, I001V, T002F, T002L, T002P, T002S, T002V, T002W, T002Y, T004E,S005D, S005N, S005P, T006C, R011I, Q017I, Q017W, Q017Y, S025D, S025F, T026K, T026L, T026R, T026V, T026Y, Y027W, Q031A, Q031K, Q031V, N033S, N033T, N037D, N037Q, N037R, F040E, F040G, F040M, F040Q, F040S, F040Y, K045E, K045L, K045S, Y046L, R047A, R047C, R047H, R047K, R047N, T048E, T049A, T049D, T049F, T049H, T049I, T049S, S053F, S053H, S053I, S053M, S053Q, S053T, S053W, A056K, A056Q, A056V, A056W, Q061M, S065I, S065M, S065Q, S065V, D072F, H074E, H074L, Y076H, Y076L, Y076M, Y076Q, V079L, V079Q, V079T, T080I, Y081F, K085E, N086L, N086S, V087D, V087E, V087G, V087I, V087S, L091D, L091E, L091F, L091K, L091M, L091P, L091Q, L091S, Y093T, G095A, G095D, G095H, G095M, G095N, G095S, N096C, N096D, N096I, N096V, N097K, A098C, A098E, A098H, A098R, A099E, A099K, A099P, S107D, Q108C, Q108E, Q108F, Q108H, G127C, G127D, G127E, Q128C, Q128D, Q128E, Q128R, Q128S, T129I, T129R, S134A, I137P, A141S, T145A, T145C, T145E, T145G, T145M, T145N, T145Q, V148L, V148N, V148Y, T149M, T149V, Y151K, T152S, A153T, G154L, G154Q, G154S, G154T, L155C, Q158A, Q158K, Q158M, Q158N, N159R, N159W, S161A, S161N, S161P, S161T, I164L, I164N, I164S, I164T, I164V, I171C, I171E, I171F, I171L, I171S, F172G, F172L, F172M, F172Q, F172S, F172V, F172W, F172Y, G173A, G173C, T174C, V176L, V176N, N181L, G196D, G196E, G196T, I197D, I197K, I197L, I197T, I197V, I197W, I197Y, S198C, S198E, S198F, S198G, S198H, S198I, S198P, S198Q, S198T, S198V, G199C, G199E, G199F, G199H, G199Q, G199S, G199T, G199W, M205L, A209D, A209E, A209L, A209S, A209T, A209V, Y211A, Y211C, Y211D, Y211F, Y211G, Y211H, Y211I, Y211L, Y211N, Y211Q, Y211S, Y211T, D213N, D213S, P214C, P214G, P214K, P214S, H216C, H216E, H216S, H216T, Y217Q, Y217S, Y217T, Y217V, Y217W, S218K, S218L, S218Y, K219D, K219F, K219G, K219H, K219I, K219M, K219N, K219Q, K219T, R220K, R220V, Y221K, Y221N, Y221Q, Y221R, Y221S, Y221T, Y221V, T222C, T222D, T222L, T222Y, T224K, T224M, Q225D, Q225G, Q225H, Q225I, Q225P, Q225V, Q225W, I232C, I232E, I232F, I232K, I232M, I232N, I232Q, I232W, S234D, G235M, I236M, Y242C, Y242F, Y242N, Y242V, I244T, I244V, Q246E, Q246N, Q246T, G247A, G247S, T249K, T249M, T249N, H250A, H250C, G252K, G252Y, V253N, V253T, S254A, S254M, S254R, S254Y, V255L, V255P, V256L, V256T, G257C, G257D, G257E, G257L, G257N, G257P, G257Q, G257S, G257T, G257Y, I258E, I258L, I258M, I258N, G259A, G259C, G259E, G259F, G259H, G259L, G259M, G259W, D261A, D261N, L263C, L263I, L263Q, L263T, K265A, K265C, K265D, K265M, K265P, K265Q, K265S, I266A, I266F, I266L, I266S, F267E, F267G, F267N, F267S, F267V, F267W, Y268M, Y268Q, Y268V, A270C, A270F, A270I, A270L, A270S, L271A, L271D, L271F, L271I, T272E, T272L, T272V, T272W, Q273A, Q273H, Q273Y, Y274F, Y274H, L275I, L275M, L275V, T276C, T276F, T276I, T276P, T276Q, T276W, P277Q, P277S, P277T, T278G, S279A, S279D, S279I, S279L, S279M, S279N, S279Q, S279T, N280A, N280C, N280D, N280E, S282K, S282N, L284V, L284W, R285K, A286D, A286E, A286F, A286G, A286H, A286I, A286S, A287I, A287L, A287N, A287V, A287Y, A288C, A288I, A288S, A288T, A288V, V289C, V289E, V289F, V289G, V289I, V289N, V289S, V289W, Q290C, Q290D, Q290F, Q290G, Q290L, Q290W, S291E, T293C, T293E, T293F, T293G, T293H, T293Q, T293S, L295C, L295I, L295N, Y296N, G297A, G297M, G297R, G297Y, S298C, S298T, S298W, S298Y, T299C, T299F, T299L, T299M, T299R, T299W, S300C, S300K, S300M, S300R, S300Y, Q301E, Q301H, Q301P, Q301R, V303C, V303H, A304C, A304D, A304L, A304N, S305G, S305I, S305L, S305N, S305W, S305Y, V306A, V306S, K307A, K307C, K307G, K307I, K307M, K307N, K307Q, K307R, K307W, K307Y, Q308C, Q308D, Q308F, Q308G, Q308I, Q308M, A309G, A309S, D311C, D311E, A312G, A312M, A312V, V313T, G314A, G314E, G314H, G314M, G314S, G314W, V315A, V315C, V315I, V315M, K316D, K316E, K316F, K316G, K316H, K316L, K316N, K316P, K316Q, K316R, K316S, K316V, K316W and K316Y.
  • Further suitable metalloproteases are the NprE variants described in WO2007/044993 , WO2009/058661 and US 2014/0315775 .
  • In one aspect the protease is a variant of a parent protease, said parent protease having at least 45%, or 60%, or 80%, or 85% or 90% or 95% or 96% or 97% or 98% or 99% or even 100% identity to SEQ ID NO:4 including those with substitutions at one or more of the following sets of positions versus SEQ ID NO:4:
    • S23, Q45, T59, S66, S129, F130, M138, V190, S199, D220, K211, and G222,
  • Another suitable metalloprotease is a variant of a parent protease, said parent protease having at least 60%, or 80%, or 85% or 90% or 95% or 96% or 97% or 98% or 99% or even 100% identity to SEQ ID NO:4 including those with substitutions at one or more of the following sets of positions versus SEQ ID NO:4:
    • Q45E, T59P, 566E, S129I, S129V, F130L, M138I, V190I, S199E, D220P, D220E, K211V, K214Q, G222C, M138L/D220P, F130L/D220P, S129I/D220P, V190I/D220P, M138L/V190I/D220P, S129I/V190I, S129V/V190I, S129V/D220P, S129I/F130L/D220P, T004V/S023N, T059K/S66Q/S129I, T059R/S66N/S129I, S129I/F130L/M138L/V190I/D220P and T059K/S66Q/S129V.
  • Especially preferred metalloproteases for use herein belong belong to EC classes EC 3.4.22 or EC3.4.24, more preferably they belong to EC classes EC3.4.22.2, EC3.4.24.28 or EC3.4.24.27. The most preferred metalloprotease for use herein belong to EC3.4.24.27.
  • Suitable commercially available metalloprotease enzymes include those sold under the trade names Neutrase® by Novozymes A/S (Denmark), the Corolase® range including Corolase® 2TS, Corolase® N, Corolase® L10, Corolase® LAP and Corolase® 7089 from AB Enzymes, Protex 14L and Protex 15L from DuPont (Palo Alto, California), those sold as thermolysin from Sigma and the Thermoase range (PC10F and C100) and thermolysin enzyme from Amano enzymes.
  • A preferred metalloprotease is selected from the M4 Metalloprotease Family.
  • Lipase: A suitable lipase is a variant of SEQ ID NO:2 comprising:
    1. (a) substitutions T231R and N233R
      and
    2. (b) at least three further substitutions selected from D27R, N33Q, G38A, D96E, D111A, G91Q, G163K, E210Q, D254S, I255A, and P256T;
    where the positions correspond to the positions of SEQ ID NO 2 and wherein the lipase variant has at least 95% but less than 100% sequence identity to the polypeptide having the amino acid sequence of SEQ ID NO: 2 and wherein the variant has lipase activity.
  • One preferred lipase is a variant of SEQ ID NO: 2 comprising the following substitutions: T231R, N233R, D27R, G38A, D96E, D111A, G163K, D254S and P256T
    One preferred lipase is a variant of SEQ ID NO: 2 comprising the following substitutions: T231R, N233R, N33Q, G91Q, E210Q, I255A.
  • Suitable lipases are commercially available from Novozymes, for example as Lipex Evity 100L (a liquid raw material) and Lipex Evity 105T (a granulate). These lipases have different structures to the products Lipex 100L, Lipex 100T and Lipex Evity 100T which are outside the scope of this particular lipase definition.
  • Builder system: A suitable water-soluble builder system comprising one or more aminocarboxylates, selected from: methylglycine diacetic acid (MGDA) and/or alkali metal or ammonium salts thereof; N,N-dicarboxymethyl glutamic acid (GLDA) and/or alkali metal or ammonium salts thereof; Aspartic acid N,N-diacetic acid (ASDA) and/or alkali metal or ammonium salts thereof; Ethylene diamine-N,N'-disuccunic acid (EDDS) and/or alkali metal or ammonium salt thereof; 2-hydroxy propylene diamine-N,N'-disuccunic acid (HPDDS), and/or alkali metal or ammonium salt thereof; ethylenediamine-N,N'-diglutaric acid (EDDG and/or alkali metal or ammonium salt thereof; ethylenediamine-N,N'-bis-(orthohydroxyphenyl)acetic acid (EDDHA) and/or alkali metal or ammonium salt thereof; N-hydroxyethyl ethylenediamine-N,N',N'-triacetic acid (HEDTA) alkali metal or ammonium salts thereof; iminodisuccinate, hydroxyethyl iminodiacetate, and ethylene iminodisuccinate and the respective alkali metal or ammonium salts; and any combination thereof.
  • Phosphonate chelant: A suitable phosphonate chelant is selected from: 1-hydroxyethane-1,1-diphosphonic acid (HEDP); Diethylene triamine pentamethylene phosphonic acid (DTPMP, CW-Base); 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC); Amino trimethylene phosphonic acid (ATMP); Ethylenediamine tetramethylene phosphonic acid (EDTMP); Diethylenetriamine pentamethylene phosphonic acid (DTPMP); Aminotrimethylene phosphonic acid (ATMP); salts of the aforementioned materials; and any combination thereof.
  • Carboxylate polymer: The composition may comprise a carboxylate polymer, such as a maleate/acrylate random copolymer, maleic-olefin copolymers or polyacrylate homopolymer. Suitable carboxylate polymers include: polyacrylate homopolymers having a molecular weight of from 4,000 Da to 9,000 Da; maleate/acrylate random copolymers having a molecular weight of from 50,000 Da to 100,000 Da, or from 60,000 Da to 80,000 Da. Examples of the foregoing include Acusol 410N, Acusol 445N (polyacrylic acid, Na salt); Acusol 450N and Acusol 480N (modified polyacrylic acid, Na salt); Acusol 479N, Acusol 490N, and Acusol 505N (acrylic acid/maleic acid, Na salt); Acusol 460N (maleic acid/olefin, Na salt); Sokolan CP5 and Sokolan CP12S (maleic acid/acrylic acid, Na salt); and Sokolan CP 9 (maleic acid/olefin, Na salt). The Acusol series are available from Rohm & Haas, Philadelphia, PA and the Sokolan series are available from BASF (Germany and New Jersey).
  • Suitable carboxylate polymers can contain other monomers including modified acrylic, fumaric, maleic, itaconic, aconitic, mesaconic, citraconic and methylenemalonic acid or their salts, modified maleic anhydride, acrylamide, alkylene, vinylmethyl ether, styrene and any mixtures thereof. Suitable carboxylate polymers can also containing 2-acrylamido-2-methyl-1-propanesulfonic acid, 2-methacrylamido-2-methyl-1-propanesulfonic acid, 3-methacrylamido-2-hydroxy-propanesulfonic acid, allysulfonic acid, methallysulfonic acid, 2-hydroxy-3-(2-propenyloxy)propanesulfonic acid, 2-methyl-2-propenen-1-sulfonic acid, styrenesulfonic acid, vinylsulfonic acid, 3-sulfopropyl acrylate, 3-sulfopropylmethacrylate, sulfomethylacrylamide, sulfomethylmethacrylamide and water soluble salts thereof.
  • Another suitable carboxylate polymer is a co-polymer that comprises: (i) from 50 to less than 98 wt% structural units derived from one or more monomers comprising carboxyl groups; (ii) from 1 to less than 49 wt% structural units derived from one or more monomers comprising sulfonate moieties; and (iii) from 1 to 49 wt% structural units derived from one or more types of monomers selected from ether bond-containing monomers represented by formulas (I) and (II):
    Figure imgb0010
    wherein in formula (I), R0 represents a hydrogen atom or CH3 group, R represents a CH2 group, CH2CH2 group or single bond, X represents a number 0-5 provided X represents a number 1-5 when R is a single bond, and R1 is a hydrogen atom or C1 to C20 organic group;
    Figure imgb0011
    wherein in formula (II), R0 represents a hydrogen atom or CH3 group, R represents a CH2 group, CH2CH2 group or single bond, X represents a number 0-5, and R1 is a hydrogen atom or C1 to C20 organic group.
    It may be preferred that the polymer has a weight average molecular weight of at least 50kDa, or even at least 70kDa.
  • Soil release polymer: The composition may comprise a soil release polymer. A suitable soil release polymer has a structure as defined by one of the following structures (I), (II) or (III):

             (I)     -[(OCHR1-CHR2)a-O-OC-Ar-CO-]d

             (II)     -[(OCHR3-CHR4)b-O-OC-sAr-CO-]e

             (III)     -[(OCHR5-CHR6)c-OR7]f

    wherein:
    • a, b and c are from 1 to 200;
    • d, e and f are from 1 to 50;
    • Ar is a 1,4-substituted phenylene;
    • sAr is 1,3-substituted phenylene substituted in position 5 with SO3Me;
    • Me is Li, K, Mg/2, Ca/2, Al/3, ammonium, mono-, di-, tri-, or tetraalkylammonium wherein the alkyl groups are C1-C18 alkyl or C2-C10 hydroxyalkyl, or mixtures thereof;
    • R1, R2, R3, R4, R5 and R6 are independently selected from H or C1-C18 n- or iso-alkyl; and
    • R7 is a linear or branched C1-C18 alkyl, or a linear or branched C2-C30 alkenyl, or a cycloalkyl group with 5 to 9 carbon atoms, or a C8-C30 aryl group, or a C6-C30 arylalkyl group.
      Suitable soil release polymers are sold by Clariant under the TexCare® series of polymers, e.g. TexCare® SRN240 and TexCare® SRA300. Other suitable soil release polymers are sold by Solvay under the Repel-o-Tex® series of polymers, e.g. Repel-o-Tex® SF2 and Repel-o-Tex® Crystal.
  • Anti-redeposition polymer: Suitable anti-redeposition polymers include polyethylene glycol polymers and/or polyethyleneimine polymers.
  • Suitable polyethylene glycol polymers include random graft co-polymers comprising: (i) hydrophilic backbone comprising polyethylene glycol; and (ii) hydrophobic side chain(s) selected from the group consisting of: C4-C25 alkyl group, polypropylene, polybutylene, vinyl ester of a saturated C1-C6 mono-carboxylic acid, C1-C6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof. Suitable polyethylene glycol polymers have a polyethylene glycol backbone with random grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone can be in the range of from 2,000 Da to 20,000 Da, or from 4,000 Da to 8,000 Da. The molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can be in the range of from 1:1 to 1:5, or from 1:1.2 to 1:2. The average number of graft sites per ethylene oxide units can be less than 1, or less than 0.8, the average number of graft sites per ethylene oxide units can be in the range of from 0.5 to 0.9, or the average number of graft sites per ethylene oxide units can be in the range of from 0.1 to 0.5, or from 0.2 to 0.4. A suitable polyethylene glycol polymer is Sokalan HP22. Suitable polyethylene glycol polymers are described in WO08/007320 .
  • Cellulosic polymer: Suitable cellulosic polymers are selected from alkyl cellulose, alkyl alkoxyalkyl cellulose, carboxyalkyl cellulose, alkyl carboxyalkyl cellulose, sulphoalkyl cellulose, more preferably selected from carboxymethyl cellulose, methyl cellulose, methyl hydroxyethyl cellulose, methyl carboxymethyl cellulose, and mixures thereof.
  • Suitable carboxymethyl celluloses have a degree of carboxymethyl substitution from 0.5 to 0.9 and a molecular weight from 100,000 Da to 300,000 Da.
    Suitable carboxymethyl celluloses have a degree of substitution greater than 0.65 and a degree of blockiness greater than 0.45, e.g. as described in WO09/154933 .
  • Care polymers: Suitable care polymers include cellulosic polymers that are cationically modified and/or hydrophobically modified. Such modified cellulosic polymers can provide anti-abrasion benefits and dye lock benefits to fabric during the laundering cycle. Suitable cellulosic polymers include cationically modified hydroxyethyl cellulose. Suitable care polymers also include guar polymers that are cationically and/or hydrophobically modified. Other suitable care polymers include dye lock polymers, for example the condensation oligomer produced by the condensation of imidazole and epichlorhydrin, preferably in ratio of 1:4:1. A suitable commercially available dye lock polymer is Polyquart® FDI (Cognis).
  • Other suitable care polymers include amino-silicone, which can provide fabric feel benefits and fabric shape retention benefits.
  • Alkoxylated polyalkyleneimine: The composition may comprise an alkoxylated polyalkyleneimine, wherein said alkoxylated polyalkyleneimine has a polyalkyleneimine core with one or more side chains bonded to at least one nitrogen atom in the polyalkyleneimine core, wherein said alkoxylated polyalkyleneimine has an empirical formula (I) of (PEI)a-(EO)b-R1, wherein a is the average number-average molecular weight (MWPEI) of the polyalkyleneimine core of the alkoxylated polyalkyleneimine and is in the range of from 100 to 100,000 Daltons, wherein b is the average degree of ethoxylation in said one or more side chains of the alkoxylated polyalkyleneimine and is in the range of from 5 to 40, and wherein R1 is independently selected from the group consisting of hydrogen, C1-C4 alkyls, and combinations thereof.
  • The composition may comprise an alkoxylated polyalkyleneimine, wherein said alkoxylated polyalkyleneimine has a polyalkyleneimine core with one or more side chains bonded to at least one nitrogen atom in the polyalkyleneimine core, wherein the alkoxylated polyalkyleneimine has an empirical formula (II) of (PEI)o-(EO)m(PO)n-R2 or (PEI)o-(PO)n(EO)m-R2, wherein o is the average number-average molecular weight (MWPEI) of the polyalkyleneimine core of the alkoxylated polyalkyleneimine and is in the range of from 100 to 100,000 Daltons, wherein m is the average degree of ethoxylation in said one or more side chains of the alkoxylated polyalkyleneimine which ranges from 10 to 50, wherein n is the average degree of propoxylation in said one or more side chains of the alkoxylated polyalkyleneimine which ranges from 1 to 50, and wherein R2 is independently selected from the group consisting of hydrogen, C1-C4 alkyls, and combinations thereof.
  • Bleach: Suitable bleach includes sources of hydrogen peroxide, bleach activators, bleach catalysts, pre-formed peracids and any combination thereof. A particularly suitable bleach includes a combination of a source of hydrogen peroxide with a bleach activator and/or a bleach catalyst.
  • Source of hydrogen peroxide: Suitable sources of hydrogen peroxide include sodium perborate and/or sodium percarbonate.
  • Bleach activator: Suitable bleach activators include tetra acetyl ethylene diamine and/or alkyl oxybenzene sulphonate.
  • Bleach catalyst: The composition may comprise a bleach catalyst. Suitable bleach catalysts include oxaziridinium bleach catalysts, transistion metal bleach catalysts, especially manganese and iron bleach catalysts. A suitable bleach catalyst has a structure corresponding to general formula below:
    Figure imgb0012
    wherein R13 is selected from the group consisting of 2-ethylhexyl, 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, n-dodecyl, n-tetradecyl, n-hexadecyl, n-octadecyl, iso-nonyl, isodecyl, iso-tridecyl and iso-pentadecyl.
  • Pre-formed peracid: Suitable pre-form peracids include phthalimido-peroxycaproic acid. However, it is preferred that the composition is substantially free of pre-formed peracid. By: "substantially free" it is meant: "no deliberately added".
  • Enzymes: Suitable enzymes include lipases, proteases, cellulases, amylases and any combination thereof.
  • Protease: Suitable proteases include metalloproteases and/or serine proteases. Examples of suitable neutral or alkaline proteases include: subtilisins (EC 3.4.21.62); trypsin-type or chymotrypsin-type proteases; and metalloproteases. The suitable proteases include chemically or genetically modified mutants of the aforementioned suitable proteases.
  • Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Savinase®, Primase®, Durazym®, Polarzyme®, Kannase®, Liquanase®, Liquanase Ultra@, Savinase Ultra@, Ovozyme®, Neutrase®, Everlase® and Esperase® by Novozymes A/S (Denmark), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Preferenz P® series of proteases including Preferenz® P280, Preferenz® P281, Preferenz® P2018-C, Preferenz® P2081-WE, Preferenz® P2082-EE and Preferenz® P2083-A/J, Properase®, Purafect®, Purafect Prime®, Purafect Ox®, FN3®, FN4®, Excellase® and Purafect OXP® by DuPont, those sold under the tradename Opticlean® and Optimase® by Solvay Enzymes, those available from Henkel/ Kemira, namely BLAP (sequence shown in Figure 29 of US 5,352,604 with the folowing mutations S99D + S101 R + S103A + V104I + G159S, hereinafter referred to as BLAP), BLAP R (BLAP with S3T + V4I + V199M + V205I + L217D), BLAP X (BLAP with S3T + V4I + V205I) and BLAP F49 (BLAP with S3T + V4I + A194P + V199M + V205I + L217D) - all from Henkel/Kemira; and KAP (Bacillus alkalophilus subtilisin with mutations A230V + S256G + S259N) from Kao.
  • A suitable protease is described in WO11/140316 and WO11/072117 .
  • Amylase: Suitable amylases are derived from AA560 alpha amylase endogenous to Bacillus sp. DSM 12649, preferably having the following mutations: R118K, D183*, G184*, N195F, R320K, and/or R458K. Suitable commercially available amylases include Stainzyme®, Stainzyme® Plus, Natalase, Termamyl®, Termamyl® Ultra, Liquezyme® SZ, Duramyl®, Everest® (all Novozymes) and Spezyme® AA, Preferenz S® series of amylases, Purastar® and Purastar® Ox Am, Optisize® HT Plus (all Du Pont).
    A suitable amylase is described in WO06/002643 .
  • Cellulase: Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are also suitable. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum.
  • Commercially available cellulases include Celluzyme®, Carezyme®, and Carezyme® Premium, Celluclean® and Whitezyme® (Novozymes A/S), Revitalenz® series of enzymes (Du Pont), and Biotouch® series of enzymes (AB Enzymes). Suitable commercially available cellulases include Carezyme® Premium, Celluclean® Classic. Suitable cellulases are described in WO07/144857 and WO10/056652 .
  • Lipase: Suitable lipases include those of bacterial, fungal or synthetic origin, and variants thereof. Chemically modified or protein engineered mutants are also suitable. Examples of suitable lipases include lipases from Humicola (synonym Thermomyces), e.g., from H. lanuginosa (T. lanuginosus).
  • The lipase may be a "first cycle lipase", e.g. such as those described in WO06/090335 and WO13/116261 . In one aspect, the lipase is a first-wash lipase, preferably a variant of the wild-type lipase from Thermomyces lanuginosus comprising T231R and/or N233R mutations. Preferred lipases include those sold under the tradenames Lipex®, Lipolex® and Lipoclean® by Novozymes, Bagsvaerd, Denmark.
  • Other suitable lipases include: Liprl 139, e.g. as described in WO2013/171241 ; and TfuLip2, e.g. as described in WO2011/084412 and WO2013/033318 .
  • Other enzymes: Other suitable enzymes are bleaching enzymes, such as peroxidases/oxidases, which include those of plant, bacterial or fungal origin and variants thereof. Commercially available peroxidases include Guardzyme® (Novozymes A/S). Other suitable enzymes include choline oxidases and perhydrolases such as those used in Gentle Power Bleach.
  • Other suitable enzymes include pectate lyases sold under the tradenames X-Pect®, Pectaway® (from Novozymes A/S, Bagsvaerd, Denmark) and PrimaGreen® (DuPont) and mannanases sold under the tradenames Mannaway® (Novozymes A/S, Bagsvaerd, Denmark), and Mannastar® (Du Pont).
  • Identity: When used herein identity or sequence identity refers to the relatedness between two amino acid sequences.
  • For purposes of the present invention, the degree of sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 3.0.0 or later. The optional parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled "longest identity" (obtained using the -nobrief option) is used as the percent identity and is calculated as follows: Identical Residues × 100 / Length of Alignment Total Number of Gaps in Alignment .
    Figure imgb0013
  • Brightener: Suitable fluorescent brighteners include: di-styryl biphenyl compounds, e.g. Tinopal® CBS-X, di-amino stilbene di-sulfonic acid compounds, e.g. Tinopal® DMS pure Xtra and Blankophor® HRH, and Pyrazoline compounds, e.g. Blankophor® SN, and coumarin compounds, e.g. Tinopal® SWN.
    Preferred brighteners are: sodium 2 (4-styryl-3-sulfophenyl)-2H-napthol[1,2-d]triazole, disodium 4,4'-bis{[(4-anilino-6-(N methyl-N-2hydroxyethyl)amino 1 ,3,5- triazin-2-yl)]amino}stilbene-2-2' disulfonate, disodium 4,4'-bis{[(4-anilino-6-morpholino-1,3,5-triazin-2-yl)]amino} stilbene-2-2' disulfonate, and disodium 4,4'- bis(2-sulfostyryl)biphenyl. A suitable fluorescent brightener is C.I. Fluorescent Brightener 260, which may be used in its beta or alpha crystalline forms, or a mixture of these forms.
  • Hueing agent: Suitable hueing agents include small molecule dyes, typically falling into the Colour Index (C.I.) classifications of Acid, Direct, Basic, Reactive (including hydrolysed forms thereof) or Solvent or Disperse dyes, for example classified as Blue, Violet, Red, Green or Black, and provide the desired shade either alone or in combination. Preferred such hueing agents include Acid Violet 50, Direct Violet 9, 66 and 99, Solvent Violet 13 and any combination thereof.
  • Many hueing agents are known and described in the art which may be suitable for the present invention, such as hueing agents described in WO2014/089386 .
  • Suitable hueing agents include phthalocyanine and azo dye conjugates, such as described in WO2009/069077 .
  • Suitable hueing agents may be alkoxylated. Such alkoxylated compounds may be produced by organic synthesis that may produce a mixture of molecules having different degrees of alkoxylation. Such mixtures may be used directly to provide the hueing agent, or may undergo a purification step to increase the proportion of the target molecule. Suitable hueing agents include alkoxylated bis-azo dyes, such as described in WO2012/054835 , and/or alkoxylated thiophene azo dyes, such as described in WO2008/087497 and WO2012/166768 .
  • The hueing agent may be incorporated into the detergent composition as part of a reaction mixture which is the result of the organic synthesis for a dye molecule, with optional purification step(s). Such reaction mixtures generally comprise the dye molecule itself and in addition may comprise un-reacted starting materials and/or by-products of the organic synthesis route. Suitable hueing agents can be incorporated into hueing dye particles, such as described in WO 2009/069077 .
  • Reserve alkalinity: Typically, the composition at 1wt% dilution in deionized water at 20°C, has a reserve alkalinity to pH 7.5 of less than 3.0gNaOH/100g, preferably less than 2.5gNaOH/100g, or even less than 2.0gNaOH/100g.
  • As used herein, the term "reserve alkalinity" is a measure of the buffering capacity of the detergent composition (g/NaOH/100g detergent composition) determined by titrating a 1% (w/v) solution of detergent composition with hydrochloric acid to pH 7.5 i.e. in order to calculate Reserve Alkalinity as defined herein: Reserve Alkalinity to pH 7.5 as % alkali in g NaOH / 100 g product = T × M × 40 × Vol 10 × Wt × Aliquot
    Figure imgb0014
    • T = titre (ml) to pH 7.5
    • M = Molarity of HCl = 0.2
    • 40 = Molecular weight of NaOH
    • Vol = Total volume (ie. 1000 ml)
    • W = Weight of product (10 g)
    • Aliquot = (100 ml)
  • Obtain a 10g sample accurately weighed to two decimal places, of fully formulated detergent composition. The sample should be obtained using a Pascall sampler in a dust cabinet. Add the 10g sample to a plastic beaker and add 200 ml of carbon dioxide-free de-ionised water. Agitate using a magnetic stirrer on a stirring plate at 150 rpm until fully dissolved and for at least 15 minutes. Transfer the contents of the beaker to a 1 litre volumetric flask and make up to 1 litre with deionised water. Mix well and take a 100 mls ± 1 ml aliquot using a 100 mls pipette immediately. Measure and record the pH and temperature of the sample using a pH meter capable of reading to ±0.01pH units, with stirring, ensuring temperature is 20°C +/- 2°C. Titrate whilst stirring with 0.2M hydrochloric acid until pH measures exactly 7.5. Note the millilitres of hydrochloric acid used. Take the average titre of three identical repeats. Carry out the calculation described above to calculate the reserve alkalinity to pH 7.5.
  • EXAMPLES Illustrative Example
  • Ingredient Amount (in wt%)
    Anionic detersive surfactant (such as alkyl benzene sulphonate, alkyl ethoxylated sulphate, alkyl ether carboxylic acid, and mixtures thereof) from 15wt% to 35wt%
    Non-ionic detersive surfactant (such as alkyl ethoxylated alcohol) from 0.1wt% to 5wt%
    Carboxylate polymer (such as co-polymers of maleic acid and acrylic acid and/or carboxylate polymers comprising ether moieties and sulfonate moieties) from 0wt% to 4wt%
    Polyethylene glycol polymer (such as a polyethylene glycol polymer comprising polyvinyl acetate side chains) from 0wt% to 4wt%
    Polyester soil release polymer (such as Repel-o-tex and/or Texcare polymers) from 0wt% to 2wt%
    Cellulosic polymer (such as carboxymethyl cellulose, methyl cellulose and combinations thereof) from 0wt% to 2wt%
    Other polymer (such as care polymers) from 0wt% to 4wt%
    Citric acid and/or sodium citrate from 10wt% to 40wt%
    Inorganic salts (such as sodium carbonate, sodium sesquicarbonate, sodium bicarbonate and combinations thereof) from 10wt% to 40wt%
    Amino acid derivative complexing agent (such as MGDA, GLDA, ASDA and combination thereof) from 0.1wt% to 40wt%
    Dye transfer inhibitor polymer (such as polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones, polyvinylimidazoles, and any combination thereof) from 0.01wt% to 20wt%
    Amylase from 0.001wt% to 0.1wt%
    Metalloprotease (such as a M4 metalloprotease) from 0.001wt% to
    0.1wt%
    Lipase from 0.001wt% to 0.1wt%
    Cellulase from 0wt% to 0.1wt%
    Pectate Lyase from 0wt% to 0.1wt%
    Mannanase from 0wt% to 0.1wt%
    Subtilisin-type protease from 0wt% to 0.1wt%
    Fluorescent brightener from 0wt% to 1.0wt%
    Alkoxylated polyaryl/polyalkyl phenol from 0.5wt% to 20wt%
    Hueing dye from 0.001wt% to 0.5wt%
    Organic pigment and/or inorganic pigment from 0.001wt% to 0.5wt%
    Other ingredients & miscellaneous balance to 100wt%
  • The dimensions and values disclosed herein are not to be understood as being strictly limited to the exact numerical values recited. Instead, unless otherwise specified, 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."
    Figure imgb0015
    Figure imgb0016
    Figure imgb0017
    Figure imgb0018
    Figure imgb0019
    Figure imgb0020
    Figure imgb0021
  • Claims (17)

    1. A solid laundry detergent composition comprising:
      (a) from 20wt% to 39wt% detersive surfactant selected from anionic detersive surfactant and/or non-ionic detersive surfactant;
      (b) from 10wt% to 40wt% inorganic salts selected from sodium carbonate, sodium sesquicarbonate, sodium bicarbonate and any mixtures thereof;
      (c) optionally, from 10wt% to 40wt% citric acid and/or salts thereof;
      (d) from 0.01wt% to 20wt% dye transfer inhibitor (DTI) polymer selected from polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones, polyvinylimidazoles, and any combination thereof,
      wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a pH in the range of from 7.6 to 10.0;
      wherein at 1wt% dilution in de-ionised water at 20°C, the composition has a reserve alkalinity to pH 7.5 of greater than 3.0,
      wherein the composition is in the form of a coated laundry detergent particle that is curved and has perpendicular dimensions x, y and z,
      wherein x is from 0.5mm to 2.0mm,
      wherein y is from 2.0mm to 8.0mm, and
      wherein z is from 2.0mm to 8.0mm,
      wherein the coating comprises the inorganic salt (b), and wherein the core comprises the detersive surfactant (a).
    2. A composition according to claim 1, wherein the composition comprises from 0.001wt% to 1.0wt% metalloprotease enzyme.
    3. A composition according to any preceding claim, wherein the composition comprises from 0.001wt% to 1.0wt% lipase that is a variant of SEQ ID NO:2 comprising:
      (3)(a) substitutions T231R and N233R
      and
      (3)(b) at least three further substitutions selected from D27R, N33Q, G38A, D96E, D111A, G91Q, G163K, E210Q, D254S, I255A, and P256T;
      where the positions correspond to the positions of SEQ ID NO 2 and wherein the lipase variant has at least 95% but less than 100% sequence identity to the polypeptide having the amino acid sequence of SEQ ID NO: 2 and wherein the variant has lipase activity.
    4. A composition according to any preceding claim, wherein the composition comprises from 0.1wt% to 40wt% amino acid derivative complexing agent selected from one or more of the following, in any stereoisomer or mixture of stereoisomer form:
      (4)(i) methylglycinediacetic acid and salts thereof (MGDA)
      Figure imgb0022
      (4)(ii) L-glutamic acid, N,N-diacetic acid and salts thereof (GLDA)
      Figure imgb0023
      and
      (4)(iii) L-aspartic acid N,N-diacetic acid and salts thereof (ASDA)
      Figure imgb0024
    5. A composition according to any preceding claim, wherein the composition comprises from 0.001wt% to 1.0wt% amylase variant comprising:
      (5)(i) a deletion and/or a substitution at two or more positions corresponding to positions R181 , G182, H183 and G184 of the mature polypeptide of SEQ ID NO: 1 , and
      (5)(ii) a substitution at one or more positions said substitutions selected from the group consisting of:
      I206Y;F;Q;P;R;V;C;G;A;C;D;E;H;K;L;M;N;S;T, particularly I206Y;F;C;L;H;S,
      N195F;Y;H;K;L,
      L63Q;P;R;V;F;C;G;A;C;D;E;H;K;I;M;N;S;T;Y, particularly L63V,
      A113M;R;W;I;L,
      M116F;Y;I;W;L,
      R118P;Q;V;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly R118P;Q;V;F;C;G,
      N128C,
      Q129P;R;V;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly Q129E,
      G133N,
      A139Q;P;R;V;F;C;G;C;D;E;H;I;K;L;M;N;S;T;Y, particularly A139T,
      R142H;V;L;Q;I,
      A186E;N;Q;S,
      E190P;R;V;F;C;G;A;C;D;Q;H;I;K;L;M;N;S;T;Y, particularly E190P,
      A204Q;P;R;V;F;C;G;C;D;E;H;I;K;L;M;N;S;T;Y, particularly A204T,
      H210M;D;C;A;Q;S;F;N;E;T,
      P211Q;R;V;F;C;G;A;C;D;E;H;1;K;L;M;N;S;T;Y, particularly
      P211L;M;S;Q;G;V;W;A;H;T;R;
      E212T;R;S;V;L;Y;R;T;G;
      V213Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly V213T;A;G;S;C;L;P,
      V214Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;Y, particularly V214T;I,
      L217M;Q;V;I;H, particularly L217V,
      Y243Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;S;T;V, particularly Y243F,
      S244Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;Y;T;V, particularly S244Q,
      T246Q;P;R;F;C;G;A;C;D;E;H;I;K;L;M;N;Y;S;V, particularly T246Q;M,
      N260E, Q280S, N311R, F343W, D418C, S419M, S420Q;R and Y482W,
      where the positions correspond to the positions of SEQ ID NO 1 and wherein the amylase variant has at least 95%, such as at least 96%, or at least 97%, or at least 98%, or at least 99% but less than 100% sequence identity to the polypeptide having the amino acid sequence of SEQ ID NO: 1 and wherein the variant has alpha-amylase activity.
    6. A composition according to any preceding claim, wherein the composition comprises a metalloprotease enzyme that is selected from the M4 Metalloprotease Family.
    7. A composition according to any preceding claim, wherein the composition comprises from 0.5wt% to 20wt% alkoxylated polyaryl/polyalkyl phenol has the following structure:
      Figure imgb0025
      wherein R1 is selected from linear of branched C3-C15 alkyl groups and aryl groups, X is selected from ethoxy or propoxy groups, n is from 2 to 70, T is selected from H, SO3 -, COO- and PO3 2-.
    8. A composition according to any preceding claim, wherein the composition comprises from 0.5wt% to 20wt% alkyl ether carboxylic acid having the following structure:

               R-(OCH2CH2)n-OCH2-COOH

      wherein,
      R is selected from saturated and mono-unsaturated C10 to C26 linear or branched alkyl chains, and
      n is selected from 5 to 20.
    9. A composition according to any preceding claim, wherein the detersive surfactant comprises from C8-C24 alkyl ethoxylated alcohol having an average degree of ethoxylation of from 20 to 50, and wherein the compositon comprises from 1wt% to 10wt% C8-C24 alkyl ethoxylated alcohol having an average degree of ethoxylation of from 20 to 50.
    10. A composition according to any preceding claim, wherein the composition comprises from 0.05wt% to 4.0wt% soil release polymer.
    11. A composition according to any preceding claim, wherein the composition comprises from 0.1wt% to 3.0wt% carboxymethylcellulose (CMC).
    12. A composition according to any preceding claim, wherein the composition comprises from 0.1wt% to 5.0wt% calcite.
    13. A composition according to any preceding claim, wherein the composition comprises from 1wt% to 10wt% carboxylate polymer.
    14. A composition according to any preceding claim, wherein the composition comprises less than 10wt% total level of silicates and aluminosilicates.
    15. A composition according to any preceding claim, wherein the composition comprises from 0.001wt% to 0.5wt% hueing dye.
    16. A composition according to any preceding claim, wherein the composition comprises from 0.001wt% to 0.5wt% organic pigment and/or inorganic pigment.
    17. A composition according to any preceding claim, wherein the composition comprises from 0.2 wt% to 10wt% chelant.
    EP17173007.0A 2016-12-22 2017-05-26 Laundry detergent composition Withdrawn EP3339419A1 (en)

    Priority Applications (1)

    Application Number Priority Date Filing Date Title
    EP16206503 2016-12-22

    Applications Claiming Priority (7)

    Application Number Priority Date Filing Date Title
    PCT/US2017/067156 WO2018118824A1 (en) 2016-12-22 2017-12-19 Laundry detergent composition
    PCT/CN2017/117072 WO2018113643A1 (en) 2016-12-22 2017-12-19 Laundry detergent composition
    PCT/US2017/067157 WO2018118825A1 (en) 2016-12-22 2017-12-19 Laundry detergent composition
    PCT/CN2017/117078 WO2018113646A1 (en) 2016-12-22 2017-12-19 Laundry detergent composition
    PCT/CN2017/117074 WO2018113645A1 (en) 2016-12-22 2017-12-19 Laundry detergent composition
    EP17208549.0A EP3339422A1 (en) 2016-12-22 2017-12-19 Laundry detergent composition
    PCT/CN2017/117073 WO2018113644A1 (en) 2016-12-22 2017-12-19 Laundry detergent composition

    Publications (1)

    Publication Number Publication Date
    EP3339419A1 true EP3339419A1 (en) 2018-06-27

    Family

    ID=57609736

    Family Applications (1)

    Application Number Title Priority Date Filing Date
    EP17173007.0A Withdrawn EP3339419A1 (en) 2016-12-22 2017-05-26 Laundry detergent composition

    Country Status (1)

    Country Link
    EP (1) EP3339419A1 (en)

    Citations (30)

    * Cited by examiner, † Cited by third party
    Publication number Priority date Publication date Assignee Title
    US5352604A (en) 1989-08-25 1994-10-04 Henkel Research Corporation Alkaline proteolytic enzyme and method of production
    US5776879A (en) * 1997-09-19 1998-07-07 Isp Investments Inc. Water soluble dye complexing polymers
    WO2000040691A1 (en) * 1999-01-06 2000-07-13 The Procter & Gamble Company Laundry detergent bar composition
    WO2006002643A2 (en) 2004-07-05 2006-01-12 Novozymes A/S Alpha-amylase variants with altered properties
    WO2006090335A1 (en) 2005-02-22 2006-08-31 The Procter & Gamble Company Detergent compositions
    WO2007044993A2 (en) 2005-10-12 2007-04-19 Genencor International, Inc. Use and production of storage-stable neutral metalloprotease
    WO2007144857A1 (en) 2006-06-16 2007-12-21 The Procter & Gamble Company Detergent compositions
    WO2008007320A2 (en) 2006-07-07 2008-01-17 The Procter & Gamble Company Detergent compositions
    WO2008087497A1 (en) 2007-01-19 2008-07-24 The Procter & Gamble Company Laundry care composition comprising a whitening agent for cellulosic substrates
    WO2009058661A1 (en) 2007-10-31 2009-05-07 Danisco Us Inc., Genencor Division Use and production of citrate-stable neutral metalloproteases
    WO2009069077A2 (en) 2007-11-26 2009-06-04 The Procter & Gamble Company Detergent compositions
    WO2009154933A2 (en) 2008-06-20 2009-12-23 The Procter & Gamble Company Laundry composition
    WO2010056652A1 (en) 2008-11-14 2010-05-20 The Procter & Gamble Company Composition comprising polymer and enzyme
    WO2010122050A2 (en) 2009-04-24 2010-10-28 Unilever Plc Manufacture of high active detergent particles
    WO2011072117A1 (en) 2009-12-09 2011-06-16 The Procter & Gamble Company Fabric and home care products
    WO2011084412A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing thermobifida fusca lipase and methods of use thereof
    WO2011140316A1 (en) 2010-05-06 2011-11-10 The Procter & Gamble Company Consumer products with protease variants
    WO2012054835A1 (en) 2010-10-22 2012-04-26 The Procter & Gamble Company Bis-azo colorants for use as bluing agents
    WO2012166768A1 (en) 2011-06-03 2012-12-06 The Procter & Gamble Company Laundry care compositions containing dyes
    WO2013033318A1 (en) 2011-08-31 2013-03-07 Danisco Us Inc. Compositions and methods comprising a lipolytic enzyme variant
    WO2013116261A2 (en) 2012-02-03 2013-08-08 The Procter & Gamble Company Compositions and methods for surface treatment with lipases
    WO2013139702A1 (en) * 2012-03-21 2013-09-26 Unilever Plc Laundry detergent particles
    WO2013171241A1 (en) 2012-05-16 2013-11-21 Novozymes A/S Compositions comprising lipase and methods of use thereof
    WO2014071410A1 (en) 2012-11-05 2014-05-08 Danisco Us Inc. Compositions and methods comprising thermolysin protease variants
    WO2014089386A1 (en) 2012-12-06 2014-06-12 The Procter & Gamble Company Soluble pouch comprising hueing dye
    WO2015158723A1 (en) * 2014-04-14 2015-10-22 Novozymes A/S Metalloprotease from chryseobacterium
    WO2015189371A1 (en) * 2014-06-12 2015-12-17 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
    WO2016041681A1 (en) * 2014-09-19 2016-03-24 Basf Se Detergent composition
    WO2016041679A1 (en) * 2014-09-18 2016-03-24 Unilever Plc Whitening composition
    WO2016102356A1 (en) * 2014-12-22 2016-06-30 Novozymes A/S Detergent compositions, lipase variants and polynucleotides encoding same

    Patent Citations (32)

    * Cited by examiner, † Cited by third party
    Publication number Priority date Publication date Assignee Title
    US5352604A (en) 1989-08-25 1994-10-04 Henkel Research Corporation Alkaline proteolytic enzyme and method of production
    US5776879A (en) * 1997-09-19 1998-07-07 Isp Investments Inc. Water soluble dye complexing polymers
    WO2000040691A1 (en) * 1999-01-06 2000-07-13 The Procter & Gamble Company Laundry detergent bar composition
    WO2006002643A2 (en) 2004-07-05 2006-01-12 Novozymes A/S Alpha-amylase variants with altered properties
    WO2006090335A1 (en) 2005-02-22 2006-08-31 The Procter & Gamble Company Detergent compositions
    US20080293610A1 (en) 2005-10-12 2008-11-27 Andrew Shaw Use and production of storage-stable neutral metalloprotease
    WO2007044993A2 (en) 2005-10-12 2007-04-19 Genencor International, Inc. Use and production of storage-stable neutral metalloprotease
    WO2007144857A1 (en) 2006-06-16 2007-12-21 The Procter & Gamble Company Detergent compositions
    WO2008007320A2 (en) 2006-07-07 2008-01-17 The Procter & Gamble Company Detergent compositions
    WO2008087497A1 (en) 2007-01-19 2008-07-24 The Procter & Gamble Company Laundry care composition comprising a whitening agent for cellulosic substrates
    WO2009058661A1 (en) 2007-10-31 2009-05-07 Danisco Us Inc., Genencor Division Use and production of citrate-stable neutral metalloproteases
    US20140315775A1 (en) 2007-10-31 2014-10-23 Danisco Us Inc. Use and production of citrate-stable neutral metalloproteases
    WO2009069077A2 (en) 2007-11-26 2009-06-04 The Procter & Gamble Company Detergent compositions
    WO2009154933A2 (en) 2008-06-20 2009-12-23 The Procter & Gamble Company Laundry composition
    WO2010056652A1 (en) 2008-11-14 2010-05-20 The Procter & Gamble Company Composition comprising polymer and enzyme
    WO2010122050A2 (en) 2009-04-24 2010-10-28 Unilever Plc Manufacture of high active detergent particles
    WO2011072117A1 (en) 2009-12-09 2011-06-16 The Procter & Gamble Company Fabric and home care products
    WO2011084412A1 (en) 2009-12-21 2011-07-14 Danisco Us Inc. Detergent compositions containing thermobifida fusca lipase and methods of use thereof
    WO2011140316A1 (en) 2010-05-06 2011-11-10 The Procter & Gamble Company Consumer products with protease variants
    WO2012054835A1 (en) 2010-10-22 2012-04-26 The Procter & Gamble Company Bis-azo colorants for use as bluing agents
    WO2012166768A1 (en) 2011-06-03 2012-12-06 The Procter & Gamble Company Laundry care compositions containing dyes
    WO2013033318A1 (en) 2011-08-31 2013-03-07 Danisco Us Inc. Compositions and methods comprising a lipolytic enzyme variant
    WO2013116261A2 (en) 2012-02-03 2013-08-08 The Procter & Gamble Company Compositions and methods for surface treatment with lipases
    WO2013139702A1 (en) * 2012-03-21 2013-09-26 Unilever Plc Laundry detergent particles
    WO2013171241A1 (en) 2012-05-16 2013-11-21 Novozymes A/S Compositions comprising lipase and methods of use thereof
    WO2014071410A1 (en) 2012-11-05 2014-05-08 Danisco Us Inc. Compositions and methods comprising thermolysin protease variants
    WO2014089386A1 (en) 2012-12-06 2014-06-12 The Procter & Gamble Company Soluble pouch comprising hueing dye
    WO2015158723A1 (en) * 2014-04-14 2015-10-22 Novozymes A/S Metalloprotease from chryseobacterium
    WO2015189371A1 (en) * 2014-06-12 2015-12-17 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
    WO2016041679A1 (en) * 2014-09-18 2016-03-24 Unilever Plc Whitening composition
    WO2016041681A1 (en) * 2014-09-19 2016-03-24 Basf Se Detergent composition
    WO2016102356A1 (en) * 2014-12-22 2016-06-30 Novozymes A/S Detergent compositions, lipase variants and polynucleotides encoding same

    Non-Patent Citations (2)

    * Cited by examiner, † Cited by third party
    Title
    NEEDLEMAN; WUNSCH, J. MOL. BIOL., vol. 48, 1970, pages 443 - 453
    RICE ET AL.: "EMBOSS: The European Molecular Biology Open Software Suite", TRENDS GENET., vol. 16, 2000, pages 276 - 277, XP004200114, DOI: doi:10.1016/S0168-9525(00)02024-2

    Similar Documents

    Publication Publication Date Title
    EP2705146B1 (en) Compositions and methods comprising serine protease variants
    JP5947213B2 (en) The use of protease variants
    JP6234960B2 (en) Cleaning composition comprising amylase variants with high stability in the presence of a chelating agent
    US10323217B2 (en) Detergent composition comprising enzymes and washing method for preventing adhesion of bacteria
    EP1904628B1 (en) Subtilase variants
    CN103180424B (en) Comprising a bluing agent and a clay soil removal / anti-redeposition agent Detergent compositions
    JP6185243B2 (en) High stability mutants and variants containing composition in the presence of a chelating agent
    US20160208198A1 (en) Automatic dishwashing detergent composition
    US8466098B2 (en) Washing agent having stabilized enzymes
    US9163226B2 (en) Storage-stable liquid washing or cleaning agent containing proteases
    RU2546834C2 (en) Detergent composition
    WO2011036264A1 (en) Use of protease variants
    WO2011076897A1 (en) Use of amylase variants at low temperature
    CN103397010A (en) Subtilase variants
    JP2015525248A (en) Compositions and methods of use thereof comprising lipase
    WO2009030632A1 (en) Polycyclic compounds as enzyme stabilizers
    JP2019059960A (en) Detergent composition
    CN102471738B (en) Comprising phthalimido peroxy caproic acid mild alkaline low-built solid detergent compositions the fabric treatment
    US20110136720A1 (en) Method for improving the cleaning action of a detergent or cleaning agent
    ES2419234T3 (en) detergent compositions and use of combinations of enzymes therein
    US8809251B2 (en) Laundry detergent composition comprising water-soluble phthalocyanine compound
    ES2401126T3 (en) detergent composition
    RU2635921C2 (en) Visually contrasting aesthetic particles having improved solubility in water, especially useful for combining with powdered or granular compositions
    RU2614765C2 (en) Laundry detergents and cleansing compositions containing polymers with carboxyl groups
    JP2019503404A (en) Detergent composition comprising protease and amylase variants

    Legal Events

    Date Code Title Description
    AK Designated contracting states

    Kind code of ref document: A1

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

    AV Request for validation of the european patent

    Extension state: MA MD

    AX Request for extension of the european patent to:

    Extension state: BA ME

    18D Application deemed to be withdrawn

    Effective date: 20190103