EP4162018A1 - Procédé d'amélioration de l'activité protéase - Google Patents

Procédé d'amélioration de l'activité protéase

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Publication number
EP4162018A1
EP4162018A1 EP21728952.9A EP21728952A EP4162018A1 EP 4162018 A1 EP4162018 A1 EP 4162018A1 EP 21728952 A EP21728952 A EP 21728952A EP 4162018 A1 EP4162018 A1 EP 4162018A1
Authority
EP
European Patent Office
Prior art keywords
protease
detergent composition
saponin
use according
laundry detergent
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.)
Granted
Application number
EP21728952.9A
Other languages
German (de)
English (en)
Other versions
EP4162018B1 (fr
Inventor
Sarah Louise Hosking
Dietmar Andreas LANG
Mark Lawrence THOMPSON
Ian Malcolm TUCKER
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.)
Unilever Global IP Ltd
Unilever IP Holdings BV
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Unilever Global IP Ltd
Unilever IP Holdings BV
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Publication of EP4162018A1 publication Critical patent/EP4162018A1/fr
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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/382—Vegetable products, e.g. soya meal, wood flour, sawdust
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/3869—Enzyme enhancers or mediators

Definitions

  • the invention concerns a method, in particular a method relating to a detergent composition comprising a protease.
  • Protease enzymes are a useful ingredient for detergent formulations, particularly for laundry detergents. As with any ingredient, especially expensive ingredients, improvement of activity of the ingredient is a problem to be solved.
  • the present invention provides a method of improving protease activity in a detergent composition, said method involving incorporation of from 0.1 to 40 wt.%, preferably from 0.5 to 25 wt.%, more preferably from 0.5 to 20 wt.%, most preferably from 0.5 to 15 wt.%, of a saponin into said composition, wherein the detergent composition comprises from 0.0005 to 2.5 wt.%, preferably from 0.001 to 2 wt.%, more preferably from 0.005 to 1 wt.% of a protease enzyme; wherein the saponin has a triterpenoid backbone, and one or more sugar moieties attached to the triterpenoid backbone.
  • the method involves improving protease activity in a detergent composition, preferably in a home care detergent composition, more preferably a laundry detergent composition.
  • the invention provides the use of saponin to improve protease activity in a detergent composition preferably in a home care detergent composition, more preferably a laundry detergent composition, wherein the saponin has a triterpenoid backbone, and one or more sugar moieties attached to the triterpenoid backbone.
  • the protease is bacterial, fungal or mammalian in origin, more preferably bacterial or fungal in origin, most preferably bacterial in origin.
  • the protease is selected from the following group, serine, acidic, metallo- and cysteine proteases. More preferably the protease is a serine and/or acidic protease.
  • the protease is a serine protease. More preferably the serine protease is subtilisin type serine protease.
  • the saponin has at least two sugar moieties attached to the triterpenoid backbone.
  • the detergent composition comprises anionic and/or nonionic surfactant, more preferably the detergent composition comprises both anionic and nonionic surfactant.
  • a preferred detergent composition is a laundry detergent composition.
  • the laundry detergent composition is a liquid, gel or a powder, more preferably the detergent is a liquid detergent.
  • the laundry detergent preferably comprises from 0.1 to 8 wt.% of an alkoxylated polyamine.
  • the alkoxylated polyamine comprises an alkoxylated polyethylenimine, and/or alkoxylated polypropylenimine, more preferably the alkoxylation is ethoxylation or propoxylation or a mixture of both.
  • the laundry detergent composition preferably comprises from 0.1 to 8 wt.% of a soil release polymer, preferably a polyester soil release polymer.
  • Preferred detergent compositions particularly laundry detergent compositions additionally comprise a further enzyme selected from the group consisting of: lipases, cellulases, alpha- amylases, peroxidases/oxidases, pectate lyases, and/or mannanases.
  • a further enzyme selected from the group consisting of: lipases, cellulases, alpha- amylases, peroxidases/oxidases, pectate lyases, and/or mannanases.
  • Figure 1 graph showing the improvement effect of different saponins on protease activity and the beneficial effect of the sugar moieties present on the triterpenoid backbone.
  • FIG. 2 graph showing that the increased protease activity using saponin is also seen in scaled-up mini-bottle wash studies.
  • FIG. 3 graph showing that the increased protease activity using saponin is also seen across many different proteases.
  • FIG 4 graph showing that the increased protease activity using saponin is also seen using two different saponins in wash conditions (100ml).
  • indefinite article “a” or “an” and its corresponding definite article “the” as used herein means at least one, or one or more, unless specified otherwise.
  • the detergent composition may take any suitable form, for example liquids, solids (including powders) or gels.
  • the detergent composition can be applied to any suitable substrate, including but not limited to any substrate to which a home care composition would be applied, for example, textiles, crockery and cutlery.
  • Particularly preferred substrates are textiles.
  • Particularly preferred detergent compositions are laundry detergent compositions.
  • the laundry detergent composition is a liquid, gel or a powder, more preferably the detergent is a liquid detergent.
  • Laundry detergent compositions may take any suitable form. Preferred forms are liquid or powder, with liquid being most preferred.
  • the detergent composition used in the method or use comprises from 0.0005 to 2.5 wt.%, preferably from 0.001 to 2 wt.%, more preferably from 0.005 to 1 wt.% of a protease enzyme.
  • the protease can be derived from fungal, bacterial or mammalian sources.
  • the protease is bacterial, fungal or mammalian in origin, more preferably bacterial or fungal in origin, most preferably bacterial in origin.
  • the protease is selected from the following group, serine, acidic, metallo- and cysteine proteases. More preferably the protease is a serine and/or acidic protease.
  • the protease is a serine protease. More preferably the serine protease is subtilisin type serine protease.
  • proteases hydrolyse bonds within peptides and proteins, in the cleaning context this leads to enhanced removal of protein or peptide containing stains.
  • Serine proteases are preferred.
  • Subtilase type serine proteases are more preferred.
  • the term "subtilases” refers to a sub-group of serine protease according to Siezen et al. , Protein Engng. 4 (1991) 719- 737 and Siezen et al. Protein Science 6 (1997) 501 -523.
  • Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate.
  • the subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • subtilases are those derived from Bacillus species such as Bacillus lentus, B. licheniformis, B. alkalophilus, B. subtilis, B. amyloliquefaciens, B. pumilus and B. gibsonii described in; US7262042 and W009/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89/06279 and protease PD138 described in (WO 93/18140).
  • proteases may be those described in WO 92/175177, WO 01/016285, WO 02/026024 and WO 02/016547.
  • trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270, WO 94/25583 and WO 05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 05/052161 and WO 05/052146.
  • protease is a subtilisin protease (EC 3.4.21.62).
  • subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and W009/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279 and protease PD138 described in (WO93/18140).
  • the subsilisin is derived from Bacillus, preferably Bacillus lentus, B. alkalophilus, B. subtilis,
  • subtilisin is derived from Bacillus gibsonii or Bacillus Lentus.
  • Suitable commercially available protease enzymes include those sold under the trade names names Georgia, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Coronase®, Coronase® Ultra, Kannase®, Liquanase®, Liquanase® Ultra, all could be sold as Ultra® or Evity® (Novozymes A/S).
  • the detergent composition used in the method or use comprises from 0.1 to 40 wt.%, preferably from 0.25 to 30 wt.%, more preferably from 0.5 to 25 wt.%, more preferably from 0.5 to 20 wt.%, most preferably from 0.5 to 15 wt.%, of a saponin.
  • Saponins are natural compounds which contain sugar moieties bound to a fused system of non-aromatic 4, 5 and 6 membered rings.
  • the ring system are preferably selected from the groups of triterpenoids, for example lanostane, dammarane, lupane, oleanane, ursane and hopane.
  • triterpenoids for example lanostane, dammarane, lupane, oleanane, ursane and hopane.
  • An overview of these ring systems is provided in Natural Product Reports 27 (2010), 79-132 by R.A. Hill etal. Saponins are discussed in “Saponins Used in Food and Agriculture” Plenum Press, New York 1996, G. R. Waller and K. Yamasaki (eds).
  • Saponins are preferably extracted from the seed, root, leaf, bulb, fruit, stem, pericarp, bark, tuber or flower of a plant. Saponin extraction and quantification is discussed in Food Research International 59 (2014) 16-40 by R. Sulaiman ey al. Extraction of saponins from agricultural products is discussed in WO2017/019599 and W01999/053933.
  • Saponins may also be produced by bacteria (for example glycosylated hopanoids such as ribosylhopane) and marine organisms including sea cucumbers, starfish and sponges (Bahrami, Y., Zhang, W. & Franco, C.M. (2016) Marine Drugs 16: 423-453). Saponins may also be produced through biotechnology, either through enzymatic biosynthesis in vitro or by the engineering of microbial cell factories (Moses, T. et al. (2014) PNAS 28:1634-1639).
  • bacteria for example glycosylated hopanoids such as ribosylhopane
  • marine organisms including sea cucumbers, starfish and sponges
  • Saponins may also be produced through biotechnology, either through enzymatic biosynthesis in vitro or by the engineering of microbial cell factories (Moses, T. et al. (2014) PNAS 28:1634-1639).
  • the saponin is preferably a Tea saponin (for example preferably derived from Camellia species), Soapnut saponin (for example preferably derived from Sapindus species), Quillaja Bark saponin or Escin (for example preferably derived from Aesculus species).
  • the saponin has a structure comprising a triterpenoid backbone and one or more sugar moieties attached to the triterpenoid backbone.
  • Saponins are listed in the Chemical Entities of Biological Interest (ChEBI) database, (Hastings, J., de Matos, P., Dekker, A., Ennis, M., Harsha, B., Kale, N., Muthukrishnan, V., Owen, G., Turner, S., Williams, M., and Steinbeck, C. (2013) The ChEBI reference database and ontology for biologically relevant chemistry: enhancements for 2013. Nucleic Acids Res.). For example, CHEBI:61778 - triterpenoid saponin.
  • Agricultural residues remaining after harvest may be suitable for extraction and supply of saponins.
  • sugarbeet leaves and skins may be further extracted to derive useful quantities of saponin.
  • saponins may be extracted from parts of the plant collected from the wild (for example, protodioscin from Tribulus terrestris) or through managed plantations (for example from the bark of Quillaja saponaria).
  • the detergent composition used in the method or use preferably comprises surfactant (which includes a mixture of two or more surfactants).
  • the composition comprises from 1 to 60 wt.%, preferably from 2.5 to 50 wt.%, more preferably from 4 to 40 wt.% of surfactant. Even more preferred levels of surfactant are from 6 to 40 wt.%, more preferably from 8 to 35 wt.%.
  • Suitable anionic detergent compounds which may be used are usually water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher alkyl radicals.
  • Suitable anionic detergent compounds are rhamnolipids, sodium and potassium alkyl sulphates, especially those obtained by sulphating higher Cs to Cie alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl Cg to C20 benzene sulphonates, particularly sodium linear secondary alkyl C10 to C15 benzene sulphonates; and sodium alkyl glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.
  • the anionic surfactant is preferably selected from: rhamnolipids, linear alkyl benzene sulphonate; alkyl sulphates; alkyl ether sulphates; soaps; alkyl (preferably methyl) ester sulphonates, and mixtures thereof.
  • the most preferred anionic surfactants are selected from: rhamnolipids, linear alkyl benzene sulphonate; alkyl sulphates; alkyl ether sulphates and mixtures thereof.
  • the alkyl ether sulphate is a C12-C14 n-alkyl ether sulphate with an average of 1 to 3EO (ethoxylate) units.
  • Sodium lauryl ether sulphate is particularly preferred (SLES).
  • the linear alkyl benzene sulphonate is a sodium Cn to C15 alkyl benzene sulphonates.
  • the alkyl sulphates is a linear or branched sodium C12 to Cie alkyl sulphates.
  • Sodium dodecyl sulphate is particularly preferred, (SDS, also known as primary alkyl sulphate).
  • Rhamnolipids may preferably be mono-rhamnolipid rich (over 60%), di-rhamnolipid rich (over 60%), or a 40/60 to 60-40 mixture of mono- and di-rhamnolipid.
  • liquid formulations preferably two or more anionic surfactant are present, for example linear alkyl benzene sulphonate together with an alkyl ether sulphate.
  • the laundry composition in addition to the anionic surfactant comprises alkyl exthoylated non-ionic surfactant, preferably from 2 to 8 wt.% of alkyl ethoxylated non-ionic surfactant.
  • Suitable nonionic detergent compounds which may be used include, in particular, the reaction products of compounds having an aliphatic hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids or amides, especially ethylene oxide either alone or with propylene oxide.
  • Preferred nonionic detergent compounds are the condensation products of aliphatic Cs to Cis primary or secondary linear or branched alcohols with ethylene oxide.
  • Alkyl polyglycosides (APG) are also preferred.
  • nonionic detergent compound is the alkyl ethoxylated non-ionic surfactant is a Cs to Cis primary alcohol with an average ethoxylation of 7EO to 9EO units.
  • surfactants used are saturated.
  • a soil release polymer is included.
  • the laundry detergent composition preferably comprises from 0.1 to 8 wt.% of a soil release polymer.
  • Preferred levels of soil release polymer range from 0.2 to 6 wt.%, more preferably from 0.5 to 5 wt.%, most preferably from 1 to 5 wt.%.
  • the soil release polymer is a polyester soil release polymer. More preferably the polyester soil release polymer is a polyethylene and/or polypropylene terephthalate based soil release polymer, most preferably a polypropylene terephthalate based soil release polymer.
  • Suitable polyester based soil release polymers are described in WO 2014/029479 and WO 2016/005338.
  • the detergent composition is in the form of a laundry composition, it is preferred that an alkoxylated polyamine is included.
  • the laundry detergent preferably comprises from 0.1 to 8 wt.% of an alkoxylated polyamine.
  • Preferred levels of alkoxylated polyamine range from 0.2 to 6 wt.%, more preferably from 0.5 to 5 wt.%. Another preferred level is from 1 to 4 wt.%.
  • the alkoxylated polyamine may be linear or branched. It may be branched to the extent that it is a dendrimer.
  • the alkoxylation may typically be ethoxylation or propoxylation, or a mixture of both.
  • the alkoxylated polyamine comprises an alkoxylated polyethylenimine, and/or alkoxylated polypropylenimine, more preferably the alkoxylation is ethoxylation or propoxylation or a mixture of both.
  • a nitrogen atom is alkoxylated, a preferred average degree of alkoxylation is from 10 to 30, preferably from 15 to 25.
  • a preferred material is alkoxylated polyethylenimine, most preferably ethoxylated polyethyleneimine, with an average degree of ethoxylation being from 10 to 30 preferably from 15 to 25, where a nitrogen atom is ethoxylated.
  • Additional enzymes other than the specified protease may be present in the detergent composition. It is preferred that additional enzymes are present in the preferred laundry detergent composition.
  • the level of each enzyme in the laundry composition of the invention is from 0.0001 wt.% to 0.1 wt.%.
  • Levels of enzyme present in the composition preferably relate to the level of enzyme as pure protein.
  • Preferred further enzymes include those in the group consisting of: lipases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases, and/or mannanases. Said preferred additional enzymes include a mixture of two or more of these enzymes.
  • the further enzyme is selected from: lipases, cellulases, and/or alpha-amylases.
  • Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa ( T . lanuginosus) as described in EP 258 068 and EP 305216 or from H. insolens as described in WO 96/13580, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 331 376), P. stutzeri (GB 1,372,034), P.
  • lipase variants such as those described in WO 92/05249,
  • Preferred commercially available lipase enzymes include LipolaseTM and Lipolase UltraTM, LipexTM and Lipoclean TM (Novozymes A/S).
  • the method of the invention may be carried out in the presence of phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32.
  • phospholipase is an enzyme which has activity towards phospholipids.
  • Phospholipids such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol.
  • Phospholipases are enzymes which participate in the hydrolysis of phospholipids.
  • phospholipases Ai and A2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid
  • lysophospholipase or phospholipase B
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • the composition may use cutinase, classified in EC 3.1.1.74.
  • the cutinase used according to the invention may be of any origin.
  • Preferably cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.
  • Suitable amylases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha- amylases obtained from Bacillus, e.g. a special strain of B. licheniformis, described in more detail in GB 1 ,296,839, or the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060.
  • amylases are DuramylTM, TermamylTM, Termamyl UltraTM, NatalaseTM, StainzymeTM, AmplifyTM, FungamylTM and BANTM (Novozymes A/S), RapidaseTM and PurastarTM (from Genencor International Inc.).
  • Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila, and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, WO 89/09259, WO 96/029397, and WO 98/012307.
  • CelluzymeTM Commercially available cellulases include CelluzymeTM, CarezymeTM, CellucleanTM, EndolaseTM, RenozymeTM (Novozymes A/S), ClazinaseTM and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation). CellucleanTM is preferred.
  • Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include GuardzymeTM and NovozymTM 51004 (Novozymes A/S).
  • the aqueous solution used in the method preferably has an enzyme present.
  • the enzyme is preferably present in the aqueous solution used in the method at a concentration in the range from 0.01 to 10ppm, preferably 0.05 to 1ppm.
  • Any enzyme present in the composition may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708.
  • a polyol such as propylene glycol or glycerol
  • a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid
  • detergent compositions preferably laundry detergent compositions
  • materials that may be included in the detergent compositions include builders, chelating agents, fluorescent agent, perfume, shading dyes and polymers.
  • the composition may comprise a builder.
  • Builder materials may be selected from 1) calcium sequestrant materials, 2) precipitating materials, 3) calcium ion-exchange materials and 4) mixtures thereof.
  • calcium sequestrant builder materials examples include alkali metal polyphosphates, such as sodium tripolyphosphate and organic sequestrants, such as ethylene diamine tetra-acetic acid.
  • precipitating builder materials examples include sodium orthophosphate and sodium carbonate.
  • Examples of calcium ion-exchange builder materials include the various types of water- insoluble crystalline or amorphous aluminosilicates, of which zeolites are well known representatives thereof, e.g. zeolite A, zeolite B (also known as zeolite P), zeolite C, zeolite X, zeolite Y and also the zeolite P-type as described in EP-A-0,384,070.
  • zeolites are well known representatives thereof, e.g. zeolite A, zeolite B (also known as zeolite P), zeolite C, zeolite X, zeolite Y and also the zeolite P-type as described in EP-A-0,384,070.
  • the composition may also contain 0-65 wt.% of a builder or complexing agent such as ethylenediaminetetraacetic acid, diethylenetriamine-pentaacetic acid, alkyl- or alkenylsuccinic acid, nitrilotriacetic acid or the other builders mentioned below.
  • a builder or complexing agent such as ethylenediaminetetraacetic acid, diethylenetriamine-pentaacetic acid, alkyl- or alkenylsuccinic acid, nitrilotriacetic acid or the other builders mentioned below.
  • Many builders are also bleach-stabilising agents by virtue of their ability to complex metal ions.
  • Zeolite and carbonate are preferred builders, with carbonates being particularly preferred.
  • the composition may contain as builder a crystalline aluminosilicate, preferably an alkali metal aluminosilicate, more preferably a sodium aluminosilicate. This is typically present at a level of less than 15 wt.%.
  • Aluminosilicates are materials having the general formula:
  • the preferred sodium aluminosilicates contain 1.5-3.5 S1O2 units in the formula above. They can be prepared readily by reaction between sodium silicate and sodium aluminate, as amply described in the literature.
  • the ratio of surfactants to alumuminosilicate (where present) is preferably greater than 5:2, more preferably greater than 3:1.
  • phosphate builders may be used.
  • phosphate embraces diphosphate, triphosphate, and phosphonate species.
  • Other forms of builder include silicates, such as soluble silicates, metasilicates, layered silicates (e.g. SKS-6 from Hoechst).
  • the laundry detergent formulation is a non-phosphate built laundry detergent formulation, i.e. , contains less than 1 wt.% of phosphate. Most preferably the laundry detergent formulation is not built i.e. contain less than 1 wt.% of builder.
  • Chelating agents may be present or absent from the detergent compositions. If present, then the chelating agent is present at a level of from 0.01 to 5 wt.%.
  • Example phosphonic acid (or salt thereof) chelating agents are: 1-Hydroxyethylidene-1,1- diphosphonic acid (HEDP); Diethylenetriaminepenta(methylenephosphonic acid) (DTPMP); Hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP); Aminotris(methylenephosphonic acid) (ATMP); Ethylenediaminetetra(methylenephosphonic acid) (EDTMP); Tetramethylenediaminetetra(methylenephosphonic acid) (TDTMP); and, Phosphonobutanetricarboxylic acid (PBTC).
  • HEDP 1-Hydroxyethylidene-1,1- diphosphonic acid
  • DTPMP Diethylenetriaminepenta(methylenephosphonic acid)
  • HDTMP Hexamethylenediaminetetra(methylenephosphonic acid)
  • AMP Aminotris(methylenephosphonic acid)
  • ETMP Ethylenediaminet
  • the composition preferably comprises a fluorescent agent (optical brightener).
  • fluorescent agents are well known, and many such fluorescent agents are available commercially. Usually, these fluorescent agents are supplied and used in the form of their alkali metal salts, for example, the sodium salts.
  • the total amount of the fluorescent agent or agents used in the composition is generally from 0.0001 to 0.5 wt.%, preferably 0.005 to 2 wt.%, more preferably 0.01 to 0.1 wt.%.
  • Preferred classes of fluorescer are: Di-styryl biphenyl compounds, e.g. Tinopal (Trade Mark) CBS-X, Di-amine stilbene di-sulphonic acid compounds, e.g. Tinopal DMS pure Xtra and Blankophor (Trade Mark) HRH, and Pyrazoline compounds, e.g. Blankophor SN.
  • Di-styryl biphenyl compounds e.g. Tinopal (Trade Mark) CBS-X
  • Di-amine stilbene di-sulphonic acid compounds e.g. Tinopal DMS pure Xtra and Blankophor (Trade Mark) HRH
  • Pyrazoline compounds e.g. Blankophor SN.
  • Preferred fluorescers are fluorescers with CAS-No 3426-43-5; CAS-No 35632-99-6; CAS-No 24565-13-7; CAS-No 12224-16-7; CAS-No 13863-31-5; CAS-No 4193-55-9; CAS-No 16090- 02-1; CAS-No 133-66-4; CAS-No 68444-86-0; CAS-No 27344-41-8.
  • fluorescers are: sodium 2 (4-styryl-3-sulfophenyl)-2H-napthol[1,2-d]triazole, disodium 4,4'-bis ⁇ [(4-anilino-6-(N methyl-N-2 hydroxyethyl) amino 1,3,5-triazin-2- yl)]amino ⁇ stilbene-2-2' disulphonate, disodium 4,4'-bis ⁇ [(4-anilino-6-morpholino-1 ,3,5-triazin- 2-yl)]amino ⁇ stilbene-2-2' disulphonate, and disodium 4,4'-bis(2-sulphostyryl)biphenyl.
  • the aqueous solution used in the method has a fluorescer present.
  • the fluorescer is present in the aqueous solution used in the method preferably in the range from 0.0001 g/l to 0.1 g/l, more preferably 0.001 to 0.02 g/l.
  • the composition preferably comprises a perfume.
  • perfumes are provided in the CTFA (Cosmetic, Toiletry and Fragrance Association) 1992 International Buyers Guide, published by CFTA Publications and OPD 1993 Chemicals Buyers Directory 80th Annual Edition, published by Schnell Publishing Co.
  • the perfume comprises at least one note (compound) from: alpha-isomethyl ionone, benzyl salicylate; citronellol; coumarin; hexyl cinnamal; linalool; pentanoic acid, 2- methyl-, ethyl ester; octanal; benzyl acetate; 1,6-octadien-3-ol, 3,7-dimethyl-, 3-acetate; cyclohexanol, 2-(1 , 1 -dimethylethyl)-, 1-acetate; delta-damascone; beta-ionone; verdyl acetate; dodecanal; hexyl cinnamic aldehyde; cyclopentadecanolide; benzeneacetic acid, 2- phenylethyl ester; amyl salicylate; beta-caryophyllene; ethyl undecylenate;
  • Useful components of the perfume include materials of both natural and synthetic origin. They include single compounds and mixtures. Specific examples of such components may be found in the current literature, e.g., in Fenaroli's Handbook of Flavour Ingredients, 1975, CRC Press; Synthetic Food Adjuncts, 1947 by M. B. Jacobs, edited by Van Nostrand; or Perfume and Flavour Chemicals by S. Arctander 1969, Montclair, N.J. (USA).
  • compositions of the present invention it is envisaged that there will be four or more, preferably five or more, more preferably six or more or even seven or more different perfume components.
  • top notes are defined by Poucher (Journal of the Society of Cosmetic Chemists 6(2):80 [1955]).
  • Preferred top-notes are selected from citrus oils, linalool, linalyl acetate, lavender, dihydromyrcenol, rose oxide and cis-3-hexanol.
  • Perfume top note may be used to cue the whiteness and brightness benefit of the invention.
  • perfume components which it is advantageous to encapsulate include those with a relatively low boiling point, preferably those with a boiling point of less than 300, preferably 100-250 Celsius. It is also advantageous to encapsulate perfume components which have a low CLog P (ie. those which will have a greater tendency to be partitioned into water), preferably with a CLog P of less than 3.0.
  • these materials have been called the "delayed blooming" perfume ingredients and include one or more of the following materials: allyl caproate, amyl acetate, amyl propionate, anisic aldehyde, anisole, benzaldehyde, benzyl acetate, benzyl acetone, benzyl alcohol, benzyl formate, benzyl iso valerate, benzyl propionate, beta gamma hexenol, camphor gum, laevo-carvone, d- carvone, cinnamic alcohol, cinamyl formate, cis-jasmone, cis-3-hexenyl acetate, cuminic alcohol, cyclal c, dimethyl benzyl carbinol, dimethyl benzyl carbinol acetate, ethyl acetate, ethyl aceto acetate, ethy
  • perfumes it is envisaged that there will be four or more, preferably five or more, more preferably six or more or even seven or more different perfume components from the list given of delayed blooming perfumes given above present in the perfume.
  • perfumes with which the present invention can be applied are the so- called aromatherapy' materials. These include many components also used in perfumery, including components of essential oils such as Clary Sage, Eucalyptus, Geranium,
  • the laundry treatment composition does not contain a peroxygen bleach, e.g., sodium percarbonate, sodium perborate, and peracid.
  • a peroxygen bleach e.g., sodium percarbonate, sodium perborate, and peracid.
  • the composition is a laundry detergent composition
  • it comprises a shading dye.
  • the shading dye is present at from 0.0001 to 0.1 wt.% of the composition.
  • Dyes are described in Color Chemistry Synthesis, Properties and Applications of Organic Dyes and Pigments, (H Zollinger, Wiley VCH, Zurich, 2003) and, Industrial Dyes Chemistry, Properties Applications. (K Hunger (ed), Wley-VCH Weinheim 2003).
  • Shading Dyes for use in laundry compositions preferably have an extinction coefficient at the maximum absorption in the visible range (400 to 700nm) of greater than
  • the dyes are blue or violet in colour.
  • Preferred shading dye chromophores are azo, azine, anthraquinone, and triphenylmethane.
  • Azo, anthraquinone, phthalocyanine and triphenylmethane dyes preferably carry a net anionic charged or are uncharged.
  • Azine preferably carry a net anionic or cationic charge.
  • Blue or violet shading dyes deposit to fabric during the wash or rinse step of the washing process providing a visible hue to the fabric. In this regard the dye gives a blue or violet colour to a white cloth with a hue angle of 240 to 345, more preferably 250 to 320, most preferably 250 to 280.
  • the white cloth used in this test is bleached non-mercerised woven cotton sheeting.
  • Mono-azo dyes preferably contain a heterocyclic ring and are most preferably thiophene dyes.
  • Bis-azo dyes are preferably sulphonated bis-azo dyes.
  • Preferred examples of sulphonated bis-azo compounds are direct violet 7, direct violet 9, direct violet 11 , direct violet 26, direct violet 31 , direct violet 35, direct violet 40, direct violet 41 , direct violet 51 , Direct Violet 66, direct violet 99 and alkoxylated versions thereof. Alkoxylated bis-azo dyes are discussed in WO2012/054058 and W02010/151906.
  • alkoxylated bis-azo dye is :
  • Thiophene dyes are available from Milliken under the tradenames of Liquitint Violet DD and Liquitint Violet ION.
  • Azine dye are preferably selected from sulphonated phenazine dyes and cationic phenazine dyes. Preferred examples are acid blue 98, acid violet 50, dye with CAS-No 72749-80-5, acid blue 59, and the phenazine dye selected from: wherein:
  • X 3 is selected from: -H; -F; -CH 3 ; -C 2 H 5 ; -OCH 3 ; and, -OC 2 H 5 ;
  • X4 is selected from: -H; -CH 3 ; -C 2 H 5 ; -OCH 3 ; and, -OC 2 H 5 ;
  • Y 2 is selected from: -OH; -OCH2CH2OH; -CH(OH)CH 2 OH; -0C(0)CH 3 ; and, C(0)0CH 3.
  • the shading dye is present in the composition in range from 0.0001 to 0.5 wt %, preferably 0.001 to 0.1 wt%. Depending upon the nature of the shading dye there are preferred ranges depending upon the efficacy of the shading dye which is dependent on class and particular efficacy within any particular class. As stated above the shading dye is a blue or violet shading dye.
  • a mixture of shading dyes may be used.
  • the shading dye is most preferably a reactive blue anthraquinone dye covalently linked to an alkoxylated polyethyleneimine.
  • the alkoxylation is preferably selected from ethoxylation and propoxylation, most preferably propoxylation.
  • 80 to 95 mol% of the N-H groups in the polyethylene imine are replaced with iso-propyl alcohol groups by propoxylation.
  • the polyethylene imine before reaction with the dye and the propoxylation has a molecular weight of 600 to 1800.
  • An example structure of a preferred reactive anthraquinone covalently attached to a propoxylated polyethylene imine is:
  • the composition may comprise one or more further polymers.
  • a preferred detergent composition comprises from 0.1 to 20 wt.%, preferably from 0.5 to 15 wt.% or one or more polymers. Examples are carboxymethylcellulose, poly (ethylene glycol), poly(vinyl alcohol), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.
  • Substrate N-Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, was dissolved in methanol to give a stock solution of 20mM.
  • Tris-HCI pH 8.5, 50mM
  • Cotton stained with aged blood CS01 (Centre for Testmaterials - Netherlands) was cut into empty 96-well microtitre plates and pre-wash readings taken for stain intensity.
  • FH32 water the stored formulation samples were diluted to give a final protease concentration of 5mg/L in FH32 water containing (1 g/L) of a laundry detergent formulation containing 15 wt.% surfactant (anionic/nonionic mix) also comprising EPEI and polyester soil release polymer plus dosed saponin, and subsequently transferred (200mI_) to the stains using a multi channel pipette just prior to incubation at 40°C, with shaking at 200rpm for 1 h. Following washing, the wash liquor was immediately removed using a multi-channel pipette, and the stain discs washed 3x with 200mI_ dH20, before leaving overnight in a cupboard to dry.
  • anionic/nonionic mix also comprising EPEI and polyester soil release polymer plus dosed sap
  • the stain plates were digitally scanned and the deltaE measured. This value is used to express cleaning effect and is defined as the colour difference between a white cloth and that of the stained cloth after being washed.
  • deltaE [ (DI_) 2 + (Aa) 2 + (Ab) 2 ] 1/2
  • DI_ is a measure of the difference in darkness between the washed and white cloth
  • Ab are measures for the difference in redness and yellowness respectively between both cloths.
  • Example 1 showing the use of saponin to improve protease activity
  • Biochemical assays for protease activity were initially used in high-throughput microtitre plate format to enable different saponins at different doses to be screened for their effect on protease activity.
  • the protease used was Carnival Evity protease - supplied by Novozymes.
  • the saponin was tested at the concentrations listed in table 1 without protease, and no effect on the assay was seen by the saponin alone.
  • Table 1 shows that when using a concentration of 100ng/ml_ protease, a positive effect on (increasing) protease activity is observed from addition of saponin (in this instance Escin). In this case, a step-up in activity corresponding to 30% was noted from Escin concentrations >0.5mM, in particular at concentrations 310mM.
  • Example 2 showing the use of different saponins to improve protease activity
  • the graph in figure 1 shows the effect of saponin at various levels for: a control (without protease); oleanolic acid (a triterpenoid backbone without sugar moieties); and saponins within the definition of the invention: the 3x and 4x glycosylated variants of oleanolic acid (OA-28 x 3Gly and OA-28 x4Gly), escin and avenacin.
  • the level of saponin at Opm corresponds to the protease only activity.
  • the saponins within the scope of the invention improved the protease activity by a statistically significant amount at a saponin level of 5mM and above. Similarity between structures of effective saponin activators of protease are observed (figure 1); with common structural features of a triterpenoid backbone to which are linked sugar moieties.
  • Example 3 - showing the activity of saponin on cleaning performance
  • Table 2 also shows that increasing the dose of saponin does not result in improved cleaning from just the saponin alone.
  • a relatively constant cleaning performance due to saponin ( ⁇ 5 dSRI) is observed at concentrations of up to 25mM (table 2).
  • the ‘add-on’ effect of boosted protease activity is noted when using Tea saponin >1mM, which leads to increased values for dSRI ( ⁇ 18).
  • Example 4 showing the activity of saponin on scaled-up cleaning performance
  • Figure 2 shows that the saponin effect on increased protease activity is also seen in scaled- up mini-bottle wash studies (63ml).
  • the figure is a graph showing the increased protease activity when 5mM of saponin is used. A statistically significant improvement in protease activity is demonstrated at this saponin level.
  • Example 5 showing the activity of saponin on different proteases
  • This example shows that many proteases are found to be activated by saponins. This includes a range of commercial bacterial laundry proteases, as well as other bacterial derived protease (Streptomyces) and proteases of fungal origin (Aspergillus and Rhizopus).
  • An example of a mammalian protease activated by escin is also shown (Bovine pancreas).
  • proteases of different active site configuration/mechanism can also be activated by saponin (examples shown are subtilisin-type alkaline proteases with a catalytic serine residue, as well as an acidic protease) (figure 3).
  • Figure 3 shows that the increased protease activity using saponin is also seen across many different proteases, both from origin and from protease type.
  • Example 6 showing the activity using different saponins at scaled-up mini-bottle (100ml) wash performance across different time points of the wash

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Abstract

L'invention concerne un procédé d'amélioration de l'activité protéase dans une composition détergente, ledit procédé impliquant l'incorporation de 0,1 à 40 % en poids d'une saponine dans ladite composition, la composition détergente comprenant de 0,0005 à 2,5 % en poids d'une enzyme protéase ; la saponine ayant un squelette triterpénoïde, et une ou plusieurs fractions de sucre fixées au squelette triterpénoïde ; et l'utilisation de saponine pour améliorer l'activité protéase dans une composition détergente.
EP21728952.9A 2020-06-08 2021-06-07 Composition de détergent Revoked EP4162018B1 (fr)

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EP4162018B1 (fr) 2024-01-31

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