WO2009118349A1 - Detergent composition comprising a triggered release system - Google Patents
Detergent composition comprising a triggered release system Download PDFInfo
- Publication number
- WO2009118349A1 WO2009118349A1 PCT/EP2009/053534 EP2009053534W WO2009118349A1 WO 2009118349 A1 WO2009118349 A1 WO 2009118349A1 EP 2009053534 W EP2009053534 W EP 2009053534W WO 2009118349 A1 WO2009118349 A1 WO 2009118349A1
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- WIPO (PCT)
- Prior art keywords
- enzyme
- rinse
- substrate
- benefit agent
- detergent composition
- Prior art date
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Classifications
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- 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
- C11D3/38672—Granulated or coated enzymes
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
- C11D17/0039—Coated compositions or coated components in the compositions, (micro)capsules
Definitions
- the present invention relates to a detergent composition, especially a laundry deter- gent composition, comprising detergent particles that comprise a triggered release system for a rinse benefit agent.
- the invention further relates to the manufacture of said detergent composition and its use.
- the invention relates to a dishwash detergent composition comprising said particles and to its use in dishwashing.
- laundry, dishwashing or cleaning products have been made up in measured portions containing all the constituents needed for a laundry, dishwashing or cleaning cycle.
- portions In the case of solid products, such portions have frequently been formed into shapes (sometimes containing more than one phase), such as pellets, beads, tablets ("tabs"), blocks, briquettes, etc., which are introduced into the wash liquor as intact products. It has also been proposed to enclose liquid products in water-soluble capsules that dissolve upon contact with the aqueous bath and release their contents into the bath.
- Adoption of a matrix material with a melting point at the temperature of the final rinse cycle ensures that the final-rinse surface-active agent emulsified in the matrix (or, ideally, in molecular dispersion in the matrix) stays enclosed in the matrix during the cleaning cycle, which is run at temperatures of up to 55°C, and is not released until the matrix material melts in the final rinse cycle in which temperatures of up to about 65°C are attained.
- WO 9937746 (Procter & Gamble) relates to a multi-layer detergent tablet comprising a core, a first encapsulating layer comprising a detergent active, and a second encapsulating layer comprising a disruption system, which leads to delayed release of the detergent active.
- EP-A-971 024 (Procter & Gamble) discloses laundry cleaning compositions comprising a detersive ingredient and a product of the reaction between a primary amine and a perfume component. It is described that the active component is released over a longer period than when it is used on its own.
- the following documents disclose other examples of particles for use in detergents:
- the present invention provides an ability to formulate in a cost-efficient manner more effective release systems targeted for the rinse phase of a laundry or dishwash process.
- One objective of the present invention is to provide a system to release rinse benefit agents into a rinse liquor in a dish wash or laundry process, at a desired process stage or point in time in the application.
- a triggered release system does not require that the liquid composition is especially tailored to the release system.
- a particle comprising a rinse benefit agent and an enzyme surrounded by a barrier layer comprising a substrate for said enzyme provides a system that is optimal for release of rinse benefit agents such as perfume to a laundry or dishwash process.
- the particle of the present invention comprises an enzyme triggered release system comprising a rinse benefit agent and an enzyme-substrate pair enabling the triggered release of the rinse benefit agent at the rinse stage in a laundry or dishwashing process.
- the enzyme- substrate pair used in the present invention forms part of an effective triggered release system for the delivery of a rinse benefit agent in order to obtain the right release profile during the application.
- the laundry detergent compositions of the present invention comprise detergent particles that comprise: a) a rinse benefit agent, b) an enzyme, and c) a substrate for said enzyme, wherein the rinse benefit agent and the enzyme are enclosed in (surrounded by) a barrier layer comprising the substrate.
- the present invention further relates to a method for preparing the laundry detergent compositions comprising the particles, to a dishwash detergent composition comprising the particles and to the use of said particles.
- the invention provides a process for washing kitchenware, comprising a washing step wherein soiled kitchenware is contacted with an aqueous composition comprising the dishwash detergent composition of claim 12, followed by a rinsing step wherein the rinse benefit agent is released from the particles into the rinse liquid.
- the particle of the invention comprises a core containing the rinse benefit agent and a layer surrounding the core.
- the core may comprise an inert carrier particle, consisting, e.g., of Na 2 SO 4 , carbonate or silicate.
- the rinse benefit agent, the substrate and the enzyme may be present together in the core and/or in the same layer.
- the particle comprises a barrier layer.
- the benefit agent, the enzyme and the sub- strate may be present homogenously mixed together in a matrix which is either the core of the particle or a layer.
- the particle may comprise a first layer and a second layer.
- the first layer may comprise the enzyme and the second layer may comprise the substrate to the enzyme that is present in the first layer.
- the enzyme and the substrate are present in the particle in such a way that they are in physical contact, thus either in the same layer or matrix or in layers bordering each other.
- the particle comprises: a) a core comprising a rinse benefit agent, b) optionally a protective layer, c) a layer comprising an enzyme, and d) a barrier layer comprising a substrate for the enzyme in c).
- the particle may further comprise one or more additional coatings.
- the particles of the present invention are preferably between 0.001 mg to l OOOOmg. In a more particular embodiment of the present invention, the particles weigh between 0.005 mg to 1000 mg. In an even more particular embodiment the mean particle weight is between O.OI mg to 100 mg.
- the mean particle size is in a particular embodiment in the range of 0.1 to 2000 ⁇ m. In a more particular embodiment the mean particle size is in the range of 50 to 1400 ⁇ m. In a most preferred embodiment of the present invention, the mean particle size is in the range of 100 to 1000 ⁇ m. In a further embodiment the mean particle size of the present invention is in the range of 100 to 800 ⁇ m.
- the particles For use in dishwashing, the particles should be chosen sufficiently large that they are not discharged to a significant extent during the pumping out after the main cleaning cycle.
- the mean particle size may be greater than 1 mm or greater than 3 mm, e.g. in the range 3-20 mm or 5-15 mm.
- the particles of the invention release more than 60% of the rinse benefit agent in the rinse phase of a washing process.
- the particles of the invention releases more than 70% of the rinse benefit agent in the rinse phase.
- the release of rinse benefit agent can be measured by means of the method described in Example 6.
- the detergent particle may comprise a core surrounded by one or more layers.
- the core of the particle may comprise the rinse benefit agent either alone or in combination with other constituents.
- the core may comprise a preformed core such as an inert core upon which the rinse benefit agent is deposited or a core prepared of porous material into which the rinse benefit agent is deposited. In a preferred embodiment the rinse benefit agent is deposited into the core.
- the benefit agent may be incorporated into the core at the same time as the core par- tide is prepared.
- the core is prepared by the granulation of filler components in the presence of the rinse benefit agent and, optionally, an additional binder material.
- Preformed cores may also be called carrier particles; nuclei, placebo nuclei (nucleus free of active compound) or seeds are inert particles upon which the mixture comprising the active compound can be deposited.
- the preformed cores may comprise inorganic salts, starch, sugars, sugar alcohols, small organic molecules such as organic acids or salts, such as carbonate, minerals such as clays, zeolite or silicates or a combination of two or more of these.
- the core may be prepared by ap- plying the mixture comprising the rinse benefit agent onto a preformed core.
- the particle of the present invention comprises a barrier layer.
- Said barrier layer provides either a physical barrier and/or a transport barrier (including charge) to the rinse benefit agent in question.
- the barrier layer prevents, reduces, delays and/or inhibits the pas- sage of the rinse benefit agent from the particle.
- the barrier layer may prevent leakage or undesired migration or transport of the rinse benefit agent from the particle into the wash liquor during the wash stage.
- the barrier layer may also improve the particle stability beneficial in formulation, storage and application.
- the barrier layer may act as a scaffold for the substrate.
- the substrate may itself act as a barrier layer or it may be a secondary component which by virtue of the enzymatic activity affects properties of the barrier material.
- the barrier layer comprises the substrate and may comprise the enzyme.
- the substrate present in the barrier layer is present in an amount of said layer so the enzyme accelerates the alteration of the substrate to such an extent that the barrier layer loses its integrity whereby the rinse benefit agent is released into the wash liquor.
- the barrier layer may comprise 1-100% w/w of substrate.
- the amount of substrate may be at least 10% w/w of the barrier layer, particularly at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70% or at least 80% w/w of the barrier layer.
- the amount of substrate in the barrier layer may particularly be from 30-100% w/w of the barrier layer, e.g. from 40-90% w/w, 50-80% w/w, less than 90% w/w, less than 80%, or less than 70%.
- the barrier layer should contain a water-insoluble continuous layer which is preferably hydrophobic and may comprise suspended particles.
- the main component of the continuous layer may be the enzyme substrate, or it may be inert.
- the main component can be a triglyceride such as a fat or oil, paraffin, tripalmitin, palm oil, beeswax, jojoba wax, polyesters, ester wax, polycaprolactone (PCL), polymers such as polystyrene and polybutyleneoxide, and mixtures thereof or a polymer such as polystyrene or polycarbonate.
- the suspended particles may comprise the enzyme or the substrate, or it may be inert, e.g., a filler, kaolin, talc, clay, silica, dye particles or calcium carbonate.
- the barrier layer may comprise a material which does not melt or disintegrate such that it significantly compromises the properties of the barrier layer, when exposed to temperatures above 35°C or are not particularly soluble in wash liquor or other aqueous solvents.
- the enzyme substrate does not have a melting point in the range of 35°C to 50 0 C.
- the rinse benefit agent is a compound, which performs its function during a rinsing cycle of a laundry or dishwash machine, either by improving the result of the washing process or by delivering a benefit as perceived by the user.
- the rinse benefit agent includes perfumes, encapsulated perfumes, fragrances, pro-fragrances, chemical malodour neutralizers, physical malodour neutralizers, fibre lubricants, anti-static agents, anti-wrinkle agents, antifoams, photo-protective agents, optical brighteners, soil release polymers, soil repelling agents, stain repellent agents, fabric softening compounds, anti-microbial agents, insecticides, fungicides, insect repellents, antioxidants, moisture management agents, shading dyes and pigments, dye fixing agents, fabric care agents, silicone oils, a second enzyme and mixtures thereof.
- the particles of the invention may comprise rinse benefit agents such as clear rinsing agents, antibacterial composi- tions, silver
- Fragrances which may be employed in fragrance particles according to the present invention are those which can be usefully released at sufficient dosage over a required period of time from the fragrance particle. They may be selected for example from natural, essential oils or synthetic perfumes, and blends thereof. Many fragrances are polar in nature because they contain substantial amounts of alcohols and other polar compounds.
- Typical perfumery materials include natural oils such as lemon oil, mandarin oil, clove leaf oil, cedar wood oil, rose absolute or jasmine absolute, natural resins such as labdanum resin or olibanum resin; single perfumery chemicals which may be isolated from natural sources or manufactured syn- thetically, as for example alcohols such as geranoil, nerol, citronellol, linalool, tetrahydrogera- noil, betaphenylathyl alcohol, methyl phenyl carbinol, dimethyl benzyl carbonol, menthol or cedrol; acetates and other esters derived from such alcohols; aldehydes such as citral, cit- ronellal, hydroxycitronella, lauric aldehyde, undecylenic aldehyde, cinnamaldehyde, amyl cin- namic aldehyde, vanillin or heliotropin; acetals derived from such
- Perfume or fragrances may be added to laundry, dishwash or cleaning compositions in order to enhance overall esthetic appeal of the products and to provide the consumer with not only the performance (fabric softening, clear rinsing) but also a sensorially unmistakable product.
- perfume oils or fragrances it is possible to use individual odorant compounds, examples being the synthetic products of the ester, ether, aldehyde, ketone, alcohol, and hydrocarbon types.
- Odorant compounds of the ester type are, for example, benzyl acetate, phenoxyethyl isobutyrate, p-tert-butylcyclohexyl acetate, linalyl acetate, dimethylbenzylcar- binyl acetate, phenylethyl acetate, linalyl benzoate, benzyl formate, ethyl methylphenylglyci- nate, allyl cyclohexylpropionate, styrallyl propionate, and benzyl salicylate.
- the ethers include, for example, benzyl ethyl ether.
- the aldehydes include, for example, the linear al- kanals having 8 to 18 carbon atoms, citral, citronellal, citronellyloxyacetaldehyde, cyclamen aldehyde, hydroxycitronellal, HIIaI and bourgeonal.
- the ketones include, for example, the io- nones, ⁇ -isomethylionone and methyl cedryl ketone.
- the alcohols include anethole, citronel- lol, eugenol, geraniol, linalool, phenylethyl alcohol, and terpineol.
- the hydrocarbons include primarily terpenes such as limonene and pinene.
- perfume oils may also contain natural odorant mixtures, as obtainable from plant sources. Examples are pine oil, citrus oil, jasmine oil, patchouli oil, rose oil or ylang-ylang oil. Likewise suitable are nutmeg oil, sage oil, chamomile oil, clove oil, balm oil, mint oil, cinnamon leaf oil, lime blossom oil, juniper berry oil, vetiver oil, olibanum oil, galbanum oil and labdanum oil, orange blossom oil, neroli oil, orange peel oil, and sandalwood oil.
- the fragrance content is in the region of up to 2% by weight of the overall detergent composition.
- the perfume is typically present in an amount of from 10-85% by total weight of the particle, preferably from 20 to 75 % by total weight of the particle.
- the perfume suitably has a molecular weight of from 50 to 500.
- Top notes are defined by Poucher (Journal of the Society of Cosmetic Chemists 6(2):80 [1955]). Examples of well known top-notes include citrus oils, linalool, linalyl acetate, lavender, dihydromyrcenol, rose oxide and cis-3-hexanol.
- Typical 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.
- perfume components which have a low LogP (ie. those which will be partitioned into water), preferably with a LogP of less than 3.0.
- materials, of relatively low boiling point and relatively low LogP have been called the "delayed blooming" perfume ingredients and include the following materials:
- AIIyI Caproate Amyl Acetate, Amyl Propionate, Anisic Aldehyde, Anisole, Benzalde- hyde, Benzyl Acetate, Benzyl Acetone, Benzyl Alcohol, Benzyl Formate, Benzyl lso Valerate, Benzyl Propionate, Beta Gamma Hexenol, Camphor Gum, Laevo-Carvone, d-Carvone, Cin- namic Alcohol, Cinamyl Formate, Cis-Jasmone, cis-3-Hexenyl Acetate, Cuminic Alcohol, Cy- clal C, Dimethyl Benzyl Carbinol, Dimethyl Benzyl Carbinol Acetate, Ethyl Acetate, Ethyl Aceto Acetate, Ethyl Amyl Ketone, Ethyl Benzoate, Ethyl Butyrate, Ethyl Hexyl Ketone, Ethyl Phenyl Acetate
- Part or all of the perfume may be in the form of a pro-fragrance.
- a pro-fragrance is any material which comprises a fragrance precursor that can be converted into a fragrance.
- Suitable pro-fragrances are those that generate perfume components which are aldehydes.
- Aldehydes useful in perfumery include but are not limited to phenylacetaldehyde, p- methyl phenylacetaldehyde, p-isopropyl phenylacetaldehyde, methyinonyl acetaldehyde, phenylpropanal, 3- (4-t-butylphenyl)-2-methyl propanal, 3- (4-t-butylphenyl)- propanal, 3- (4- methoxyphenyl)-2-methylpropanal, 3- (4-isopropylphenyl)-2- methylpropanal, 3- (3, 4- methylenedioxyphenyl)-2-methyl propanal, 3- (4- ethylpheny)-2, 2-dimethylpropanal, phenyl- butanal, 3-methyl-5-phenylpentanal, hexanal, trans-2-hexenal,
- Suitable fabric softening and/or conditioning agent groups are preferably chosen from those of the cationic detergent active type, clays and silicones.
- Those of the cationic detergent active type are preferably selected from quaternary ammonium cationic molecules, for example those having a solubility in water at pH 2.5 and 20 0 C of less than 10 g/l.
- Fabric softening compounds which may be contained in particles according to the present invention may be cationic, e.g. substantially water-insoluble quaternary ammonium materials comprising a single alkyl or alkenyl long chains having an average chain length greater than or equal to C 2 o or, more preferably, compounds comprising a polar head group and two alkyl or alkenyl chains having an average chain length greater than or equal to Ci 4 .
- the fabric softening compounds have two long chain alkyl of alkenyl chains eacg having an average chain length greater than or equal to Ci ⁇ . Most preferably at least 50% of the long chain alkyl or alkenyl groups have a chain length of Ci 8 or above. It is preferred if the long chain alkyl or alkenyl groups of the fabric softening are predominantly linear. Silicones with similar functional properties may also be preferred.
- ester-linked quaternary ammonium compounds it is preferred for the ester-linked quaternary ammonium compounds to contain two or more ester groups.
- ester group (s) is a linking group between the nitrogen atom and an alkyl group.
- the ester groups (s) are preferably attached to the nitrogen atom via another hydro- carbyl group.
- suitable mate- rials include: non-volatile silicone fluids, such as poly (di) alkyl siloxanes, especially polydi- methyl siloxanes and carboxylated or ethoxylated variants. They may be branched, partially cross-linked or preferably linear aminosilicones, comprising any organosilicone having amine functionality.
- Suitable silicones include dimethyl, methyl (aminoethylaminoisobutyl) siloxane, typi- cally having a dynamic viscosity of from 100 mPas to 200 000 mPas (when measured at 25°C and a shear rate of around 100s) with an average amine content of ca. 2 mol%.
- the second enzyme could be used for the purpose of bacterial control (e.g., a protease or lysozyme), as a fabric care active (e.g. a cellulase), as an activator (e.g. a lipase degrading pro-perfumes or pro-bleach molecules), for prevention of biofilm or for prevention of odor in washing machines washing always at low temperatures.
- bacterial control e.g., a protease or lysozyme
- a fabric care active e.g. a cellulase
- an activator e.g. a lipase degrading pro-perfumes or pro-bleach molecules
- the amount of rinse benefit agent present in the particle may be from 1 to 95%, preferably 10 to 95% more preferably 30 to 90%.
- the enzyme may either hydrolyze the enzyme substrate or help in the process of modifying its properties in such a way as to destroy its barrier properties and thereby destabilize the particles' structural integrity.
- the enzyme in the context of the present invention may be any enzyme or combination of different enzymes. Accordingly, when references are made to "an enzyme” this will in generally be understood not only single enzymes but to combinations of more than one enzyme.
- the particles of the present invention may comprise at least one, at least two or at least three enzymes. It is to be understood that enzyme variants (produced, for example, by recombinant techniques) are included within the meaning of the term "enzyme”. Examples of such enzyme variants are disclosed, e.g.
- enzymes which may appropriately be incorporated in particles of the invention include oxidoreductases (EC 1.-.-.-), transferases (EC 2.-.-.-), hydrolases (EC 3.-.-.-), lyases (EC 4.-.-.-), isomerases (EC 5.-.-.-) and ligases (EC 6.-.-.-).
- Preferred oxidoreductases in the context of the invention are peroxidases (EC 1.11.1 ) and laccases (EC 1.10.3.2)
- Preferred hydrolases in the context of the invention are: carboxylic ester hydrolases (EC 3.1.1.-) such as lipases (EC 3.1.1.3); phytases (EC 3.1.3.-), e.g. 3-phytases (EC 3.1.3.8) and 6-phytases (EC 3.1.3.26); glycosidases (EC 3.2, which fall within a group denoted herein as "carbohydrases”), such as ⁇ -amylases (EC 3.2.1.1 ).
- carbohydrase is used to denote not only enzymes capable of breaking down carbohydrate chains (e.g. starches or cellulose) of especially five- and six-membered ring structures (i.e. glycosidases, EC 3.2), but also enzymes capable of isomerizing carbohydrates, e.g. six-membered ring structures such as D-glucose to five- membered ring structures such as D-fructose.
- Carbohydrases of relevance include the following (EC numbers in parentheses): ⁇ -amylases (EC 3.2.1.1 ), ⁇ -amylases (EC 3.2.1.2), glucan 1 ,4- ⁇ -glucosidases (EC 3.2.1.1 ), ⁇ -amylases (EC 3.2.1.2), glucan 1 ,4- ⁇ -glucosidases (EC 3.2.1.1 ), ⁇ -amylases (EC 3.2.1.2), glucan 1 ,4- ⁇ -glucosidases (EC
- lipases examples include LipoprimeTM LipolaseTM, Lipo- laseTM Ultra, LipozymeTM, PalataseTM, NovozymTM 435 and LecitaseTM (all available from No- vozymes A/S).
- Other commercially available lipases include LumafastTM (Pseudomonas mendocina lipase from Genencor International Inc.); LipomaxTM (Ps. pseudoalcaligenes lipase from Gist- Brocades/Genencor Int. Inc.; and Bacillus sp. lipase from Solvay enzymes. Further lipases are available from other suppliers.
- carbohydrases examples include Alpha-GalTM, Bio-FeedTM Alpha, Bio-FeedTM Beta, Bio-FeedTM Plus, Bio-FeedTM Plus, NovozymeTM 188, CelluclastTM, CellusoftTM, CeremylTM, CitrozymTM, DenimaxTM, DezymeTM, DextrozymeTM, FinizymTM, Fun- gamylTM, GamanaseTM, GlucanexTM, LactozymTM, MaltogenaseTM, PentopanTM, PectinexTM, PromozymeTM, PulpzymeTM, NovamylTM, TermamylTM, AMGTM (Amyloglucosidase Novo), MaltogenaseTM and AquazymTM (all available from Novozymes A/S). Further carbohydrases are available from other suppliers.
- the enzyme substrate used in the present invention is a material which can be modified, degraded and/or altered by the enzyme used in the present invention.
- the enzyme and the substrate are present in the particle in such amounts, that the substrate changes in structure to an extent that makes the particle lose its integrity and thereby releases the rinse benefit agent into the rinse liquor.
- the substrate is preferably water insoluble.
- enzyme-substrate pair is used in relation to the enzyme and the substrate comprised in the particle and where the "substrate” is a substrate for the enzyme, meaning that the enzyme will recognize the substrate and will react with it.
- the enzyme is used to alter the substrate in order to release the rinse benefit agent into the process. This means that if an enzyme is chosen, the group of substrates from which to select is given and vice versa.
- lipase substrates which are not necessarily natu- rally occurring, include but are not limited to lipids, mono-, di- and triglycerides such as tri- palmitin, palm oil, beeswax, jojoba wax, polyesters, ester wax, Polycaprolactone (PCL) and mixtures thereof.
- PCL Polycaprolactone
- cutinase degradable materials which are not necessarily naturally occurring, include but are not limited to triglycerides, waxes, polyesters and mixtures thereof.
- the enzyme is a cutinase and the enzyme substrate is selected from the group consisting of tripalmitin, palm oil, beeswax, jojoba wax, polyester ester wax, Polycaprolactone (PCL) and mixtures thereof.
- cellulase substrates include but are not limited to the group consisting of cellulose, methyl cellulose, ethyl cellulose, propyl cellulose, carboxy- methyl cellulose, cellulose monoacetate, cellulose diacetate, cellulose triacetate, Rayon, cu- prammonium rayon, crystalline cellulose, amorphous cellulose, beta 1 ,3-1-4 glucan and mixtures thereof.
- polysaccharide-comprising materials include but are not limited to gellan gum, xanthan gum, schizophillan gum, sclero- glucan gum, alginate, carageenan gum and pectin such as protopectin or pectic acid.
- the enzyme is pectate lyase and the enzyme substrate is selected from the group consisting of pectin of various modifications. If a xylanase is chosen a xylan-comprising material is given. Examples of xylan- comprising enzyme substrates include but are not limited to xylan and carboxymethyl xylan.
- the enzyme is a xylanase and the enzyme substrate is selected from the group consisting of to birch xylan, wheat xylan, oat husk xylan, corn cob xylan.
- amylase a starch-comprising enzyme substrate is given.
- Starch is a mixture of amylose and amylopectin. The ratio of these two components may vary. Naturally occurring forms occur in the 20:80 to 30:70 range.
- Amylases for the purpose of the invention, can mean any enzyme capable of modifying intermolecular bonds present in amylose or amylopectin.
- Blends of enzyme substrates mentioned in the above section are possible and may give unique barrier properties. Furthermore the barrier properties of such blends can be partially or totally destroyed through use of an enzyme acting on a component of the blend.
- enzyme substrate-enzyme pairs are: Polyhydroxyalkanoate (PHAs) such as polyhydroxybutyrate (PHB), poly-4- hydroxybutyrate (P4HB), polyhydroxyvalerate (PHV), polyhydroxyhexanoate (PHH), polyhy- droxyoctanoate (PHO) and their copolymers. These compounds were first identified in bacteria such as Alcaligenes eutrophus. PHAs. Enzymes that can modify PHAs have been identified such as Polyhydroxybutyrate depolymerase (EC 3.1.1.75).
- Enzymes relevant for modifying starch and starch based biopolymers are in a non limiting example: amylases, glucoamylase ((EC 3.2.1.3) and EC 3.2.1.20), amylase (EC 3.2.1.1 ); pullulanase (EC 3.2.1.41 ); maltogenic amylase (EC 3.2.1.133); neopullulanase (EC 3.2.1.135); maltotetraose-forming a-amylase (EC 3.2.1.60); isoamylase (EC 3.2.1.68); gluco- dextranase (EC 3.2.1.70); maltohexaose-forming a-amylase (EC 3.2.1.98); maltopentaose- forming a-amylase (EC 3.2.1.-).
- Suitable substrates for amylases include thermoplastic starch which is raw starch to which a flexibiliser and plasticiser such as sorbitol or glycine are added. The amounts of added plasticiser affect the properties of thermoplastic starch.
- Blending starch with degradable synthetic aliphatic polyesters such as PLA and PCL has recently become a focus of biodegradable plastic development.
- Biodegradable plastics can be prepared by blending up to 45% starch with degradable PCL. This new material is amenable to coating payload particles because the melting temperature is typically only 60 0 C and it gets soft at temperatures above 40 0 C.
- polyesters that are blended with starch to improve material mechanical properties are polybutylene succinate (PBS) or polybutylene succinate adipate (PBSA).
- PBS polybutylene succinate
- PBSA polybutylene succinate adipate
- a small amount (5% by weight) of compatibiliser maleic anhydride functionalised polyester
- starch content >60%, such sheets can become brittle.
- plasticisers are often added to reduce the brittleness and improve flexibility.
- Starch content, and addition of plasticisers can be used to alter the physical properties or melting temperature.
- Enzymes capable of modifying chitin are for example Chitinase (EC 3.2.1.14).
- Chitin is a polysaccharide that is synthesized from units of N-acetylglucosamine. These units form co- valent ⁇ -1 ,4 linkages (similar to the linkages between glucose units forming cellulose).
- the acetylamine group allows for increased hydrogen bonding between adjacent polymers, giving the chitin-polymer matrix increased strength.
- Chitin layers do exhibit barrier properties that can be modulated by the degree of acetylation or other modifications. Other known modifications include but are not limited too: phosphated chitin (P-chitin), phosphated-sulfated chitin (PS-chitin), and sulfated chitin (S-chitin).
- chitin can also be deacetylated by the action of enzymes such as chitin deacetylase (EC- 3.5.1.41 ). Full deacetylation leads to a con- version from chitin to chitosan. Chitosan can be gel like, water and fat absorbing and certainly not as mechanically strong as chitin. Therefore, one method of the invention is use of chitin as a barrier substance and a chitin deacetylase as the enzyme pair. Full or even partial deacetylation of the chitin in the formulated particle will allow for release of the payload. Furthermore, chitosan has bioadhesive effects thus conversion of all or some of the chitin in the barrier may also affect binding of the particles to components in the chosen application.
- enzymes such as chitin deacetylase (EC- 3.5.1.41 ).
- Full deacetylation leads to a con- version from chitin to chitosan.
- Bioplastics polyester resins may be used such as Impranil® DLN Dispersion W 50 which is an anionic aliphatic polyester-polyurethane dispersion produced by Bayer (Bayer MaterialScience AG,D-51368 Leverkusen, Germany www.bayercoatings.com). The aqueous suspension can be applied to particles where the polyester can form a barrier.
- Bionolle is a biodegradable resin produced by Showa Highpolymer Co., Ltd, Japan. Ecoflex® is BASF's completely biodegradable and compostable plastic.
- BAK1095 is a thermoplastic polyester amide from Bayer.
- Polyester Wax is a synthetic wax (Nature, 1957, 179 1345). It has a low melting point of 37°C.
- the wax is soluble in most organic solvents, including alcohols, ethers, esters, ketones and hydrocarbons; warming to 25°C facilitates solution.
- Ester wax 1960 is a synthetic wax (Quarterly Journal of Microscopical Science, VoI
- This wax is typical of ester wax blends and consists of: Diethylene glycol disterate 6Og
- Polyethylene glycol disterate 10g Ester wax 1960 has a melting point of 48°C. Adjustments in the melting temperature are achieved by adjusting relative component concentrations.
- PCL Polycaprolactone
- EC Polycaprolactone
- PCL is a biodegradable polyester with a low melting point of around 60 0 C and a glass transition temperature of about -60 0 C.
- PCL can be prepared by ring opening polymerization of ⁇ -caprolactone using a catalyst such as stannous octanoate.
- a catalyst such as stannous octanoate.
- PCL can be blended with starch to form thermoplastic starches.
- Amylose degrading enzymes can be used to degrade such blends.
- PCL itself is degradable with serine esterases.
- lipases EC
- the following natural products can also be degraded with serine esterases such as lipase and cutinase; rosin gum, bees wax, jojoba wax.
- serine esterases such as lipase and cutinase
- rosin gum such as bees wax
- jojoba wax essentially any natural fat or oil can be used in the invention as a barrier and these can be degraded by serine esterases such as lipase or cutinase.
- the particle may further comprise known conventional materials used in formulation of active components as auxiliary particle components such as binders, solvents, fillers etc., e.g. as described in WO 89/08694, WO 89/08695, EP 270608 B1 and/or WO 00/01793.
- Suitable fillers are water soluble and/or inorganic salts such as finely ground alkali sulphate, alkali carbonate and/or alkali chloride), clays such as kaolin (e.g. SpeswhiteTM, English China Clay), bentonites, talcs, zeolites such as zelolite 4A or zeolite A24, chalk, calcium carbonate, silicates and/or silicas.
- inorganic salts such as finely ground alkali sulphate, alkali carbonate and/or alkali chloride
- clays such as kaolin (e.g. SpeswhiteTM, English China Clay), bentonites, talcs, zeolites such as zelolite 4A or zeolite A24, chalk, calcium carbonate, silicates and/or silicas.
- Suitable binders are binders with a high melting point or no melting point at all and of a non waxy nature e.g. polyvinyl pyrrolidone, polyvinylalcohol, high melting point ethoxylated alcohols, high melting point polyethyleneglycols or polyethylene oxides, cellulose derivatives, for example hydroxypropyl cellulose, hydroxypropyl methyl cellulose, methyl cellulose or carboxy methyl cellulose, carbohydrate binders like starch, dextrin, maltodextrin, pregelati- nized starch, sugars and polyols, for example sucrose, mannitol, lactose and sorbitol, gums like gum arabic, pectin or alginate, protein-type binders like gelatin or any other binder known in the art.
- a suitable binder is a carbohydrate binder such as Glucidex 21 D available from Roquette Freres, France or Avedex W80 from Avebe
- the invention further provides a process for preparing the particle of the invention.
- the particles may be prepared by methods known to those skilled in the art of granulation, including mixer granulation, fluid bed coating, prilling, disc granulation, pan drum coat- ing, spray drying, extrusion, fluid bed spray drying, high shear agglomeration, spheronization or combinations of these techniques.
- Particles of relevance may be but are not limited to layered products, absorbed products, pelletized products, and prilled products.
- the particles may optionally be dried after granulation.
- the particles may further be sieved after granulation. Methods for preparing the particle can be found in Handbook of Powder Technology;
- Preparation methods include known granulation technologies, i.e.: a) Spray dried products, wherein a liquid rinse benefit agent-containing solution is atomized in a spray drying tower to form small droplets which during their way down the drying tower dry to form a rinse benefit agent-containing particulate material. Very small particles can be produced this way (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; vol. 71 ; page 140-142; Marcel Dekker).
- Fluid bed granulation involves suspending particulates in an air stream and spraying a liquid onto the fluidized particles via nozzles. Particles hit by spray droplets get wetted and become tacky. The tacky particles collide with other particles and adhere to them and form a granule.
- the cores and particles may be subjected to drying, such as in a fluid bed drier.
- the drying preferably takes place at a product temperature of from 25 to 9O 0 C.
- the cores preferably contain 0.1-10 % w/w water.
- Layers may be applied onto the particle comprising the active component by atomiza- tion onto the particles in a fluid bed or a fluid bed spray dryer, the layers may further be applied in mixers, dragee type coaters (pan-drum coaters), equipment for coating of seeds, equipment comprising rotating bottoms (eks. Roto Glatt, CF granulators (Freund), torbed processors (Gauda) or in rotating fluid bed processors such as Omnitex (Nara).
- mixers dragee type coaters (pan-drum coaters), equipment for coating of seeds, equipment comprising rotating bottoms (eks. Roto Glatt, CF granulators (Freund), torbed processors (Gauda) or in rotating fluid bed processors such as Omnitex (Nara).
- the particle may optionally be dried.
- the drying of the particle can be achieved by any drying method available to the skilled person, such as spray- drying, freeze drying, vacuum drying, fluid bed drying, pan drum coating and microwave dry- ing. Drying of the particle can also be combined with granulation methods which comprise e.g. the use of a fluid bed, a fluid bed spray dryer (FSD) or a Multi-stage dryer (MSD).
- FSD fluid bed spray dryer
- MSD Multi-stage dryer
- the substrate coating is applied via hot melt coating in a fluid bed.
- This method is well known in the art.
- the melted coating material is sprayed onto the cores in a fluidized bed.
- the fluidization gas has a temperature below the solidification temperature of the coating material (see e.g. "Fluid Bed Coating” by Teunou & Poncelet in “Encapsulated And Powdered Foods", edited by Onwulata, CRC Press 2005).
- the process for preparing the particle of the invention comprises the steps of: a) preparing a core comprising a benefit agent; b) optionally applying a protective layer onto the core of a); c) applying a layer comprising an enzyme; and d) applying one or more barrier layer(s) comprising a material which is degradable by the enzyme of c).
- a) preparing a core comprising a benefit agent b) optionally applying a protective layer onto the core of a
- c) applying a layer comprising an enzyme a layer comprising an enzyme
- one or more barrier layer(s) comprising a material which is degradable by the enzyme of c).
- optional further coating comprises the steps of: a) preparing a core comprising a benefit agent; b) optionally applying a protective layer onto the core of a); c) applying a layer comprising an enzyme; and d) applying one or more barrier layer(s) comprising a material which is degradable by the enzyme of c).
- the particle may comprise further layers or coatings besides the barrier layer to provide further improved properties of the particle.
- the particles may be pre-coated by applying a protective pre-coat to cores comprising the rinse benefit agent before applying the coating according to the invention.
- the pre-coat may serve to protect and retain the rinse benefit agent during the further processing and may consist, e.g., of a fat or oil.
- compositions comprising the particle and their application
- the particles of the invention may be added to cleaning compositions, including fabric and home care detergent products, for use in treatment of textile and hard surfaces.
- the particles of the invention may be used as a component of a detergent composition.
- the detergent composition may for example be formulated as a laundry or dishwash detergent composition for hand or machine washings including a cleaning additive composition suitable for pre-treatment of stained fabrics or a fabric softener composition, or a detergent composition for use in general household hard surface cleaning operations, or a composition for hand or machine dishwashing operations.
- the detergent composition may be in any convenient dry form, e.g., a bar, a tablet, a powder, a particle or a paste. It may also be a liquid detergent, in particular low-content aqueous (less than 70% by weight) or non-aqueous liquid detergent.
- the detergent composition comprises one or more surfactants, which may be non- ionic including semi-polar and/or anionic and/or cationic and/or zwitterionic.
- the level of surfactants is typically from 0.1 % to 60% by weight. In a dishwash detergent, it is typically from 0.1 to 15%, particularly 2-12%.
- the detergent When included therein the detergent will usually contain from about 1% to about 40% of an anionic surfactant such as linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap.
- an anionic surfactant such as linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap.
- the detergent When included therein the detergent will usually contain from about 0.2% to about 40% of a non-ionic surfactant such as alcohol ethoxylate, nonylphenol ethoxylate, alkylpoly- glycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or N-acyl N-alkyl derivatives of glucosamine ("glucamides").
- glucamides N-acyl N-alkyl derivatives of glucosamine
- the detergent may contain 0-65 % of a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, carbonate, citrate, nitrilotriacetic acid, ethyl- enediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g. SKS-6 from Hoechst).
- a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, carbonate, citrate, nitrilotriacetic acid, ethyl- enediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g. SKS-6 from Hoechst).
- the level of builder is typically 40-65%, particularly
- the detergent composition may comprise one or more other enzymes such as a protease, a lipase, a cutinase, an amylase, a carbohydrase, a cellulase, a pectinase, a man- nanase, an arabinase, a galactanase, a xylanase, an oxidase, e.g., a laccase, and/or a peroxidase
- the detergent may comprise one or more polymers.
- Examples are carboxymethylcel- lulose, poly(vinylpyrrolidone), poly (ethylene glycol), polyvinyl alcohol), poly(vinylpyridine-N- oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.
- the detergent may contain a bleaching system, which may comprise a H 2 O 2 source such as perborate or percarbonate, which may be combined with a peracid-forming bleach activator such as tetraacetylethylenediamine or nonanoyloxybenzenesulfonate.
- a bleaching system may comprise peroxyacids of e.g. the amide, imide, or sulfone type.
- a dishwash detergent typically contains 10-30% of bleaching system.
- the detergent may also contain other conventional detergent ingredients such as e.g. fabric conditioners including clays, foam boosters, suds suppressors, anti-corrosion agents, soil-suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, or perfumes.
- fabric conditioners including clays, foam boosters, suds suppressors, anti-corrosion agents, soil-suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, or perfumes.
- rinse cycle means the cycle after the main wash cycle in a laundry washing or dish washing process wherein the wash load is treated with rinse water to remove the detergent for the wash load.
- the particles release the rinse benefit agent(s) into one or more of the rinse cycles subsequent to the main wash cycle in order to maximise the effectiveness of the rinse benefit agent. It is envis- aged that the current invention may be employed in a wide range of wash processes and hence it may be necessary to adjust the composition and/or morphology of particle to optimise its release characteristics.
- Typical wash processes would include the use of front loading automatic machines which may include a lengthy high temperature wash cycle with high levels of mechanical agi- tation followed by two, three or four short rinse cycles. Top loading automatic or semi automatic machines may be used which would involve the use of a shorter, low temperature main wash cycle followed by only one or two rinse cycles. It is also anticipated that the current invention will be utilized in hand wash processes, where the wash cycle is at ambient temperature and is of varying length and involving variable levels of mechanical agitation. In this hand-wash process, the number of rinse cycles may vary from one to seven.
- the triggered-release particles are incorporated in the main detergent composition and are hence dosed into the wash process in a manner that is typically associated with the specific wash process and will be well known to those skilled in the art.
- the triggered-release particles are incorporated in an ancillary detergent component that is contained in a dosing device that keeps it separate from the main detergent composition until both are in contact with the liquor of the main wash cycle and aids retention of the intact particles within the wash vessel from one cycle to the next.
- Example 1 This example describes a screening assay to assess the activity profile (enzymatic activity under wash versus rinse conditions in a laundry process, respectively) of combinations or pairs of enzymes and substrates.
- the aim of this assay is to select pairs of enzymes and substrates which display the desired activity profile, namely low enzymatic activity during wash conditions relative to the enzymatic activity during rinse.
- Table 1 we provide the activity index (score parameter) from comparison of a series of data. For a given pair of enzyme and substrate, enzymatic activity was quantified under wash and rinse conditions, respectively. The activity index results from the difference in net activity during rinse and wash, multiplied by the sum of the activities during wash and rinse.
- Table 1 below lists the activity index calculated for a series of pre- ferred hydrophobic substrates and two esterases, a cutinase and a lipase. Note that the polyester systems display a negative activity index, indicating that these combinations of enzymes and potential substrates are hydrolyzed faster under wash conditions than under rinse conditions. Particularly high activity indices were recorded for glycerides in combination with a lipase, specifically mono-, di- and tripalmitin. The specific experiments were carried out in a beaker format at room temperature; alternatively this type of assay could take form as a HTS assay in microtiter plates. The potential substrates were suspended with the non-ionic surfactant TX-100 in a buffer solution adjusted to pH 9. We evaluated enzymatic activity in this assay by monitoring the change in pH due to hydrolysis using a standard pH-meter. Alternative methods include but are not limited to light scattering, calorimetry, ultrasound velocimetry, and spectrophotometry. Table 1
- a sample of 4 kg of Na 2 SO 4 cores (350 - 500 ⁇ m) was transferred to a GEA MP 3/2/3 conventional fluid bed apparatus.
- a bottom spray/Wurster coating technique with an air inlet temperature of ca. 65 0 C, air outlet temperature of ca. 43 0 C and with air quantity of 250 kg per hour the following steps were carried out in sequence: a) an enzyme containing layer was applied onto the Na 2 SO 4 cores by spraying a Sav- inase® (protease) aqueous solution (concentrate) at a rate of 30 g per minute. Approximately 250 g Savinase® concentrate were applied per kg cores.
- An enzyme containing granule was produced as in Example 2, with the exception that no lipase coating was applied to the product.
- Example 5 An enzyme containing granule was produced as in Example 2, with the exception that no lipase coating was applied and PEG 4000 was used as final coating instead of tripalmitin.
- Example 5 An enzyme containing granule was produced as in Example 2, with the exception that no lipase coating was applied and PEG 4000 was used as final coating instead of tripalmitin.
- An enzyme containing granule was produced as in example 2, with he exception that palm oil was used instead of tripalmitin as substrate and spray dried lipase was mixed into the palm oil before the coating comprising the substrate and the lipase was applied to the core particle.
- the release profile of the granules produced as in Example 2, 3 and 4 during wash and rinse conditions was studied by use of the following assay: a) 0.6 g of liquid detergent (comprising 30% water, 20% Neodol 25-7EO [ex Shell Chemicals], 14% alkyl benzene sulphonic acid, 9% mono propylene glycol, 7% sodium lauryl tri-ethoxy sulphate, 5% glycerol, 5% Prifac 5908 [ex Uniqema], 3% triethanolamine, 3% sodium hydroxide, 1 % citric acid) was added to 100 ml of water (dH° 12) in a beaker glass.
- liquid detergent comprising 30% water, 20% Neodol 25-7EO [ex Shell Chemicals], 14% alkyl benzene sulphonic acid, 9% mono propylene glycol, 7% sodium lauryl tri-ethoxy sulphate, 5% glycerol, 5% Prifac 5908 [
- Perfume-containing granule cores were produced batchwise by adding 1.86 kg of zeo- lite A24 to a Roto Junior mixer (ex Zanchetta). The impellor and chopper were switched-on and 250 g of a perfume (comprising 1 1.3% 1-acetate, 2-(1 ,1-dimethylethyl)-cyclohexanol, 1.6% 1-(2,6,6-trimethyl-3-cyclohexen-1-yl)-2-buten-1-one, 6.6% dodecanal, 6.7% 4-(2,6,6- trimethyl-1-cyclohexen-1-yl)-3-buten-2-one, 6.7% 4,7-Methano-1 H-inden-6-ol, 3a,4,5,6,7,7a- hexahydro-, 6-acetate, 6.7% 2-ethyl-4-(2,2,3-trimethyl-3-cyclopenten-1-yl)-2-buten-1-ol, 6.7% I ⁇ I ⁇ .S ⁇ .S
- a sample of 3 kg of perfume-containing granule cores produced as an Example 7 was transferred to a GEA MP 3/2/3 conventional fluid bed apparatus.
- a bottom spray/Wurster coating technique with an air inlet temperature of ca. 65 0 C, air outlet temperature of ca. 43 0 C and with air quantity of 250 kg per hour the following steps were carried out in sequence: a) an enzyme containing layer was applied onto the agglomerated Zeolite cores (350 - 700 ⁇ m) by spraying a Lipex® aqueous solution (0.6 g Lipex® concentrate in 1 kg of water) at a rate of 35 g per minute. Approximately 0.02 g Lipex® were applied per kg cores.
- a final coating was applied by spraying 200 g of melted (heated to ca. 100 0 C) tri- palmitin per kg product, at a spraying rate of 30 g per minute.
- a sample of 10 kg of Zeolite powder was transferred to a conventional Lodiger mixer.
- the shovel speed was approximately 180 rpm, the knife speed was 3000 rpm and the mixer temperature was around 40 0 C.
- PEG4000 to the Zeolite powder granulated particles was generated.
- the granules were sieved between 300 and 800 micron.
- a sample of 5 kg of sieved Zeolite/PEG4000 granules was transferred to a Lodiger mixer.
- the shovel speed was approximately 180 rpm and the mixer temperature was kept at room temperature.
- 1 kg of AKK perfume was absorbed into the granules by slowly adding the perfume.
- a sample of 3 kg of Zeolite/PEG4000 granules with absorbed perfume was transferred to a Lodiger mixer.
- the shovel speed was approximately 180 rpm and the mixer temperature was kept at room temperature.
- a pre-coat was applied by slowly adding 0.3 kg of melted (75 0 C) palm oil (Palmotex 16T, Aarhus Oliefabrik A/S, Aarhus, Denmark) to the granules.
- a sample of 0.75 kg of pre-coated granules was transferred to a STREA conventional fluid bed.
- a top spray coating technique with an air inlet temperature of ca. 30 0 C, air outlet temperature of ca. 40 0 C and with air quantity of 70 kg per hour the final coating were applied by spraying 0.25 kg of melted (80 0 C) tripalmitin, at a spray rate of 25 g per minutes.
- a sample of 0.75 kg of pre-coated granules was transferred to a STREA conventional fluid bed.
- a top spray coating technique with an air inlet temperature of ca. 30 0 C, air outlet temperature of ca. 40 0 C and with air quantity of 70 kg per hour the final coating were carried out in the following sequence: first an aqueous lipase solution (1.1 g Thermomyces lanuginosus lipase concentrate (LipolaseTM, Thermomyces lanuginosus lipase with a total activity of 2200 KLU) in 0.1 kg of water) is sprayed onto the product at a spraying rate of 15 g per minutes, then followed by spraying 0.25 kg of melted (80 0 C) tripalmitin, at a spray rate of 25 g per minutes.
- LipolaseTM Thermomyces lanuginosus lipase concentrate
- a sample of 0.75 kg of pre-coated granules was transferred to a STREA conventional fluid bed.
- a top spray coating technique with an air inlet temperature of ca. 30 0 C, air outlet temperature of ca. 40 0 C and with air quantity of 70 kg per hour the final coating were applied by spraying 0.25 kg of melted (80 0 C) PEG4000, at a spray rate of 25 g per minutes.
- 190 g of sieved Zeolite/PEG4000 granules prepared as in Example 9 were dosed with 10 g of AKK perfume, pre-coated with 20 g of Palmotex 16T, followed by coating with 50 g of tripalmitin.
- 0.07 g of spray-dried lipase was added to the tripalmitin, and in another sample 0.07 g of spray-dried lipase was added to the Palmotex.
- Two further samples were prepared in the same manner, excerpt that PEG4000 was used instead of Palmotex.
- An enzyme containing granule is produced as in example 2, with the exception that a pectate lyase is used instead of a lipase, and 5 % (W/W) poly-galacturonic acid as substrate is mixed with tripalmitin before the coating is applied to the core particle.
- An enzyme containing granule is produced as in example 2, with the exception that a cellulase is used instead of a lipase, and 5 % (W/W) barley beta-glucan as substrate is mixed with tripalmitin before the coating is applied to the core particle.
- Example 13 An enzyme containing granule is produced as in example 2, with the exception that a cellulase is used instead of a lipase, and 5 % (W/W) barley beta-glucan as substrate is mixed with tripalmitin before the coating is applied to the core particle.
- An enzyme containing granule is produced as in example 2, with the exception that an amylase is used instead of a lipase, and 5 % (W/W) potato starch as substrate is mixed with tripalmitin before the coating is applied to the core particle.
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Abstract
Description
Claims
Priority Applications (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
ES09726019.4T ES2442718T3 (en) | 2008-03-28 | 2009-03-25 | Detergent composition comprising an enzyme activated release system |
CN2009801193297A CN102046766B (en) | 2008-03-28 | 2009-03-25 | Detergent composition comprising a triggered release system |
AU2009228822A AU2009228822B2 (en) | 2008-03-28 | 2009-03-25 | Detergent composition comprising a triggered release system |
BRPI0909729A BRPI0909729A2 (en) | 2008-03-28 | 2009-03-25 | detergent composition comprising a triggered release particle, and process for preparing a detergent composition |
EP09726019.4A EP2254982B1 (en) | 2008-03-28 | 2009-03-25 | Detergent composition comprising an enzyme triggered release system |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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EP08153568 | 2008-03-28 | ||
EP08153568.4 | 2008-03-28 |
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WO2009118349A1 true WO2009118349A1 (en) | 2009-10-01 |
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PCT/EP2009/053534 WO2009118349A1 (en) | 2008-03-28 | 2009-03-25 | Detergent composition comprising a triggered release system |
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Country | Link |
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EP (1) | EP2254982B1 (en) |
CN (1) | CN102046766B (en) |
AR (1) | AR071093A1 (en) |
AU (1) | AU2009228822B2 (en) |
BR (1) | BRPI0909729A2 (en) |
CL (1) | CL2009000764A1 (en) |
ES (1) | ES2442718T3 (en) |
WO (1) | WO2009118349A1 (en) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN105925399A (en) * | 2016-04-28 | 2016-09-07 | 山西勇宁记科技有限公司 | High-efficiency complex lipase for detergents |
WO2017070131A3 (en) * | 2015-10-19 | 2017-06-08 | The Procter & Gamble Company | Particles for malodor reduction |
US11879112B2 (en) | 2017-08-24 | 2024-01-23 | Conopco, Inc. | Foam control ingredient comprising glycerol monooleate sorbed on zeolite for detergent composition |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
TWI645028B (en) * | 2013-10-16 | 2018-12-21 | 梅拉洛伊卡公司 | Powdered automatic dishwashing detergent |
WO2017116398A1 (en) * | 2015-12-28 | 2017-07-06 | Colgate-Palmolive Company | Fabric softening compositions |
US10538720B2 (en) | 2016-03-08 | 2020-01-21 | The Procter & Gamble Company | Particles including enzyme |
GB202210371D0 (en) * | 2022-07-14 | 2022-08-31 | Reckitt Benckiser Finish Bv | Detergents |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1997022680A1 (en) * | 1995-12-20 | 1997-06-26 | The Procter & Gamble Company | Bleach catalyst plus enzyme particles |
WO1999029820A1 (en) * | 1997-12-10 | 1999-06-17 | Henkel Kommanditgesellschaft Auf Aktien | Enzyme granulate containing cellulase |
US20030191043A1 (en) * | 2001-06-01 | 2003-10-09 | Becker Nathaniel T. | Methods and formulations for enhancing the dissolution of a solid material in liquid |
-
2009
- 2009-03-25 BR BRPI0909729A patent/BRPI0909729A2/en not_active Application Discontinuation
- 2009-03-25 EP EP09726019.4A patent/EP2254982B1/en not_active Revoked
- 2009-03-25 AU AU2009228822A patent/AU2009228822B2/en not_active Ceased
- 2009-03-25 ES ES09726019.4T patent/ES2442718T3/en active Active
- 2009-03-25 CN CN2009801193297A patent/CN102046766B/en active Active
- 2009-03-25 WO PCT/EP2009/053534 patent/WO2009118349A1/en active Application Filing
- 2009-03-27 AR ARP090101093A patent/AR071093A1/en active IP Right Grant
- 2009-03-27 CL CL2009000764A patent/CL2009000764A1/en unknown
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1997022680A1 (en) * | 1995-12-20 | 1997-06-26 | The Procter & Gamble Company | Bleach catalyst plus enzyme particles |
WO1999029820A1 (en) * | 1997-12-10 | 1999-06-17 | Henkel Kommanditgesellschaft Auf Aktien | Enzyme granulate containing cellulase |
US20030191043A1 (en) * | 2001-06-01 | 2003-10-09 | Becker Nathaniel T. | Methods and formulations for enhancing the dissolution of a solid material in liquid |
Cited By (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2017070131A3 (en) * | 2015-10-19 | 2017-06-08 | The Procter & Gamble Company | Particles for malodor reduction |
US9714401B2 (en) | 2015-10-19 | 2017-07-25 | The Procter & Gamble Company | Particles for malodor reduction |
US10240108B2 (en) | 2015-10-19 | 2019-03-26 | The Procter & Gamble Company | Particles for malodor reduction |
CN105925399A (en) * | 2016-04-28 | 2016-09-07 | 山西勇宁记科技有限公司 | High-efficiency complex lipase for detergents |
US11879112B2 (en) | 2017-08-24 | 2024-01-23 | Conopco, Inc. | Foam control ingredient comprising glycerol monooleate sorbed on zeolite for detergent composition |
Also Published As
Publication number | Publication date |
---|---|
EP2254982A1 (en) | 2010-12-01 |
AR071093A1 (en) | 2010-05-26 |
AU2009228822B2 (en) | 2012-03-01 |
CN102046766A (en) | 2011-05-04 |
AU2009228822A1 (en) | 2009-10-01 |
CN102046766B (en) | 2013-06-12 |
CL2009000764A1 (en) | 2010-01-15 |
BRPI0909729A2 (en) | 2015-10-06 |
EP2254982B1 (en) | 2013-10-16 |
ES2442718T3 (en) | 2014-02-13 |
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