Particulate Composition

Abstract

Enzymes tend to be inactivated during wash by a bleach catalyst in combination with a source of organic peroxyacids. The risk of enzyme inactivation by active bleach catalyst is reduced when the release of the enzyme into the wash solution is delayed. The enzyme stability during washing together with a bleach catalyst can be improved by applying a delayed-release coating to cores which comprise the enzyme.

1 : A particulate composition comprising:
 a) particles comprising a source of organic peroxyacids, and   b) particles comprising a non-metal bleach catalyst, and   c) particles comprising
 i) a core comprising an enzyme surrounded by 
 ii) a delayed-release coating. 
   
     
     
         2 : The particulate composition of  claim 1  wherein the enzyme is an amylase, a carbohydrase, a protease, a lipolytic enzyme, a cellulase, an oxidoreductase, a mannanase or a pectate lyase. 
     
     
         3 : A particulate composition comprising:
 a) particles comprising a source of organic peroxyacids, and   b) particles comprising a bleach catalyst, and   c) particles comprising
 i) a core comprising an enzyme which is a first-wash lipolytic enzyme, surrounded by 
 ii) a delayed-release coating. 
   
     
     
         4 : The particulate composition of  claim 3  wherein the bleach catalyst is an organic bleach catalyst, a non-metal bleach catalyst or a catalytic metal complex. 
     
     
         5 : The particulate composition of  claim 1  wherein the enzyme is sensitive to the bleach catalyst. 
     
     
         6 : The particulate composition of  claim 1  wherein the enzyme is a lipolytic enzyme which has lipase activity (triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74), sterol esterase (EC 3.1.1.13), and/or wax-ester hydrolase activity (EC 3.1.1.50). 
     
     
         7 : The particulate composition of  claim 1  wherein the enzyme is a lipase having at least 90% identity with the wild-type lipase derived from  Thermomyces lanuginosus  strain DSM 4109. 
     
     
         8 : The particulate composition of  claim 1  wherein the enzyme comprises a lipase selected from variants of  Thermomyces lanuginosus  lipase variants having the mutations T231R and N233R. 
     
     
         9 : The particulate composition of  claim 1  wherein the enzyme comprises a cutinase, preferably selected from variants of  Pseudomonas mendocina  cutinase and  Humicola insolens  cutinase. 
     
     
         10 : The particulate composition of  claim 1 , wherein the source of organic peroxyacids is a preformed peracid or a diacyl peroxide. 
     
     
         11 : The particulate composition of  claim 1 , wherein the source of organic peroxyacids comprises a source of hydrogen peroxide and a bleach activator. 
     
     
         12 : The particulate composition of  claim 1  wherein the bleach catalyst is organic and is selected among iminium cations and polyions; iminium zwitterions; modified amines; modified amine oxides; N-sulphonyl imines; N-phosphonyl imines; N-acyl imines; thiadiazole dioxides; perfluoroimines; and cyclic sugar ketones. 
     
     
         13 : The particulate composition of  claim 1  wherein the bleach catalyst has a structure corresponding to the general formula below: 
       
         
           
           
               
               
           
         
         wherein R 13  is a branched alkyl group containing from three to 24 carbon atoms (including the branching carbon atoms) or a linear alkyl group containing from one to 24 carbon atoms. 
       
     
     
         14 : The particulate composition of  claim 1  wherein the delayed-release coating comprises a hydrophobic substance and a water-insoluble substance. 
     
     
         15 : The particulate composition of  claim 14  wherein the hydrophobic substance is a fat or wax. 
     
     
         16 : The particulate composition of  claim 14  wherein the water-insoluble substance is titanium dioxide, calcium carbonate or kaolin. 
     
     
         17 : The particulate composition of  claim 1  wherein the delayed-release coating comprises a substrate for the enzyme. 
     
     
         18 : The particulate composition of  claim 1  wherein the enzyme-containinq particles (c) comprise an additional top coating, which preferably comprises polyethylene glycol (PEG), polyvinyl alcohol (PVA) or hydroxypropyl methyl cellulose (HPMC). 
     
     
         19 : The particulate composition of  claim 1  wherein the enzyme-containing particles (c) have a time for 50% release of enzyme in detergent solution at 20° C. of at least 300 seconds. 
     
     
         20 : The particulate composition of  claim 1  wherein the enzyme-containing particles (c) have a time required for release of 50% of the enzyme activity which is at least 1.5 times longer than the time required for similar enzyme granules without the coating. 
     
     
         21 : The particulate composition of  claim 1  wherein the enzyme-containing particles (c) have a time required for release of 90% of the enzyme activity which is at least 1.5 times longer than the time required for similar enzyme granules without the coating. 
     
     
         22 : A method of preparing lipase particles, comprising:
 a) testing the bleach-catalyst sensitivity of at least one enzyme by determining the wash performance for a combination of the enzyme with a bleach catalyst and a source of organic peroxyacids, and comparing with the performance without the bleach catalyst, to identify a bleach-catalyst sensitive enzyme,   b) providing a core comprising the sensitive enzyme, and surrounding the core with a delayed-release coating.