Particulate composition

Patent metadata

Field	Value
Publication number	US-10829721-B2
Application number	US-201214127712-A
Country	US
Kind code	B2
Filing date	Jun 14, 2012
Priority date	Jun 20, 2011
Publication date	Nov 10, 2020
Grant date	Nov 10, 2020

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.

First claim

The invention claimed is:

1. A particulate composition comprising:
a) particles comprising a source of organic peroxyacids, said particles having a time required to release 50% of the organic peroxyacids at 20° C. which is below 100 seconds, 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 such that the particles have a time required to release 50% of the enzyme activity at 20° C. which is at least 100 seconds

wherein the delayed-release coating comprises a substrate for the first-wash lipolytic enzyme selected from lipids, mono-, di- and triglycerides, palm oil, beeswax, jojoba oil, carnauba wax, polyesters, polyester block copolymers and polycaprolactone.

2. The particulate composition of claim 1 wherein the bleach catalyst is an organic bleach catalyst, a non-metal bleach catalyst or a catalytic metal complex.

3. The particulate composition of claim 1 wherein the enzyme is sensitive to the bleach catalyst.

4. The particulate composition of claim 1 wherein the enzyme activity is selected from the group consisting of a triacylglycerol lipase EC 3.1.1.3, cutinase EC 11.1.74, sterol esterase EC 3.1.1.13, and wax-ester hydrolase EC 3.1.1.50.

5. 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.

6. 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.

7. The particulate composition of claim 1 wherein the enzyme comprises a cutinase, preferably selected from variants of Pseudomonas mendocina cutinase and Humicola insolens cutinase.

8. The particulate composition of claim 1 , wherein the source of organic peroxyacids is a preformed peracid or a diacyl peroxide.

9. The particulate composition of claim 1 , wherein the source of organic peroxyacids comprises a source of hydrogen peroxide and a bleach activator.

10. 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.

11. 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.

12. The particulate composition of claim 1 wherein the delayed-release coating comprises a hydrophobic substance and a water-insoluble substance.

13. The particulate composition of claim 12 wherein the hydrophobic substance is a fat or wax.

14. The particulate composition of claim 12 wherein the water-insoluble substance is titanium dioxide, calcium carbonate or kaolin.

15. The particulate composition of claim 1 wherein the delayed-release coating comprises a substrate for the enzyme.

16. The particulate composition of claim 1 wherein the enzyme-containing particles (c) further comprise an additional top coating selected from the group consisting of polyethylene glycol, polyvinyl alcohol and hydroxypropyl methyl cellulose.

17. 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.

18. 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.

19. 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.

Assignees

• Simonsen Ole
• Hansen Carsten Hoerslev
• Erlandsen Luise
• Novozymes As

Inventors

• Simonsen Ole
• Hansen Carsten Hoerslev
• Erlandsen Luise

Classifications

• C11D3/38672 Primary

  Granulated or coated enzymes · CPC title

• C11D3/3932

  Inorganic compounds or complexes · CPC title

• C12N9/98 Primary

  Preparation of granular or free-flowing enzyme compositions (C12N9/96 takes precedence) · CPC title

• C11D3/38636

  containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase · CPC title

• C11D3/3945

  Organic per-compounds (C11D3/3902 takes precedence) · CPC title