Danisco US Inc.

Genencor International, Inc.

The Procter Gamble Company

Other

Genencor, Inc.

University of California

Thomas P Graycar

David Aaron Estell

Richard Ray Bott

Ayrookaran J Poulose

Robert Mark Caldwell

Lori Jean Wilson

Sina Pricelius

Clement K Choy

Andrew Shaw

Scott Douglas Power

Brian E Jones

Kathleen A Clarkson

Katherine D Collier

Edmund A Larenas

Nathaniel T Becker

Walter Weyler

Andre Cesar Baeck

Chanchal Kumar Ghosh

Donn N Rubingh

Chris Leeflang

Casper Vroemen

Sandra W Ramer

Melodie Estabrook

Philip Frederick Brode, Iii

Bobby Lee Barnett

Matthew Grant Boston

Edit L Braunstein

You-Lo Hsieh

Claudine Chang

Mary Michelle Hartzell

Mansi Goyal

Victoria E Huang

Colin Mitchinson

Marc Kolkman

Karsten Matthias Kragh

Elizabeth Ann Bodie

Deborah S Winetzky

Paul Elliott Correa

Grant C Ganshaw

J Bryan Jones

Casper Willem Vroemen

Yong Zhu

William S Borneman

Jacquelyn A Huitink

Saroj Rai

Matthew J Flynn

Casper Vroeman

Kerry Hollands

Peter F Plank

David L Wong

Su Yin Marina Chow

Marc Kolkmam

Karsten Kraugh

Victoria Huang

Karsten M Kragh

Su Yin Maria Chow

Described are compositions and methods relating to the expression of β-glucosidase in yeast for use in industrial ethanol production. The yeast demonstrates increased ethanol production and reduced production of unwanted side-products, including acetate. Such yeast is particularly useful for large-scale ethanol production from starch substrates.

Expression of beta-glucosidase in yeast for improved ethanol production

The present invention provides lipolytic enzyme variants. Specifically, the present invention provides lipolytic enzyme variants having one or more modifications as compared to a parent lipolytic enzyme having at least one improved property. In addition, the present invention provides compositions comprising a lipolytic enzyme variant of the invention. The present invention also provides methods of cleaning using compositions comprising a lipolytic enzyme variant of the invention.

Compositions and methods comprising a lipolytic enzyme variant

The present invention provides lipolytic enzyme variants. Specifically, the present invention provides lipolytic enzyme variants having two, three, or more modifications as compared to a parent lipolytic enzyme and having at least one improved property. In addition, the present invention provides compositions comprising a lipolytic enzyme variant of the invention. The present invention also provides methods of cleaning using compositions comprising a lipolytic enzyme variant of the invention.

Embodiments of the present disclosure relate toglucoamylase (TrGA) variants having improved properties (e.g., improved thermostability, improved specific activity, and/or resistant to oxidation-related activity loss). Also provided are compositions comprising variant glucoamylases. These compositions are useful in various starch process applications.

Trichoderma reesei glucoamylase variants resistant to oxidation-related activity loss and the use thereof

Variants ofsp. TS-23 strain alpha-amylases exhibit improved enzymatic performance, including increased thermostability, reduced calcium dependence, increased washing/cleaning performance, and baking ability. Compositions comprising these variants are useful in methods of starch processing, starch liquefaction, fermatation, starch saccharification, cleaning, laundrying, textile desizing, baking, and biofilm removal.

[object Object]

Variants ofsp. TS-23 strain alpha-amylases exhibit improved enzymatic performance, including increased themostability, reduced calcium dependence, increased washing/cleaning performance, and baking ability. Compositions comprising these variants are useful in methods of starch processing, starch liquefaction, fermatation, starch saccharification, cleaning, laundrying, textile desizing, baking, and biofilm removal.

Novel carbonyl hydrolase variants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases are disclosed. The variant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor carbonyl hydrolase. Such variant carbonyl hydrolases have properties which are different from those of the precursor hydrolase, such as altered proteolytic activity, altered stability, etc. The substituted amino acid residues correspond to positions +76 in combination with one or more of the following residues +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265 and/or +274 insubtilisin.

Subtilisin variants

Enzyme granulates contain besides the enzyme water-soluble and water-insoluble fillers, binders and if required other additives for granulates. In order to stabilize the enzyme, an alkaline or earth alkaline metal formiate is added, as well as reducing sugar, if required. These enzyme granulates may contain all usual enzymes for washing and cleaning purposes, in particular alkaline proteases. A process for preparing these enzyme granulates, as well as their use in powdery washing product compositions are also disclosed.

Accelerated stability test

Novel carbonyl hydrolase variants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases are disclosed. The variant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor carbonyl hydrolase. Such variant carbonyl hydrolases have properties which are different from those of the precursor hydrolase, such as altered proteolytic activity, altered stability, etc. The substituted amino acid residues correspond to positions &plus;76 in combination with one or more of the following residues &plus;99, &plus;101, &plus;103, &plus;104, &plus;107, &plus;123, &plus;27, &plus;105, &plus;109, &plus;126, &plus;128, &plus;135, &plus;156, &plus;166, &plus;195, &plus;197, &plus;204, &plus;206, &plus;210, &plus;216, &plus;217, &plus;218, &plus;222, &plus;260, &plus;265 and/or &plus;274 in subtilisin.

Subtilisin variants multiply-substituted subtilising variants having a substitution at position 76

Textile fibers are treated with enzymes in the absence of surfactants, with the effect of increasing the wettability and absorbency of the fibers. The enzymes are pectinases, cellulases, proteases, lipases or combinations thereof. The wetting properties of cotton fibers are found to be most substantially improved by treatment with a mixture of cellulase and pectinase. The effects of five hydrolyzing enzymes on improving the hydrophilicity of several polyester fabrics have been studied. Four out of the five lipases studied improve the water wetting and absorbent properties of the regular polyester fabrics more than alkaline hydrolysis under optimal conditions (3N NaOH at 55&deg; C. for 2 hours). Compared to aqueous hydrolysis, the enzyme reactions have shown to be effective under more moderate conditions, including a relatively low concentration (0.01 g/L), a shorter reaction time (10 minutes), at an ambient temperature (25&deg; C.). Contrary to the results with alkaline hydrolysis, the improved water wettability is accompanied by full strength retention. Lipase has also shown to be effective in improving the wetting and absorbent properties of sulfonated polyester and microdenier polyester fabrics.

Enzyme treatment to enhance wettability and absorbancy of textiles

Detergent formulations are prepared by directly agglomerating a fermentation broth extract, containing a detergent-type enzyme and a nonionic detergent-type surfactant, with a suitable detergent base mixture, without need for prior isolation of the enzyme.

Direct enzyme agglomeration process

The present relates to cleaning compositions comprising a protease enzyme which is a carbonyl variant having an amino acid sequence not found in nature, which is derived by replacement of a plurality of amino acid residues of a precursor carbonyl ydrolase with different amino acids.

Protease enzymes for tough cleaning and/or spot and film reduction and compositions incorporating same

Growing community of inventors

Pacifica, CA, United States of America

Thomas P Graycar