Genencor International, Inc.

Danisco US Inc.

Other

Genecor International, Inc.

Finnfeeds International Ltd.

University of California

Kathleen A Clarkson

Edmund A Larenas

Geoffrey L Weiss

Michael C Ward

Katherine D Collier

Benjamin S Bower

Timothy Fowler

Nigel S Dunn-Coleman

Suzanne E Lantz

Andrew J Morgan

Pushkaraj J Lad

Piet Van Solingen

Craig E Pilgrim

Michael Richard Bedford

Frits Goedegebuur

Scott Douglas Power

Bo Zhang

Thomas P Graycar

Martijn Scheffers

Casper Vroemen

Sharon Shoemaker

Ling Hua

Jing Ge

Zhongmei Tang

Michael D Ward

James T Kellis, Jr

Nathaniel T Becker

Toby M Baldwin

Elizabeth Ann Bodie

William Albert Cuevas

Deborah S Winetzky

Douglas A Dale

Edward Larenas

Jeffrey D Lorch

Matthew Grant Boston

Paula Johanna Maria Teunissen

You-Lo Hsieh

Jacquelyn A Huitink

Marco Van Brussel-Zwijnen

Mary Michelle Hartzell

Nancy S Bjork

Barbara A Swanson

Fred Fenel

Casper Willem Vroemen

Curran M Simpson

Pieter Van Solingen

Zhi C Wang

Hagen K Schulze

Kathy Collier

Eunice C Ashizawa

Moira B Kelly

M M Mullins

Lindsay Jacobs

Beth Fryksdale

Mark S Gerbert

Martijn Silvan Scheffers

Troels Gravesen

Michael Partsuf

Sharon P Shoemaker

A fungal &#x3b1;-amylase is provided from(AcAmy1). AcAmy1 has an optimal pH of 4.5 and is operable at 30-75&#xb0; C., allowing the enzyme to be used in combination with a glucoamylase in a saccharification reaction. This obviates the necessity of running a saccharification reaction as a batch process, where the pH and temperature must be readjusted for optimal use of the &#x3b1;-amylase or glucoamylase. AcAmy1 also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DP1+DP2) compared to the products of saccharification catalyzed by an &#x3b1;-amylase from. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.

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A fungal &#x3b1;-amylase is provided from(AcAmyl). AcAmyl has an optimal pH of 4.5 and is operable at 30-75&#xb0; C., allowing the enzyme to be used in combination with a glucoamylase in a saccharification reaction. This obviates the necessity of running a saccharification reaction as a batch process, where the pH and temperature must be readjusted for optimal use of the &#x3b1;-amylase or glucoamylase. AcAmyl also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DP1+DP2) compared to the products of saccharification catalyzed by an &#x3b1;-amylase from. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.

The use is provided composition as a feed additive which comprises one or more endoglucanases, and 0-20% by weight, based upon the content of cellulase proteins in the composition, of a cellobiohydrolase. The endoglycanases may be one or more of EGI, EGII, EGIII and any functionally active derivative of any thereof. Such endoglucanases may be obtained from a genetically modified strain of the fungus. Also provided is an enzyme-based feed additive which comprises EGI and/or EGII which lack the cellulose binding domain, and 0-20% by weight, based upon the content of cellulase proteins in the additive, of a cellobiohydrolase. A further enzyme-based feed additive is provided which comprises a cereal-based carrier, one or more endoglucanases, and 0-20% by weight, based upon the content of cellulase proteins in the additive, of a cellobiohydrolase.

Enzyme feed additive and animal feed including it

The present invention is directed to novel acid proteases and more specifically to NSP24 family proteases and NSP25 family proteases including biologically active fragments thereof and to nucleic acid molecules encoding said proteases. Also provided are vectors and host cells including nucleic acid sequences coding for the proteases, methods for producing the proteases, enzyme compositions and methods employing said proteases.

Acid fungal proteases

The present invention relates to the co-expression and production of a heterologous alpha amylase and an endogenous glucoamylase in anstrain and enzyme compositions including the same.

DNA is provided which encodes an enzyme having phytase activity isolated fromand. Also provided for is a method of isolating DNA encoding an enzyme having phytase activity from organisms which possess such DNA, transformation of the DNA into a suitable host organism, expression of the transformed DNA and the use of the expressed phytase protein in feed as a supplement.

Phytase enzymes, nucleic acid sequences encoding phytase enzymes and vectors and host cells incorporating same

DNA is provided which encodes an enzyme having phytase activity isolated fromandAlso provided for is a method of isolating DNA encoding an enzyme having phytase activity from organisms which possess such DNA, transformation of the DNA into a suitable host organism, expression of the transformed DNA and the use of the expressed phytase protein in feed as a supplement.

The invention is directed to modified xylanases having increased stability in harsh industrial environments, such as increased pH and/or temperature.

Modified enzymes, methods to produce modified enzymes and use thereof

The use is provided of a composition as a feed additive which comprises one or more endoglucanases, and 0&#x2013;20% by weight, based upon the content of cellulase proteins in the composition, of a cellobiohydrolase. The endoglycanases may be one or more of EGI, EGII, EGIII and any functionally active derivative of any thereof. Such endoglucanases may be obtained from a genetically modified strain of the fungus. Also provided is an enzyme-based feed additive which comprises EGI and/or EGII which lack the cellulose binding domain, and 0&#x2013;20% by weight, based upon the content of cellulase proteins in the additive, of a cellobiohydrolase. A further enzyme-based feed additive is provided which comprises a cereal-based carrier, one or more endoglucanases, and 0&#x2013;20% by weight, based upon the content of cellulase proteins in the additive, of a cellobiohydrolase. Such enzyme-based feed additives can be incorporated into a cereal-based feed which includes one or more of barley, wheat, triticale, rye and maize. The feed additive has the advantage of improving the feed conversion ratio and/or increasing the digestibility of a cereal-based feed in which it is included.

Improved methods of treating cellulose containing fabrics with cellulase comprising contacting the cellulose fabrics with truncated cellulase enzyme. Treatment of cellulose containing fabrics with cellulase core domains of the invention are disclosed as offering specific advantages of reduced redeposition of dye and increased abrasion.

Method and compositions for treating cellulose containing fabrics using truncated cellulase enzyme compositions

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San Francisco, CA, United States of America

Kathleen A Clarkson