Genencor International, Inc.

Danisco US Inc.

Other

Carol A Requadt

Scott Douglas Power

Colin Mitchinson

Christopher Charles Barnett

Leif P Solheim

Andrew Shaw

Michael Jay Pepsin

Sandra W Ramer

William Albert Cuevas

Sang-Kyu Lee

Louise Wallace

Amr R Toppozada

Traci H Ropp

Regina Chin

David Aaron Estell

Anthony G Day

Luis Gustavo Cascao-Pereira

David E Estell

Christopher Ringer

William A Cuevas

Alpha-amylases from(AmyE), variants thereof, nucleic acids encoding the same, and host cells comprising the nucleic acids are provided. Methods of using AmyE or variants thereof are disclosed, including liquefaction and/or saccharification of starch. Such methods may yield sugars useful for ethanol production or high fructose corn syrup production. In some cases, the amylases can be used at low pH, in the absence of calcium, and/or in the absence of a glucoamylase.

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An &#x3b1;-amylase from(AmyE) produces significant amounts of glucose from various carbohydrate substrates, including vegetable starch, maltoheptaose, and maltotriose. Among other things, this advantageous property allows AmyE or variants thereof to be used in a saccharification reaction having a reduced or eliminated requirement for glucoamylase. The reduction or elimination of the glucoamylase requirement significantly improves the efficiency of the production of ethanol or high fructose corn syrup, for example.

Novel alpha-amylase mutants derived from the DNA sequences of naturally occurring or recombinant alpha-amylases are disclosed. The mutant alpha-amylases, in general, are obtained by in vitro modifications of a precursor DNA sequence encoding the naturally occurring or recombinant alpha-amylase to generate the substitution (replacement) or deletion of one or more oxidizable amino acid residues in the amino acid sequence of a precursor alpha-amylase. Such mutant alpha-amylases have altered oxidative stability and/or altered pH performance profiles and/or altered thermal stability as compared to the precursor. Also disclosed are detergent and starch liquefaction compositions comprising the mutant amylases, as well as methods of using the mutant amylases.

Oxidatively stable alpha-amylase

Mutant .alpha.-amylase

Oxidativley stable alpha-amylase

Novel .alpha.-amylase enzymes are disclosed in which one or more asparagine residues are substituted with a different amino acid or deleted. The disclosed .alpha.-amylase enzymes show altered or improved low pH starch hydrolysis performance, stability and activity profiles.

Mutant A-amylase

Growing community of inventors

Paradise, CA, United States of America

Carol A Requadt