Abstract: The present invention relates to novel variant EGIII or EGIII-like cellulases which have improved stability. The variant cellulases have performance sensitive residues replaced to a residue having modified stability.

Abstract: The present invention relates to variant EGIII cellulases that have improved stability and/or performance. The variant cellulases have replacements at sensitive residues to improve stability and/or performance.

Abstract: The present invention relates to variant EGIII cellulases that have improved stability and/or performance. The variant cellulases have replacements at sensitive residues to improve stability and/or performance.

Abstract: The present invention relates to variant EGIII cellulases that have improved stability and/or performance. The variant cellulases have replacements at sensitive residues to improve stability and/or performance.

Abstract: The present invention relates to variant EGIII cellulases that have improved stability and/or performance. The variant cellulases have replacements at sensitive residues to improve stability and/or performance.

Abstract: 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.

Abstract: Modified enzymes are provided in which at least one amino acid, such as asparagine, leucine, methionine or serine, of an enzyme is replaced with a cysteine and the thiol hydrogen is replaced with a substituent group providing a thiol side chain selected from the group consisting of: a) —SR1R2, wherein R1 is an alkyl and R2 is a charged or polar moiety; b) —SR3, wherein R3 is a substituted or unsubstituted phenyl; c) —SR4, wherein R4 is substituted or unsubstituted cyclohexyl; d) —SR5, wherein R5 is C10-C15 alkyl; and e) —SR6 wherein R6 is a C1-6 alkyl. Also, methods of producing the modified enzymes are provided, as well as detergent and feed additives and a composition for the treatment of a textile. A method for using the modified enzymes in organic synthesis is additionally provided. Further, modified enzymes having improved activity, altered pH profile and/or wash performance are provided.

Abstract: The present invention relates to novel variant EGIII or EGIII-like cellulases which have improved stability. The variant cellulases have performance sensitive residues replaced to a residue having improved stability.

Abstract: Novel &agr;-amylase enzymes are disclosed having a substution equivalent to G475R in Bacillus licheniformis. The disclosed &agr;-amylase enzymes show improved specific activity and starch hydrolysis performance. Also provided are polynucleotides encoding such enzymes, expression vectors including such polynucleotides, host cells transformed with such expression vectors, and the use of such enzymes in detergent compositions.

Abstract: The present invention relates to variant EGIII cellulases which have improved stability and/or performance. The variant cellulases have replacements at sensitive residues to improve stability and/or performance.

Abstract: According to the invention a method is provided for liquefying starch comprising the steps of adding a sodium composition to the starch prior to or simultaneously with liquefying the starch; adding &agr;-amylase to the treated starch; and reacting the treated starch for a time and at a temperature effective to liquefy the treated starch. Preferred sodium compositions comprise sodium chloride, sodium bicarbonate, sodium benzoate, sodium sulfate, sodium bisulfite, sodium ascorbate, sodium acetate, sodium nitrate, sodium tartrate, sodium tetraborate, sodium propionate, sodium citrate, sodium succinate, monosodium glutamate, trisodium citrate, sodium phosphate or a mixture thereof.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: According to the invention a method is provided for liquefying starch comprising the steps of treating the starch prior to or simultaneously with liquefying the starch to inactivate and/or remove the enzyme inhibiting composition present in the starch and form treated starch; adding .alpha.-amylase to the treated starch; and reacting the treated starch for a time and at a temperature effective to liquefy the treated starch. Effective means to treat the starch include the addition of a phytate degrading enzyme and heat treatment, optionally followed by filtration or centrifugation, of granular starch or a starch solution.

Abstract: 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.

Abstract: According to the invention a method is provided for liquefying starch comprising the steps of adding a sodium composition to the starch prior to or simultaneously with liquefying the starch; adding .alpha.-amylase to the treated starch; and reacting the treated starch for a time and at a temperature effective to liquefy the treated starch. Preferred sodium compositions comprise sodium chloride, sodium bicarbonate, sodium benzoate, sodium sulfate, sodium bisulfite, sodium ascorbate, sodium acetate, sodium nitrate, sodium tartrate, sodium tetraborate, sodium propionate, sodium citrate, sodium succinate, monosodium glutamate, trisodium citrate, sodium phosphate or a mixture thereof.