Abstract: The present invention relates to variants of a parent ?-amylase, which parent ?-amylase (i) has an amino acid sequence selected from the amino acid sequences shown in SEQ ID No. 1, SEQ ID No. 2, SEQ ID No. 3, and SEQ ID No.

Abstract: The invention relates to a variant of a parent Termamyl-like alpha-amylase, which variant has a-amylase activity and exhibits an alteration in at least one of the following properties relative to said parent a-amylase: substrate specificity, substrate binding, substrate cleavage pattern, thermal stability, pH/activity profile, pH/stability profile, stability towards oxidation, Ca2+ dependency and specific activity.

Abstract: The inventors realized that in some applications the control of the maltose-to-glucose ratio is of great importance. Particularly for ethanol production from granular starch by fermentation, it may be an advantage to form a larger amount of glucose which is more readily fermentable than maltose. Particularly for production of maltose syrups glucose is an undesired product, and hence it of interest to increase the maltose-to-glucose ratio. They then developed a method of constructing such variants of based on the three-dimensional structure of a parent maltogenic alpha-amylase.

Abstract: New subtilisin homologues (both nucleic acids and proteins) are provided. Compositions which include these new proteins, recombinant cells, shuffling methods involving the new homologues, antibodies to the new homologues, and methods of using the homologues are also provided.

Abstract: Novel subtilases having an improved wash performance on egg stains. These subtilases are useful exhibiting excellent or improved wash performance on egg stains when used in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dish wash compositions, including automatic dish wash compositions.

Abstract: The present invention relates to a method of constructing a variant of a parent Termamyl-like alpha-amylase, which variant has alpha-amylase activity and at least one altered property as compared to the parent alpha-amylase, comprising i) analyzing the structure of the parent Termamyl-like alpha-amylase to identify at least one amino acid residue or at least one structural part of the Termamyl-like alpha-amylase structure, which amino acid residue or structural part is believed to be of relevance for altering the property of the parent Termamyl-like alpha-amylase (as evaluated on the basis of structural or functional considerations), ii) constructing a Termamyl-like alpha-amylase variant, which as compared to the parent Termamyl-like alpha-amylase, has been modified in the amino acid residue or structural part identified in i) so as to alter the property, and iii) testing the resulting Termamyl-like alpha-amylase variant for the property in question.

Abstract: The present invention relates to a hybrid enzyme comprising at least one carbohydrate-binding module amino acid sequence and at least the catalytic module of a glucoamylase amino acid sequence. The invention also relates to the use of the hybrid enzyme in starch processing and especially ethanol production.

Abstract: The present invention relates to pectate lyase variants exhibiting alterations relative to a parent enzyme exhibiting pectate lyase activity as its major enzymatic activity; to a method of producing such enzymes; and to methods for using such enzymes in the textile, detergent and cellulose fiber processing industries. Compared to the parent enzyme, the pectate lyase variants of the present invention exhibit improved stability in detergents.

Abstract: Abstract of the Disclosure The present invention relates to variants of a parent ?-amylase, which parent ?-amylase (i) has an amino acid sequence selected from the amino acid sequences shown in SEQ ID No. 1, SEQ ID No. 2, SEQ ID No. 3, and SEQ ID No.

Abstract: The present invention relates to methods for preparing sweetners and alcohol using alpha-amylase variants.

Abstract: The present invention relates to a method of constructing a variant of a parent Termamyl-like ?-amylase, which variant has ?-amylase activity and at least one altered property as compared to the parent ?-amylase, comprises i) analysing the structure of the parent Termamyl-like ?-amylase to identify at least one amino acid residue or at least one structural part of the Termamyl-like ?-amylase structure, which amino acid residue or structural part is believed to be of relevance for altering the property of the parent Termamyl-like ?-amylase (as evaluated on the basis of structural or functional considerations), ii) constructing a Termamyl-like ?-amylase variant, which as compared to the parent Termamyl-like ?-amylase, has been modified in the amino acid residue or structural part identified in i) so as to alter the property, and, optionally, iii) testing the resulting Termamyl-like ?-amylase variant with respect to the property in question.

Abstract: The present invention relates to a hybrid enzyme comprising at least one carbohydrate-binding module amino acid sequence and at least the catalytic module of a glucoamylase amino acid sequence. The invention also relates to the use of the hybrid enzyme in starch processing and especially ethanol production.

Abstract: The invention relates to a variant of a parent Termamyl-like a-amylase, which variant has a-amylase activity and exhibits an alteration in at least one of the following properties relative to said parent a-amylase: substrate specificity, substrate binding, substrate cleavage pattern, thermal stability, pH/activity profile, pH/stability profile, stability towards oxidation, Ca2+ dependency and specific activity.

Abstract: The invention relates to a variant of a parent Termamyl-like ?-amylase, which exhibits an alteration in at least one of the following properties relative to said parent ?-amylase: i) improved pH stability at a pH from 8 to 10.5; and/or ii) improved Ca2+ stability at pH 8 to 10.5, and/or iii) increased specific activity at temperatures from 10 to 60° C.

Abstract: The present invention relates to variants of a parent ?-amylase, which parent ?-amylase (i) has an amino acid sequence selected from the amino acid sequences shown in SEQ ID No. 1, SEQ ID No. 2, SEQ ID No. 3, and SEQ ID No.

Abstract: The present invention relates to a method of constructing a variant of a parent Termamyl-like alpha-amylase, which variant has alpha-amylase activity and at least one altered property as compared to the parent alpha-amylase, comprising i) analyzing the structure of the parent Termamyl-like alpha-amylase to identify at least one amino acid residue or at least one structural part of the Termamyl-like alpha-amylase structure, which amino acid residue or structural part is believed to be of relevance for altering the property of the parent Termamyl-like alpha-amylase (as evaluated on the basis of structural or functional considerations), ii) constructing a Termamyl-like alpha-amylase variant, which as compared to the parent Termamyl-like alpha-amylase, has been modified in the amino acid residue or structural part identified in i) so as to alter the property, and iii) testing the resulting Termamyl-like alpha-amylase variant for the property in question.

Abstract: The present invention relates to a method of constructing a variant of a parent Termamyl-like .alpha.-amylase, which variant has .alpha.-amylase activity and at least one altered property as compared to the parent .alpha.-amylase, comprisesi) analyzing the structure of the parent Termamyl-like .alpha.-amylase to identify at least one amino acid residue or at least one structural part of the Termamyl-like .alpha.-amylase structure, which amino acid residue or structural part is believed to be of relevance for altering the property of the parent Termamyl-like .alpha.-amylase (as evaluated on the basis of structural or functional considerations),ii) constructing a Termamyl-like .alpha.-amylase variant, which as compared to the parent Termamyl-like .alpha.-amylase, has been modified in the amino acid residue or structural part identified in i) so as to alter the property, and, optionally,iii) testing the resulting Termamyl-like .alpha.-amylase variant with respect to the property in question.