Abstract: The present invention relates to isolated nucleic acid sequences encoding polypeptides having oxaloacetate hydrolase activity. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as recombinant methods for producing the polypeptides.

Abstract: The invention relates to a variant of a parent Fungamyl-like fungal alpha-amylase, which exhibits improved thermal stability at acidic pH suitable for, e.g., starch processes.

Abstract: Attaching a peptide extension to the C-terminal amino acid of a lipase re-duces the tendency to form odor. This may lead to lipase variants with a reduced odor generation when washing textile soiled with fat which includes relatively short-chain fatty acyl groups (e.g. up to C8) such as dairy stains containing butter fat or tropical oils such as coconut oil or palm kernel oil.

Abstract: The present invention relates to polypeptides having antimicrobial activity and polynucleotides having a nucleotide sequence which encodes for the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid constructs as well as methods for producing and using the polypeptides.

Abstract: The present invention relates to an enzyme exhibiting endo-beta-1,4-glucanase activity (EC 3.2.1.4), which is a) a polypeptide encoded by the DNA sequence of positions 1 to 2322 of SEQ ID NO: 1; b) a polypeptide produced by culturing a cell comprising the sequence of SEQ ID NO: 1 under conditions wherein the DNA sequence is expressed; c) an endo-beta-1,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO: 2; and fragments thereof exhibiting endo-beta-1,4-glucanase activity, and d) a polypeptide having endo-beta-1,4-glucanase activity that is encoded by a polynucleotide that hybridizes with the nucleotide sequence shown in positions 1–2322 of SEQ ID NO: 1, is useful for detergent and textile applications.

Abstract: The present invention relates to subtilases having a reduced tendency towards inhibition by substances present in eggs, such as the trypsin inhibitor type IV-0. 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 dishwash compositions, including automatic dishwash compositions.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved autoproteolytic stability in comparison to their wild type parent enzymes.

Abstract: An esterase isolated from Aspergillus oryzae is capable of stereoselective hydrolysis of chiral esters and also has arylesterase activity (EC 3.1.1.2) and feruloyl esterase activity (EC 3.1.1.73). The esterase has only a limited homology to known amino acid sequences.

Abstract: The present invention relates to coated particles comprising a coating and a core particle comprising an active, wherein the coating comprises a gas phase component. The invention also relates to processes for the manufacture of such coated particles comprising (a) providing a coating material comprising a gas phase component and applying the gas containing coating material to a core particle or (b) providing a coating material comprising a gas generating component, applying the coating material to a core particle and treating the coated particles so as to generate a gas from the gas generating component. Furthermore, it also relates to the use of such coated particles in a number of applications.

Abstract: The invention relates to a DNA sequences for regulating transcription of a structural gene encoding a polypeptide in a eukaryotic host cell comprising (a) a first DNA sequence to which RNA polymerase binds which DNA sequence comprises a mRNA initiation site; and further (b) one or more DNA sequence(s) to which RNA polymerase binds with or without a mRNA initiation site. The invention also relates to a DNA construct and an expression vector and a host cell comprising the DNA sequence of the invention.

Abstract: The properties of dough or bread can be improved by the addition of a carbohydrate oxidase which can oxidize the reducing end of an oligosaccharide more efficiently than the corresponding monosaccharide, e.g., preferentially oxidizing maltodextrins or cellodextrins over glucose. A novel carbohydrate oxidase having the capability to oxidize maltodextrins and cellodextrins more efficiently than glucose may be obtained from a strain of Microdochium, particularly M. nivale. The amino acid sequence of the novel carbohydrate oxidase has very low homology (<20% identity) with known amino acid sequences.

Abstract: The present invention relates to protease subtilase enzyme, characterized by an insertion in at least one active site loop. The enzymes exhibit improved wash performance in a detergent in comparison to its parent enzyme if it is a subtilase variant.

Abstract: The invention relates to a variant of a parent Fungamyl-like fungal alpha-amylase, which exhibits improved thermal stability at acidic pH suitable for, e.g., starch processes.

Abstract: The present invention relates to methods for modifying proteins by mapping one or more epitopes of the protein and altering the amino acid sequence of one or more epitopes of the protein in order to make the protein less immunogenic.

Abstract: Lipolytic enzymes are chemically modified by covalently linking one or more (particularly 1–3) hydrophobic groups to the enzyme molecule. The chemical modification improves the performance of the lipolytic enzyme, e.g., in baking or in detergents.

Abstract: Acid-stable proteases of the subtilisin family, their use in animal feed, feed-additives and feed compositions containing such proteases, and methods for the treatment of vegetable proteins using such proteases.

Abstract: The present invention relates to methods of producing a polypeptide comprising culturing a mutant of a parent cell, wherein the mutant produces less oxaloacetate hydrolase than the parent cell, wherein the oxaloacetate hydrolase (i) has an amino acid sequence that has at least 90% identity with amino acids 1-341 of SEQ ID NO: 2: (ii) is encoded by a nucleic acid sequence having at least 90% homology with a nucleotide sequence comprising nuclotides 1157-1411, 1504-1651 and 1764-2383 of SEQ ID NO: 1: (iii) is encoded by a nucleic acid sequence which hybridizes under high stringency conditions with the nucleic acid sequence of SEQ ID NO: 1, the cDNA sequence of SEQ ID NO: 1, the complementary strand of SEQ ID NO: 1, and/or the complementary strand of the cDNA sequence of SEQ ID NO: 1: and/or (iv) a subsequence of one or both of (i) and (ii), wherein the subsequence encodes a fragment that has oxaloacetate hydrolase activity.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved wash performance in any detergent in comparison to their wild type parent enzymes.

Abstract: The present invention relates to mutations of a subtilisin gene which result in changes in the chemical characteristics of subtilisin enzymes. Mutations at specific nucleic acids of the subtilisin gene result in amino acid substitutions and consequently, altered enzyme function. Some of these mutant enzymes exhibit physical properties advantageous to industrial applications, particularly in the detergent industry, providing subtilisin which is more stable to oxidation, possesses greater protease activity, and exhibits improved washability.

Abstract: In the method raw starch is treated with the amylase with the enzyme classification EC 3.21.133 below the gelatinization temperature, whereafter the maltose and the limit dextrin are recovered. The method is simple and cheap and gives rise to a maltose of high purity and to a cheap limit dextrin useable as a fat replacer in foods.