Abstract: The invention relates to nucleases with improved properties such as enzymatic activity at high temperature, at low temperature, and/or high salt concentration. The invention also relates to methods for hydrolyzing polynucleotide substrates using the nucleases at high temperatures, at low temperature, or at high salt concentration. The invention further relates to uses of the nucleases for hydrolyzing polynucleotides in the manufacture of biopharmaceuticals, pharmaceutical compositions, vaccines, or viral vectors. Furthermore, the invention relates to kits comprising the nucleases.

Abstract: The invention relates to nucleases with improved properties such as enzymatic activity at high temperature, at low temperature, and/or high salt concentration. The invention also relates to methods for hydrolyzing polynucleotide substrates using the nucleases at high temperatures, at low temperature, or at high salt concentration. The invention further relates to uses of the nucleases for hydrolyzing polynucleotides in the manufacture of biopharmaceuticals, pharmaceutical compositions, vaccines, or viral vectors. Furthermore, the invention relates to kits comprising the nucleases.

Abstract: The invention relates to glucose isomerase enzymes (glucose isomerases) with improved enzymatic activity at low pH values and tolerance of calcium ions in the enzymatic reactions.

Abstract: The present invention is related to a trehalose phosphorylase comprising an amino acid sequence, wherein the amino acid sequence of the trehalose phosphorylase is at least 80% identical to and/or at least 80% homologous to an amino acid sequence of SEQ ID NO: 1, wherein the amino acid sequence of the trehalose phosphorylase comprises an amino acid substitution at one or more amino acid positions, wherein the one or more amino acid positions is/are selected from the group consisting of amino acid positions of SEQ ID NO: 1712, 383, 10, 114, 118, 192, 197, 220, 225, 304, 306, 318, 323, 339, 349, 357, 459, 476, 481, 484, 487, 488, 506, 511, 526, 530, 532, 533, 537, 550, 556, 564, 590, 649, 667, 703 and 705.

Abstract: The invention relates to a process for the preparation of a glycosylated organic compound by in vitro glycosylation of an organic compound having a nucleophilic group with a saccharide under catalysis of a Leloir glycosyltrans-ferase system comprising at least a first glycosyl transferase and a second glycosyl transferase. The invention further relates to a composition comprising a glycosylated organic compound that is obtainable by the process according to the invention.

Abstract: The present invention relates to polypeptide, preferably to a glucose isomerase, comprising an amino acid sequence, wherein the amino acid sequence of the polypeptide, preferably the glucose isomerase, is at least 95% identical to an amino acid sequence of SEQ ID NO:1, wherein the amino acid sequence of the polypeptide, preferably the glucose isomerase, comprises an amino acid substitution at one or more amino acid positions, wherein the one or more amino acid positions is/are each and independently selected from the group consisting of SEQ ID NO: 1 amino acid positions 89, 90, 95, 0, 33, 34, 35, and 59. The present invention further relates to methods preparing glucose including the use of the polypeptides of the invention for preparing glucose.

Abstract: The present invention relates to a method for producing trehalose, comprising the steps of mixing and reacting, in any order, (i) at least one alpha-phosphorylase capable of catalyzing the production of alpha-D-glucose 1-phosphate intermediate from a saccharide raw material, and from at least one phosphorus source; (ii) at least one trehalose phosphorylase capable of catalyzing the production of trehalose from an alpha-D-glucose 1-phosphate intermediate and a glucose substrate, wherein the trehalose phosphorylase is a trehalose phosphorylase variant with an amino acid sequence which differs from the amino acid sequence of a wild type trehalose phosphorylase in at least one amino acid position, (iii) at least one saccharide raw material which produces an alpha-D-glucose 1-phosphate intermediate and a co-product by catalytic action of the alpha-phosphorylase; and (iv) at least one phosphorus source selected from the group consisting of a phosphoric acids and an inorganic salt thereof.

Abstract: Disclosed are ketoreductases and the use thereof. The disclosed ketoreductases are particularly useful for enzymatically catalyzing the reduction of ketones to chiral or non-chiral secondary alcohols and oxidation of chiral or non-chiral secondary alcohols to ketones.

Abstract: The invention relates to a process for the manufacturing and purification of recombinant enzyme products, in particular of food enzyme products and the use thereof. The invention particularly relates to a process for the processing of enzyme products from a microbial fermentation broth by methods of separation, enzymatic treatment and filtration procedures.

Abstract: The present invention is related to a trehalose phosphorylase comprising an amino acid sequence, wherein the amino acid sequence of the trehalose phosphorylase is at least 80% identical to and/or at least 80% homologous to an amino acid sequence of SEQ ID NO: 1, wherein the amino acid sequence of the trehalose phosphorylase comprises an amino acid substitution at one or more amino acid positions, wherein the one or more amino acid positions is/are selected from the group consisting of amino acid positions of SEQ ID NO: 1 712, 383, 10, 114, 118, 192, 197, 220, 225, 304, 306, 318, 323, 339, 349, 357, 459, 476, 481, 484, 487, 488, 506, 511, 526, 530, 532, 533, 537, 550, 556, 564, 590, 649, 667, 703 and 705.

Abstract: The present invention relates to polypeptide, preferably to a glucose isomerase, comprising an amino acid sequence, wherein the amino acid sequence of the polypeptide, preferably the glucose isomerase, is at least 95% identical to an amino acid sequence of SEQ ID NO:1, wherein the amino acid sequence of the polypeptide, preferably the glucose isomerase, comprises an amino acid substitution at one or more amino acid positions, wherein the one or more amino acid positions is/are each and independently selected from the group consisting of SEQ ID NO: 1 amino acid positions 89, 90, 95, 0, 33, 34, 35, and 59. The present invention further relates to methods preparing glucose including the use of the polypeptides of the invention for preparing glucose.

Abstract: The present invention relates to a sucrose phosphorylase variant comprising or consisting of an amino acid sequence with at least 75% homologous and/or identical to an amino acid sequence of wild type sucrose phosphorylase, preferably wherein the sucrose phosphorylase is characterized by different structural and functional features. The invention also relates to method for preparing aG1P and a co-product, wherein the method comprises reacting a sucrose phosphorylase with a glucoside substrate, wherein the sucrose phosphorylase is a sucrose phosphorylase as defined in the context of the present invention.

Abstract: The invention relates to the enzymatic treatment of a virgin liquid nutrient naturally containing carbohydrates for the in-situ production of functional carbohydrates, thereby obtaining a fortified processed liquid nutrient, being rich (or enriched) in such functional carbohydrates and offering a beneficial nutritional value. The invention relates to the in-situ use of enzymes during food processing of a virgin liquid nutrient for the preparation of fortified food containing supplementary functional carbohydrates of specified composition.

Abstract: The invention relates to transaminases and their use. The ATAs according to the invention are particularly useful for catalyzing the conversion of amines to ketones and/or vice versa. Preferably, the transaminase (ATA) according to the invention comprises an amino acid sequence with at least 80% homology to SEQ ID NO:1, wherein the amino acid sequence is engineered compared to SEQ ID NO:1 such that it comprises at least a substitution selected from the group consisting of F255L, F255A, F255C, F255D, F255E, F255G, F255H, F255K, F255M, F255N, F255P, F255Q, F255R, F255S, F255T, F255V, F255W, and F255Y.

Abstract: The invention relates to ketoreductases and the use thereof. The ketoreductases of the invention are particularly useful for enzymatically catalyzing the reduction of ketones to chiral secondary alcohols.

Abstract: The invention relates to transaminases that are particularly useful for catalyzing the conversion of amine substrates to ketone products and/or vice versa.

Abstract: The invention relates to transaminases and their use. The ATAs according to the invention are particularly useful for catalyzing the conversion of amines to ketones and/or vice versa. Preferably, the transaminase (ATA) according to the invention comprises an amino acid sequence with at least 80% homology to SEQ ID NO:1, wherein the amino acid sequence is engineered compared to SEQ ID NO:1 such that it comprises at least a substitution selected from the group consisting of F255L, F255A, F255C, F255D, F255E, F255G, F255H, F255K, F255M, F255N, F255P, F255Q, F255R, F255S, F255T, F255V, F255W, and F255Y.

Abstract: The invention relates to ketoreductases and the use thereof. The ketoreductases of the invention are particularly useful for enzymatically catalyzing the reduction of ketones to chiral secondary alcohols.

Abstract: An expression vector including two separately inducible converging promoters P1 and P2, and expression system including such an expression vector and an additional regulator vector, a method of protein expression using such an expression system, and a method of investigating (meta)genome libraries using such an expression system.

Abstract: The invention relates to transaminases that are particularly useful for catalyzing the conversion of amine substrates to ketone products and/or vice versa.