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 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 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 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: The present invention relates to polypeptide variants of porcine trypsin, to nucleic acid molecules encoding these variants, and to host cells comprising such nucleic acid molecules. It also relates to the use of these variants in methods for producing insulin. The invention further relates to the use of these variants as medicaments, as food ingredients, or as feed ingredients and to the use of these variants within a process of manufacturing a food ingredient or a feed ingredient.

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 a saccharose phosphorylase that catalyzes the synthesis of glucose-1-phosphate and fructose from saccharose and phosphate, among other things. The saccharose phosphorylase according to the invention can be considered to be a mutation of the saccharose phosphorylase from Bifidobacterium adolescentis. In comparison to wild-type saccharose phosphorylase, the saccharose phosphorylase according to the invention is distinguished by improved activity, process stability, temperature stability, and lower product inhibition and is therefore particularly suitable for use in industrial processes.

Abstract: In order to at least approximately determine statistical properties of raw measured values, e.g., measurement noise and/or average errors, without knowledge of a filter applied to raw measured values and only with the aid of a useful signal obtained from the filtering, i.e., in order to make statements regarding measurement conditions by assuming a few frequently encountered boundary conditions, statistical properties of raw measured values are determined from the useful signal, which is composed of a temporal sequence of filter output values.

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 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: 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: Methods of preparing highly purified steviol glycosides, particularly rebaudiosides M, D, E and I are described. The methods include utilizing enzyme preparations and recombinant microorganisms for converting various staring compositions to target steviol glycosides. The highly purified rebaudiosides are useful as non-caloric sweetener in edible and chewable compositions such as any beverages, confectioneries, bakery products, cookies, and chewing gums.

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 invention relates to a cellobiose phosphorylase, which catalyzes, among other things, the synthesis of cellobiose from glucose 1-phosphate and glucose. The cellobiose phosphorylase according to the invention can be understood as a mutation of the cellobiose phosphorylase from Cellulomonas uda. In comparison to cellobiose phosphorylase of the wild type, the cellobiose phosphorylase according to the invention is distinguished by improved activity and process stability, in particular temperature stability, and lower product inhibition and therefore is especially suitable for use in industrial processes.

Abstract: The invention provides engineered enzymes of transsialidase and/or sialyl transferase activity that have increased regioselectivity and/or increased thermostability.

Abstract: Mutated fucosidases are provided demonstrating improved properties in terms of thermal stability and transfucosidase synthetic performance compared with a wild type transfucosidase isolated from Bifidobacterium longum subsp. infantis.

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.