Lipase enzymes and methods of using the lipases in a baking for improving the volume, stability, tolerance of a baked product and/or reducing and reducing or eliminating the use of DATEM.

The present invention relates to a baked product made without any addition of sugar, which still has a suitable sweetness intensity and a good taste. The baked product has a very low content of fructose. The baked product is obtained by a two-step enzymatic process involving a first step of providing sugar from starch, suitable for a fermentation process, followed by a second step of enzymatic hydrolysis of polysaccharides, oligosaccharides and disaccharides, notably to form primarily glucose and maltose. The novel process further allows for an optimized and/or shortened proofing of the dough in the first step.

A method for improving the freshness of flat breads comprising a) adding to flour or to a dough comprising a flour, a first maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, and F188L; and a second maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, F194Y, and N375S; and b) making flat breads from the dough.

Disclosed are compositions and methods relating to a simplified process for producing maltodextrin and specialty syrups using fewer enzymes and less complicated conditions than required for contemporary enzymatic processes.

Lipase enzymes, methods of making lipase enzymes, methods of using lipase enzymes in food, feed, personal care, detergents, grain processing, pulp and paper processing, biofuels, ethanol production, textiles, dairy processing, cocoa butter processing, cocoa extraction, dietary supplements, coffee processing, coatings, water treatment, and oil processing.

A method for removing a stain from a surface using lipase enzymes, and a formulation comprising a lipase enzyme.

The present disclosure concerns recombinant yeast host cells expressing cell-associated heterologous food and/or feed enzymes which are expressed during the propagation phase of the recombinant yeast hosts cells. The recombinant yeast host cells can be used in a subsequent production process to make food and/or feed products, for example, baked products.

Isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from Alicyclobacillus acidocaldarius are provided. Further provided are methods of at least partially degrading, cleaving, or removing polysaccharides, lignocellulose, cellulose, hemicellulose, lignin, starch, chitin, polyhydroxybutyrate, heteroxylans, glycosides, xylan-, glucan-, galactan-, or mannan-decorating groups using isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from Alicyclobacillus acidocaldarius.

A method for improving the freshness of flat breads comprising a) adding to flour or to a dough comprising a flour, a first maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, and F188L; and a second maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, F194Y, and N375S; and b) making flat breads from the dough.

The present invention relates to a variant polypeptide having maltogenic alpha-amylase activity wherein the polypeptide comprises an amino acid sequence, which, when aligned with an amino acid sequence of SEQ ID NO: 1, comprises an amino acid substitution F188L/I, S200N, and D261G, and optionally a further amino acid substitution T288P, wherein the amino acid substitutions are determined with reference to SEQ ID NO: 1, and wherein the polypeptide has an amino acid sequence which has at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or at least 99% identity to the amino acid sequence of SEQ ID NO: 1. The invention also relates to a process for the preparation of a dough or a baked product wherein the variant polypeptide is used.