Abstract: The present invention relates to a method for solubilizing arabinoxylan-containing material (particularly insoluble arabinoxylan-containing material), comprising admixing a xylan-containing material with a xylanase comprising a polypeptide sequence shown herein as SEQ ID No. 3, SEQ ID No. 2, SEQ ID No. 1, SEQ ID No. 9, SEQ ID No. 10, SEQ ID No. 11 or SEQ ID No. 15, or a variant, homolog, fragment or derivative thereof having at least 75% identity with SEQ ID No. 3 or SEQ ID No. 2 or SEQ ID No. 1 or SEQ ID No. 9 or SEQ ID No. 10 or SEQ ID No. 11 or SEQ ID No. 15; or a polypeptide sequence which comprises SEQ ID No. 3, SEQ ID No. 2, SEQ ID No. 1, SEQ ID No. 9, SEQ ID No. 10, SEQ ID No. 11 or SEQ ID No. 15 with a conservative substitution of at least one of the amino acids; or a xylanase which is encoded by a nucleotide sequence shown herein as SEQ ID No. 6, SEQ ID No. 5, SEQ ID No. 4, SEQ ID No. 12, SEQ ID No. 13, SEQ ID No. 14, SEQ ID No. 16, SEQ ID No. 17 or SEQ ID No.

Abstract: Enzymatic reactions are disclosed herein comprising water, glucose-1-phosphate, cellodextrin, and at least one cellodextrin phosphorylase enzyme comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:2 or SEQ ID NO:6. These reactions produce a low molecular weight, insoluble cellulose with enhanced features.

Abstract: Disclosed are methods and compositions using glycoside hydrolases, such as an alpha-L-fucosidases, to prevent and/or treat a pathogenic infection and/or diarrhea in an animal wherein the pathogenic infection is caused by a pathogen capable of binding to an animal intestinal cell wherein said binding of the pathogen is dependent on the presence of a pathogen binding site having at least one glycan structure substituted with at least one alpha-1,2-L-fucose moiety comprising administering to the animal an effective amount of a glycoside hydrolase capable of removing the at least one alpha-1,2-L-fucose moiety from the pathogen binding site.

Abstract: Reaction compositions are disclosed herein comprising at least water, alpha-glucose-1-phosphate (alpha-G1P), an acceptor molecule, and a beta-1,3-glucan phosphorylase enzyme. These reactions can synthesize oligosaccharides and polysaccharides with beta-1,3 glycosidic linkages. Further disclosed are methods of isolating beta-1,3-glucan.

Abstract: Reaction compositions are disclosed herein comprising at least water, beta-glucose-1-phosphate (beta-G1P), an acceptor molecule, and an alpha-1,3-glucan phosphorylase enzyme. These reactions can synthesize oligosaccharides and polysaccharides with alpha-1,3 glycosidic linkages. Further disclosed are alpha-1,3-glucan phosphorylase enzymes and methods of use thereof.

Abstract: Enzymatic reactions are disclosed herein comprising water, glucose-1-phosphate, cellodextrin, and at least one cellodextrin phosphorylase enzyme comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:2 or SEQ ID NO:6. These reactions produce a low molecular weight, insoluble cellulose with enhanced features.

Abstract: The present disclosure relates to polypeptides having alpha-glucosidase activity isolated, derived or derivable from Rasamsonia or engineered polypeptides having alpha-glucosidase activity isolated, derived or derivable from Rasamsonia homologs. The present disclosure also pertains to polynucleotides encoding the polypeptides, nucleic acid constructs, vectors, host cells and mutant cells comprising the polynucleotides. The disclosure further pertains to compositions comprising such polypeptides, methods of producing the polypeptides and compositions, as well as methods for using such polypeptides and compositions for industrial applications.

Abstract: Enzymatic reactions are disclosed herein comprising water, glucose-1-phosphate, cellodextrin, and at least one cellodextrin phosphorylase enzyme comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:2 or SEQ ID NO:6. These reactions produce a low molecular weight, insoluble cellulose with enhanced features.

Abstract: The present invention relates to a method of preparing a corn based product said method comprising contacting a plant composition comprising (consisting of or consisting essentially of) corn or a corn by-product or a combination thereof with a xylanase comprising: i) a polypeptide as set forth in SEQ ID No. 8 or SEQ ID No. 7 or SEQ ID No. 6; or ii) a variant, fragment homologue, fragment or derivative thereof having at least 85% identity with SEQ ID No. 8 or SEQ ID No. 7 or SEQ ID No. 6; or with a xylanase encoded by: a) a nucleotide sequence shown herein as SEQ ID No. 3. SEQ ID No. 2 or SEQ ID No. 1; or b) a nucleotide sequence which can hybridize to the complement of SEQ ID No. 3. SEQ ID No. 2 or SEQ ID No. 1 under high stringency conditions: or c) a nucleotide sequence which has at least 80% identity with SEQ ID No. 3. SEQ ID No. 2 or SEQ ID No. 1. The present invention further relates to the use of the enzyme to produce corn based feedstuffs.

Abstract: Described are methods and compositions relating to granular starch-converting glucoamylases and ?-amylases. The enzymes can be used to perform enzymatic starch hydrolysis of granular starch at or below the gelatinization temperature of insoluble granular starch.

Abstract: Described are methods and compositions relating to granular starch-converting glucoamylases and ?-amylases. The enzymes can be used to perform enzymatic starch hydrolysis of granular starch at or below the gelatinization temperature of insoluble granular starch.

Abstract: Described are methods and compositions relating to granular starch-converting glucoamylases and ?-amylases. The enzymes can be used to perform enzymatic starch hydrolysis of granular starch at or below the gelatinization temperature of insoluble granular starch.

Abstract: Compositions are disclosed herein comprising cellulose that has (i) a weight-average degree of polymerization (DPw) of about 10 to about 1000, (ii) a cellulose II crystal structure, and that is (iii) insoluble in an aqueous composition. Further disclosed are cellodextrin phosphorylase enzymes that synthesize this cellulose material. Methods of using cellulose for viscosity modification or film/coating applications are also disclosed.

Abstract: Enzymatic reactions are disclosed herein comprising water, glucose-1-phosphate, cellodextrin, and at least one cellodextrin phosphorylase enzyme comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:2 or SEQ ID NO:6. These reactions produce a low molecular weight, insoluble cellulose with enhanced features.

Abstract: Disclosed herein are proteins capable of forming glucans having alpha-1,2 linkages/branches, reactions and methods for producing such glucan, compositions comprising such glucan, and various applications thereof.

Abstract: The present invention relates to a method for solubilising arabinoxylan-containing material (particularly insoluble arabinoxylan-containing material), comprising admixing a xylan-containing material with a xylanase comprising a polypeptide sequence shown herein as SEQ ID No. 3, SEQ ID No. 2, SEQ ID No. 1, SEQ ID No. 9, SEQ ID No. 10, SEQ ID No. 11 or SEQ ID No. 15, or a variant, homologue, fragment or derivative thereof having at least 75% identity with SEQ ID No. 3 or SEQ ID No. 2 or SEQ ID No. 1 or SEQ ID No. 9 or SEQ ID No. 10 or SEQ ID No. 11 or SEQ ID No. 15; or a polypeptide sequence which comprises SEQ ID No. 3. SEQ ID No. 2, SEQ ID No. 1, SEQ ID No. 9, SEQ ID No. 10, SEQ ID No. 11 or SEQ ID No. 15 with a conservative substitution of at least one of the amino acids; or a xylanase which is encoded by a nucleotide sequence shown herein as SEQ ID No. 6, SEQ ID No. 5, SEQ ID No. 4, SEQ ID No. 12, SEQ ID No. 13, SEQ ID No. 14, SEQ ID No. 16, SEQ ID No. 17 or SEQ ID No.

Abstract: The present disclosure relates to polypeptides having alpha-glucosidase activity isolated, derived or derivable from Rasamsonia or engineered polypeptides having alpha-glucosidase activity isolated, derived or derivable from Rasamsonia homologs. The present disclosure also pertains to polynucleotides encoding the polypeptides, nucleic acid constructs, vectors, host cells and mutant cells comprising the polynucleotides. The disclosure further pertains to compositions comprising such polypeptides, methods of producing the polypeptides and compositions, as well as methods for using such polypeptides and compositions for industrial applications.

Abstract: Enzymatic reactions are disclosed herein comprising water, glucose-1-phosphate, cellodextrin, and at least one cellodextrin phosphorylase enzyme comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:2 or SEQ ID NO:6. These reactions produce a low molecular weight, insoluble cellulose with enhanced features.

Abstract: An enzymatically produced soluble ?-glucan fiber composition is provided suitable for use as a digestion resistant fiber in food and feed applications. The soluble ?-glucan fiber composition can be blended with one or more additional food ingredients to produce fiber-containing compositions. Methods for the production and use of compositions comprising the soluble ?-glucan fiber are also provided.

Abstract: A fungal alpha-amylase is provided from Aspergillus fumigatus (AfAmy1). AfAmy1 has an optimal pH of 3.5 and is operable at 30-75 degrees C., allowing the enzyme to be used in combination with a glucoamylase and a pullulanase in a saccharification reaction. This obviates the necessity of running a saccharification reaction as a batch process, where the pH and temperature must be readjusted for optimal use of the alpha-amylase or glucoamylase. AfAmy1 also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DP1+DP2) compared to the products of saccharification catalyzed by an alpha-amylase from Aspergillus kawachii. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.