An enzymatically produced soluble α-glucan fiber composition is provided suitable for use as a digestion resistant fiber in food and feed applications. The soluble α-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 α-glucan fiber are also provided.

An enzymatically produced soluble α-glucan fiber composition is provided suitable for use as a digestion resistant fiber in food and feed applications. The soluble α-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 α-glucan fiber are also provided.

A fungal alpha-amylase is provided from Aspergillus fumigatus (AfAmyl). AfAmyl 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 an isoamylase 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. AfAmyl also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DPI+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.

The present application relates to a psicose-6-phosphate phosphatase comprising motif A and motif B, a composition for producing D-psicose comprising the enzyme, and a method for producing D-psicose using the enzyme.

An enzymatically produced soluble α-glucan fiber composition is provided suitable for use as a digestion resistant fiber in food and feed applications. The soluble α-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 α-glucan fiber are also provided.

This disclosure provides isolated nucleic acid molecules comprising nucleic acid sequences encoding microbial polypeptides that are codon optimized for expression in mammalian cells, vectors comprising an immunotolerant dual promoter system, and methods using these polynucleotides and polypeptides to treat glycogen storage diseases and other inherited diseases.

Provided herein, in some embodiments, are cell-free systems, methods, kits, and compositions (e.g., cells and cell lysates) for converting a polysaccharide to allulose via the use of enzymes, such as thermostable enzymes.

Provided are a novel isoamylase improved in optimum temperature, and more specifically, improved in heat resistance, and a process for producing the isoamylase. An isoamylase having at least one amino acid mutation selected from the group consisting of D268A, M277I, A549P, A554P and A580T in an isoamylase consisting of an amino acid sequence represented by SEQ ID No: 1 or an isoamylase consisting of the amino acid sequence represented by SEQ ID No: 1 and having deletion, substitution or insertion of one to several amino acid residues.

The present disclosure relates to tagatose-6-phosphate phosphatase consisting of an amino acid sequence of SEQ ID NO: 1, a nucleic acid encoding the tagatose-6-phosphate phosphatase, and a transformant comprising the nucleic acid. Additionally, the present disclosure relates to a composition for producing tagatose, which comprises the tagatose-6-phosphate phosphatase of the present disclosure, and a method for producing tagatose using the tagatose-6-phosphate phosphatase of the present disclosure.

Provided are a novel isoamylase improved in optimum temperature, and more specifically, improved in heat resistance, and a process for producing the isoamylase.

An isoamylase having at least one amino acid mutation selected from the group consisting of D268A, M277I, A549P, A554P and A580T in an isoamylase consisting of an amino acid sequence represented by SEQ ID No: 1 or an isoamylase consisting of the amino acid sequence represented by SEQ ID No: 1 and having deletion, substitution or insertion of one to several amino acid residues.