The present disclosure discloses a maltooligosyl trehalose synthase mutant with improved thermal stability, and belongs to the technical fields of enzyme engineering and protein engineering. The residual enzyme activities of the MTSase mutants S361R, S444E, S361R/S444E, S361K/S444E, G415P/S361R/S444E and G415P consistent with the present disclosure after treatment at 60 C. for 10 min are respectively 70.3%, 50.1%, 83.5%, 65.9%, 100% and 80.7%, which are respectively 1.6, 1.1, 1.9, 1.5, 2.3 and 1.9 times of that of the wild type. The half-lives of the S361R/S444E and G415P/S361R/S444E at 60 C. are respectively 14.9 min and 90.8 min which are respectively 3.2 and 19.7 times of that of the wild type, indicating that the thermal stability of the MTSase mutant consistent with the present disclosure is significantly improved than that of the wild type.

The present invention relates to processes for producing fermentation products from starch-containing material, wherein an alpha-amylase and a thermostable hemicellulase is present and/or added during liquefaction. The invention also relates to compositions suitable for use in processes of the invention.

The present invention provides, inter alia, a method for combined preparation of saccharides, alcohols (biofuel) and biodiesel using a composition comprising interior hydrophobic or hydrophilic medium encapsulated by a layer comprising cellulose, cellulose derivative material, and/or starch surrounded by a hydrophilic or hydrophobic medium, respectively.

The present disclosure provides a method for continuously producing starch saccharification products by using high-concentration starch milk.

The present disclosure relates to a method for preparing myo-inositol using myo-inositol monophosphate synthase consisting of an amino acid sequence of SEQ ID NO: 1 and/or myo-inositol monophosphate phosphatase consisting of an amino acid sequence of SEQ ID NO: 3.

The present invention provides enzymes that have been optimized by implementation of Protein Repair One Stop Shop (PROSS), an algorithm that generates protein design(s) for enhanced stability without changing either enzymatic properties or enzyme active site conformation of the respective enzyme. The protein design(s) generated by PROSS introduce mutations to the amino acid sequence of a wild-type protein, resulting in a mutated amino acid sequence that encodes a variant of the wild-type enzyme, i.e., an enzyme variant, which has an enhanced stability, core packing, surface polarity and backbone rigidity, a higher functional expression, and/or a combination thereof, compared to the stability core packing, surface polarity and backbone rigidity, functional expression and/or a combination thereof, of the wild-type enzyme.

The present invention relates to pullulanase variants comprising substitutions of the parent pullulanase at one or more positions corresponding to positions 393, 143, 150, 243, 244, 345, 346, 368, 370, 373, 381, 382, 385, 387, 402, 429, 430, 431, 432, 456, 486, 492, 610, 624, 631, 632, 665 and 699 of the polypeptide of SEQ ID NO: 3. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present disclosure provides a method for continuously producing starch saccharification products by using high-concentration starch milk.

The present invention relates to processes for producing fermentation products from starch-containing material, wherein an alpha-amylase and a thermostable hemicellulase is present and/or added during liquefaction. The invention also relates to compositions suitable for use in processes of the invention.

The present invention relates to a method of making glucose syrup from liquefied starch, and to compositions useful therein.