What is aimed at is provision of an inexpensive and efficient saccharification method for lignocellulose using a thermostable xylanase and provision of a mutant xylanase that has a substitute amino acid residue, and that exhibits stable activity even under severe conditions in which enzymes easily inactivate, and that provides an initial rate of reaction not significantly reduced as compared to a wild-type xylanase corresponding to the mutant xylanase. Provided is a method of producing a saccharified product of lignocellulose, including contacting a lignocellulosic raw material with a thermostable xylanase, and a mutant xylanase that provides an initial rate of reaction that is at least 70% of that provided by a wild-type xylanase corresponding thereto, that has a xylanase activity after heat treatment at 50 C. for 24 hours that is at least 50% of its xylanase activity before the heat treatment, and that has a substitute amino acid residue.

Provided are isolated polypeptides having beta-xylosidase activity and polynucleotides encoding the polypeptides. Also provided are nucleic acid constructs, vectors and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.

Described herein is a process for producing saccharides and ethanol from biomass feedstock that includes (a) producing an enzyme composition by culturing a fungal strain(s) in the presence of a lignocellulosic medium, (b) using the enzyme composition to saccharify the biomass feedstock, and (c) fermenting the saccharified biomass feedstock to produce ethanol. The process is scalable and, in certain aspects, is capable of being deployed on farms, thereby allowing local production of saccharides and ethanol and resulting in a reduction of energy and other costs for farm operators. Optional steps to improve the biomass-to-fuel conversion efficiency are also contemplated, as are uses for byproducts of the process described herein.

The present invention relates to xylanase variants, comprising an alteration at least at one position corresponding to position 87 of the polypeptide of SEQ ID NO: 3, wherein the variant has xylanase activity and has increased xylanase inhibitor tolerance compared to the xylanase of SEQ ID NO: 3; and i) wherein the variant has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100% sequence identity to the polypeptide of SEQ ID NO: 3; or ii) wherein the number of alterations is 1-20, e.g., 1-10 such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 alterations. 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.

A thermostable -xylosidase including a -xylosidase catalytic domain, the -xylosidase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl--D-xylopyranoside as a substrate at least under conditions of a temperature of 85 C. and a pH of 6.0; or (C) a polypeptide including an amino acid sequence having at least 80% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl--D-xylopyranoside as a substrate at least under conditions of a temperature of 85 C. and a pH of 6.0.

A hyperthermostable endoglucanase including an endoglucanase catalytic domain, the endoglucanase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11, and having hydrolytic activity using carboxymethyl cellulose as a substrate at least under conditions of a temperature of 110 C. and a pH of 4.0; or (C) a polypeptide including an amino acid sequence having at least 70% sequence identity with the amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11, and having hydrolytic activity using carboxymethyl cellulose as a substrate at least under conditions of a temperature of 110 C. and a pH of 4.0.

The invention relates to temperature-stable polypeptides with -pyranosidase activity. The polypeptide substrates include -glucopyranosides and -xylopyranosides. The polypeptides can be expressed alone or as fusion proteins for example in yeast or bacteria and subsequently purified. The polypeptides according to the invention can be used alone or in a mixture with other enzymes for the degradation of plant raw materials, among others for the enzymatic degradation of biomass containing lignocellulose, in particular hemicellulose and the hemicellulose component xylan. The enzymes are suitable for use in textile processing, as an additive of detergents, or in the food or feed industry.

The present invention relates to enzyme compositions for high temperature saccharification of cellulosic material and to uses thereof.

The present invention relates to an improved process of treating crop kernels to provide a starch product of high quality suitable for conversion of starch into mono- and oligosaccharides, ethanol, sweeteners, etc. The present invention also relates to polypeptides having GH10 xylanase activity and polypeptides having GH62 arabinofuranosidase activity. Further, the present invention also relates to a process for extraction or separation of crude palm oil.

The present disclosure relates to a modified polypeptide having xylanase activity and use thereof.