The present invention discloses a polypeptide having beta-glucosidase activity. The activity is retained also in high glucose concentration. The invention also discloses an isolated polynucleotide, a nucleic acid construct and a recombinant host usable in production of said polypeptide, and a method for producing the polypeptide. Further the invention discloses compositions including the polypeptide and method of using the polypeptide in hydrolysis or synthesis.

The present invention relates to GH61 polypeptide variants. 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 invention relates to a process for the preparation of a sugar and/or fermentation product from lignocellulosic material.

Fungi that are genetically inactivated for the mstC gene (or a homolog thereof) are provided, which can also be genetically modified to increase production of heterologous proteins from a glucoamylase promoter. Methods of using these fungi, for example to degrade a biomass, are also provided.

A range of Cel7 putative cellobiohydrolase genes were identified using genome mining and homologous sequence alignment to Cel7A from Trichoderma reesei. A representative subset of these genes from across a broad diversity of evolutionarily disparate sources were cloned and expressed in T. reesei using a constitutive promotor and a common secretion signal. The purified recombinant enzymes were tested for efficacy on various substrates. The top performers were subjected to structural studies and subsites likely to confer enhanced performance were predicted using homology modeling and comparisons of natural sequence diversity. Once identified, the subsites were genetically introduced individually and combinatorically into the best in class Cel7A backbone we have found to date and then expressed in T. reesei and tested. A triple mutant was determined to have the highest cellulase activity we have measured in a cellobiohydrolase to date.

The present invention relates to recombinant filamentous fungal host cells producing cellulolytic enzyme compositions and methods of producing and using the compositions.

Provision of a mutant β-glucosidase having high protease resistance. A mutant β-glucosidase consists of an amino acid sequence having at least 90% sequence identity to SEQ ID NO: 1, wherein the amino acid sequence comprises Gln and Thr respectively at positions corresponding to positions 649 and 655 of SEQ ID NO: 1 or Tyr-Glu-Pro-Ala-Ser-Gly in a region corresponding to the region from position 653 to position 658 of SEQ ID NO: 1, and has β-glucosidase activity.

The present invention relates to enzyme compositions and processes of producing and using the compositions for the saccharification of lignocellulosic material.

The present invention provides for heterologous expression of beta-glucosidase (BGL) polypeptides encoded by Humicola grisea, Candida wickerhamii, Aspergillus aculeatus, Aspergillus oryzae, Penicillium decumbens, Chaetomium globosum, Neocallimastix frontalis, Debaryomyces hansenii, Kluyveromyces marxianus, or Phytophthora infestans in host cells, such as the yeast Saccharomyces cerevisiae. The expression in such host cells of the corresponding genes, and variants and combinations thereof, result in improved specific activity of the expressed BGL. Thus, such genes and expression systems are useful for efficient and cost-effective consolidated bioprocessing systems.

The object of the present invention is to separate and provide a β-glucosidase gene having the effect of efficiently promoting saccharification in hydrolysis of cellulose-containing biomass from a hardly culturable symbiotic protist community of Coptotermes formosanus, and the present invention specifically relates to β-glucosidase derived from a protist of the genus Pseudotrichonympha consisting of the amino acid sequence represented by SEQ ID NO: 1.