Abstract: A fusant F001 able to digest polysaccharides is formed by protoplast fusion between Bacillus amyloliquefaciens and Bacillus coagulans. The fusant F001 is deposited at NITE Patent Microorganisms Depositary (NPMD) in Japan with a deposit number NITE BP-02873.

Abstract: A cellulose hydrolase and a gene thereof are obtained by screening a cDNA genomic library constructed with Orpinomyces sp. Y102. The gene is 1071 base pairs long and comprises an open reading frame (ORF) for producing the cellulose hydrolase comprising 357 amino acids by translation. A transformed cell and a carrier carrying the gene are introduced. The gene is transferred to E. coli by transformation, such that E. coli can acquire activity of decomposing CMC, beta-glucan, and xylan. The cellulose hydrolase is multifunctional and is capable of decomposing cellubiose and directly decomposing fiber into glucose.

Abstract: A cellulose hydrolase and a gene thereof are obtained by screening a cDNA genomic library constructed with Orpinomyces sp. Y102. The gene is 1071 base pairs long and comprises an open reading frame (ORF) for producing the cellulose hydrolase comprising 357 amino acids by translation. A transformed cell and a carrier carrying the gene are introduced. The gene is transferred to E. coli by transformation, such that E. coli can acquire activity of decomposing CMC, beta-glucan, and xylan. The cellulose hydrolase is multifunctional and is capable of decomposing cellubiose and directly decomposing fiber into glucose.

Abstract: An isolated xylanase gene with mutations includes a fifty-eighth amino acid or a thirty-eighth amino acid generated from transforming asparagine to aspartic acid so as to form the isolated xylanase gene. A site-specific mutagenesis method includes: mutating the forty-first amino acid or the thirty-eighth amino acid of the xylanase gene by transforming asparagine to aspartic acid so as to form the isolated xylanase gene.

Abstract: A xylanase gene, denoted xynR8, encoding a xylanase (XynR8) obtained from the unisolated rumen microorganisms is provided. The DNA sequence of the xynR8 gene, xylanase, is also provided, the enzyme is thermostable, and highly specific for xylans with high activity. Transformation of microbial hosts with the xynR8 gene is described. A method for degrading the xylan-containing structure comprises hydrolyzing the ?-1,4-glycosidic bonds of xylans by contacting xylanase is provided, and a composition employing the above-mentioned hydrolyzing method is further addressed.

Abstract: A mutated xylanase gene with a broad pH range of reaction includes a forty-first amino acid or a twenty-first amino acid generated from transforming asparagine to aspartic acid so as to form the mutated xylanase gene. A site-specific mutagenesis method includes the step of: mutating the forty-first amino acid or the twenty-first amino acid of the xylanase gene by transforming asparagine to aspartic acid so as to form the mutated xylanase gene.

Abstract: A mutated xylanase gene with high reaction activity includes a fifty-eighth amino acid or a thirty-eighth amino acid generated from transforming asparagine to aspartic acid so as to form the mutated xylanase gene. A site-specific mutagenesis method includes the step of: mutating the forty-first amino acid or the thirty-eighth amino acid of the xylanase gene by transforming asparagine to aspartic acid so as to form the mutated xylanase gene.

Abstract: A mutated xylanase gene with a broad pH range of reaction includes a forty-first amino acid or a twenty-first amino acid generated from transforming asparagine to aspartic acid so as to form the mutated xylanase gene. A site-specific mutagenesis method includes the step of: mutating the forty-first amino acid or the twenty-first amino acid of the xylanase gene by transforming asparagine to aspartic acid so as to form the mutated xylanase gene.

Abstract: A xylanase gene, denoted xynR8, encoding a novel xylanase (XynR8) obtained from the unisolated rumen microorganisms is provided. The DNA sequence of the xynR8 gene, xylanase, is also provided, the enzyme is thermo-tolerable, and highly specific for xylans with high activity. Transformation of microbial hosts with the xynR8 gene is described. A method for degrading the xylan-containing structure comprises hydrolyzing the ?-1,4-glycosidic bonds of xylans by contacting xylanase is provided, and a composition employing the above-mentioned hydrolyzing method is further addressed.