Abstract: An object is to identify endoglucanase and ?-glucosidase genes by isolating genomic DNA containing cellulase genes, which are classified into endoglucanases or ?-glucosidases, from Acremonium cellulolyticus, and sequencing the nucleotide sequences thereof. The inventors intensively compared the amino acid sequences of known endoglucanases and ?-glucosidases with each other to find conserved region of amino acid sequences in Acremonium cellulolyticus, and various primers were designed based on the information. PCR was carried out using the various primers thus designed and genomic DNA or cDNA as a template. As a result, gene fragments of endoglucanases and ?-glucosidases were obtained. Primers were designed based on the gene fragments, and PCR was carried out to amplify nine genes of endoglucanases and ?-glucosidases. The nucleotide sequences thereof were sequenced, and the present invention was completed.

Abstract: An object is to identify endoglucanase and ?-glucosidase genes by isolating genomic DNA containing cellulase genes, which are classified into endoglucanases or ?-glucosidases, from Acremonium cellulolyticus, and sequencing the nucleotide sequences thereof. The inventors intensively compared the amino acid sequences of known endoglucanases and ?-glucosidases with each other to find conserved region of amino acid sequences in Acremonium cellulolyticus, and various primers were designed based on the information. PCR was carried out using the various primers thus designed and genomic DNA or cDNA as a template. As a result, gene fragments of endoglucanases and ?-glucosidases were obtained. Primers were designed based on the gene fragments, and PCR was carried out to amplify nine genes of endoglucanases and ?-glucosidases. The nucleotide sequences thereof were sequenced, and the present invention was completed.

Abstract: By combination of hydrophobic chromatography and strongly basic anion-exchange chromatography, a novel, highly hydrophobic ?-glucosidase was successfully identified from Acremonium cellulolyticus. Further, a gene corresponding to the identified ?-glucosidase was isolated. When multiple modifications were introduced into the base sequence of the gene, the gene was successfully expressed in Trichoderma viride at a high level, and the expression product successfully exhibited a high ?-glucosidase activity.

Abstract: An object is to identify endoglucanase and ?-glucosidase genes by isolating genomic DNA containing cellulase genes, which are classified into endoglucanases or ?-glucosidases, from Acremonium cellulolyticus, and sequencing the nucleotide sequences thereof. The inventors intensively compared the amino acid sequences of known endoglucanases and ?-glucosidases with each other to find conserved region of amino acid sequences in Acremonium cellulolyticus, and various primers were designed based on the information. PCR was carried out using the various primers thus designed and genomic DNA or cDNA as a template. As a result, gene fragments of endoglucanases and ?-glucosidases were obtained. Primers were designed based on the gene fragments, and PCR was carried out to amplify nine genes of endoglucanases and ?-glucosidases. The nucleotide sequences thereof were sequenced, and the present invention was completed.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: A modified polynucleotide has a different base sequence in at least one codon from a wild-type base sequence encoding a horseradish peroxidase polypeptide. The usage frequency of the modified codon of the polynucleotide corresponds to the codon usage frequencies of three filamentous fungal species in Humicola, Aspergillus, and Trichoderma. The polynucleotide is capable of expressing the polypeptide to be encoded in a filamentous fungus.

Abstract: 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.

Abstract: 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.

Abstract: A modified polynucleotide has a different base sequence in at least one codon from a wild-type base sequence encoding a horseradish peroxidase polypeptide. The usage frequency of the modified codon of the polynucleotide corresponds to the codon usage frequencies of three filamentous fungal species in Humicola, Aspergillus, and Trichoderma. The polynucleotide is capable of expressing the polypeptide to be encoded in a filamentous fungus.

Abstract: By combination of hydrophobic chromatography and strongly basic anion-exchange chromatography, a novel, highly hydrophobic ?-glucosidase was successfully identified from Acremonium cellulolyticus. Further, a gene corresponding to the identified ?-glucosidase was isolated. When multiple modifications were introduced into the base sequence of the gene, the gene was successfully expressed in Trichoderma viride at a high level, and the expression product successfully exhibited a high ?-glucosidase activity.

Abstract: By combination of hydrophobic chromatography and strongly basic anion-exchange chromatography, a novel, highly hydrophobic ?-glucosidase was successfully identified from Acremonium cellulolyticus. Further, a gene corresponding to the identified ?-glucosidase was isolated. When multiple modifications were introduced into the base sequence of the gene, the gene was successfully expressed in Trichoderma viride at a high level, and the expression product successfully exhibited a high ?-glucosidase activity.

Abstract: 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.

Abstract: An object is to identify endoglucanase and ?-glucosidase genes by isolating genomic DNA containing cellulase genes, which are classified into endoglucanases or ?-glucosidases, from Acremonium cellulolyticus, and sequencing the nucleotide sequences thereof. The inventors intensively compared the amino acid sequences of known endoglucanases and ?-glucosidases with each other to find conserved region of amino acid sequences in Acremonium cellulolyticus, and various primers were designed based on the information. PCR was carried out using the various primers thus designed and genomic DNA or cDNA as a template. As a result, gene fragments of endoglucanases and ?-glucosidases were obtained. Primers were designed based on the gene fragments, and PCR was carried out to amplify nine genes of endoglucanases and ?-glucosidases. The nucleotide sequences thereof were sequenced, and the present invention was completed.

Abstract: By combination of hydrophobic chromatography and strongly basic anion-exchange chromatography, a novel, highly hydrophobic ?-glucosidase was successfully identified from Acremonium cellulolyticus. Further, a gene corresponding to the identified ?-glucosidase was isolated. When multiple modifications were introduced into the base sequence of the gene, the gene was successfully expressed in Trichoderma viride at a high level, and the expression product successfully exhibited a high ?-glucosidase activity.

Abstract: This invention provides novel PF1270A substance, PF1270B substance and PF1270C substance represented by the following formula (1) or pharmaceutically acceptable salts thereof, a method for producing the same and a pharmaceutical composition which comprises at least one of the same as the active ingredient. Since a group of the PF1270 substances of the invention show high affinity for histamine H3 receptor, they are expected as novel histamine H3 receptor ligands useful as medicaments.

Abstract: This invention provides novel PF1270A substance, PF1270B substance and PF1270C substance represented by the following formula (1) or pharmaceutically acceptable salts thereof, a method for producing the same and a pharmaceutical composition which comprises at least one of the same as the active ingredient. Since a group of the PF1270 substances of the invention show high affinity for histamine H3 receptor, they are expected as novel histamine H3 receptor ligands useful as medicaments.