Meiji Seika Pharma Co., Ltd.

Mitsui Chemicals, Inc.

Meui Seika Kaisha, Ltd.

Fumikazu Yokoyama

Kaoru Okakura

Atsushi Inoue

Masami Osabe

Hisaaki Yanai

Hiroki Tamai

Nobuko Mazuka

Kengo Yokoyama

Koji Yanai

Takashi Yaguchi

Akitaka Nakane

Koichiro Murashima

Goh Tsujiuchi

Nobuaki Kushida

Naoko Watanabe

Toshiaki Nagasato

Takako Okuda

An object is to identify endoglucanase and &#x3b2;-glucosidase genes by isolating genomic DNA containing cellulase genes, which are classified into endoglucanases or &#x3b2;-glucosidases, from, and sequencing the nucleotide sequences thereof. The inventors intensively compared the amino acid sequences of known endoglucanases and &#x3b2;-glucosidases with each other to find conserved region of amino acid sequences in, 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 &#x3b2;-glucosidases were obtained. Primers were designed based on the gene fragments, and PCR was carried out to amplify nine genes of endoglucanases and &#x3b2;-glucosidases. The nucleotide sequences thereof were sequenced, and the present invention was completed.

Cellulase gene

By combination of hydrophobic chromatography and strongly basic anion-exchange chromatography, a novel, highly hydrophobic &#x3b2;-glucosidase was successfully identified from. Further, a gene corresponding to the identified &#x3b2;-glucosidase was isolated. When multiple modifications were introduced into the base sequence of the gene, the gene was successfully expressed inat a high level, and the expression product successfully exhibited a high &#x3b2;-glucosidase activity.

Protein having B-glucosidase activity and uses thereof

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&#xb0; 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.

Mutant xylanase, manufacturing method and use therefor, and method for manufacturing saccharified lignocellulose

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, and. The polynucleotide is capable of expressing the polypeptide to be encoded in a filamentous fungus.

Method for producing horseradish peroxidase recombinant protein using filamentous fungus

Protein having &#x3b2;-glucosidase activity and uses thereof

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 Hreceptor, they are expected as novel histamine Hreceptor ligands useful as medicaments. 

Physiologically active substances PF1270A, B and C substances

Growing community of inventors

Yokohama, Japan

Fumikazu Yokoyama