Meiji Seika Pharma Co., Ltd.

Meiji Seika Kaisha, Ltd.

Mitsui Chemicals, Inc.

National Institute of Advanced Industrial Science and Technology

Kaoru Okakura

Koji Yanai

Fumikazu Yokoyama

Koichiro Murashima

Atsushi Inoue

Masami Osabe

Hiroki Tamai

Hisaaki Yanai

Takeshi Murakami

Manabu Watanabe

Naoki Midoh

Takayoshi Fukushima

Fusuke Mazuka

Koichi Miyamoto

Koji Nishizawa

Akitaka Nakane

Takashi Yamanobe

Chuhei Nojiri

Horst Kleinkauf

Shohei Yasuda

Sato Aihara

Toshiaki Nagasato

Tetsuya Yasutake

Takafumi Futamura

Tomoyuki Fukasawa

Nobuo Matsuhashi

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

An object is to efficiently produce thermostable catalase at low cost by expressing it as a recombinant protein in large quantity. A recombinant microorganism capable of efficiently expressing thermostable catalase can be provided by obtaining a DNA necessary for efficiently producing it as a recombinant protein, and the thermostable catalase can be efficiently produced at low cost by cultivating the obtained recombinant microorganism. Hydrogen peroxide can be efficiently decomposed at low cost, even at high temperature, by treating a solution containing hydrogen peroxide with the thermostable catalase of the present invention.

Thermostable catalase

By having a cellulase preparation comprising at least a certain amount of endoglucanases derived from two different types of microorganisms, the cellulase preparation can be provided with a higher activity and a wider pH property than those of cellulase preparations each containing one of the endoglucanases alone. Moreover, by introducing and expressing simultaneously two different types of cellulase genes in a single host cell, a cellulase preparation having a high activity and a wide pH property can be produced easily.

Cellulase preparation comprising endoglucanases derived from two different types of microorganisms

Disclosed is a novel cellulose having an amino acid sequence in which the 162nd and/or 166th amino acid residues in the amino acid sequence of cellulose NCE5 are substituted. Further, a polynucleotide encoding the novel cellulose, an expression vector containing the polynucleotide, a host cell transformed with the expression vector, and a cellulose preparation and a washing composition containing the cellulose are disclosed. The cellulose of the present invention is resistant to surfactants, and maintains a high activity even under alkaline conditions.

Cellulase resistant to surfactants

Disclosed is a novel cellulase having an amino acid sequence in which the 162nd and/or 166th amino acid residues in the amino acid sequence of cellulase NCE5 are substituted. Further, a polynucleotide encoding the novel cellulase, an expression vector containing the polynucleotide, a host cell transformed with the expression vector, and a cellulase preparation and a washing composition containing the cellulase are disclosed. The cellulase of the present invention is resistant to surfactants, and maintains a high activity even under alkaline conditions.

Cellulase tolerant to surfactants

The present invention provides an enzyme that synthesizes a cyclic depsipeptide, particularly the substance 1022, and a gene thereof. A cyclic depsipeptide synthetase according to the present invention comprises (a) an amino acid sequence of SEQ ID NO: 2 or (b) a modified amino acid sequence of the amino acid sequence of SEQ ID NO: 2 that have one or more modifications selected from a substitution, a deletion, an addition and an insertion and has cyclic depsipeptide synthetase activity. A cyclic depsipeptide synthetase gene according to the present invention comprises a nucleotide sequence encoding a cyclic depsipeptide synthetase. The present invention also provides a recombinant vector and a transformant for expressing the cyclic depsipeptide synthetase, and a mass production system for the cyclic depsipeptide. The present invention further provides a method for producing the cyclic depsipeptide synthetase.

Cyclic depsipeptide synthetase and method for recombinant production

The invention is to provide a novel &#x3b2;-glucosidase and a gene that codes for the enzyme, and to develop a technique of utilizing the &#x3b2;-glucosidase or a composition that contains the enzyme for processing plants or plant-derived substances. According to the invention, there are provided a novel enzyme showing a &#x3b2;-glucosidase activity and derived from filamentous fungi of the genus Acremonium, a gene that codes for the enzyme, a method of using the gene for expressing &#x3b2;-glucosidase, an enzyme composition that contains &#x3b2;-glucosidase, and a method of processing plants or plant-derived substances with the enzyme or the enzyme compositions.

Enzyme having &#x3b2;-glucosidase activity and use thereof

An objective of the present invention is to provide a transformant altered so as to produce a secondary metabolite in which a benzene ring of the secondary product is modified at the para-position with a functional group containing a nitrogen atom. A transformant according to the present invention is a transformant of an organism producing a secondary metabolite having a benzene ring skeleton without substitution at the para-position with a functional group containing a nitrogen atom, said transformant being transformed by introducing genes involved in a biosynthetic pathway from chorismic acid to p-aminophenylpyruvic acid, including a gene encoding an amino acid sequence (SEQ ID NO: 2) having 4-amino-4-deoxychorismic acid synthase activity, a gene encoding an amino acid sequence (SEQ ID NO: 4) having 4-amino-4-deoxychorismic acid mutase activity and a gene encoding an amino acid sequence (SEQ ID NO: 6) having 4-amino-4-deoxyprephenic acid dehydrogenase activity, so as to produce a secondary metabolite having a benzene ring skeleton substituted at the para-position with a functional group containing a nitrogen atom. Another objective of the present invention is to provide a novel gene involved in the biosynthetic pathway from chorismic acid to p-aminophenylpyruvic acid. A novel gene according to the present invention comprises genes encoding the amino acid sequences of SEQ ID NOs: 2, 4 and 6 or modified sequences thereof.

Transformant producing secondary metabolite modified with functional group and novel biosynthesis genes

Growing community of inventors

Odawara, Japan

Kaoru Okakura