Ajinomoto Co., Ltd.

Toyama Prefecture

Mitsubishi Rayon Company, Limited

Toyama Prefectural University

Mitsubishi Chemical Corporation

Mitsubishi Gas Chemical Company, Inc.

Central Glass Company, Limited

Nippon Steel Chemical Co., Ltd.

Toyama Prefectual University

Public University Corporation Toyama Prefectural University

Yasuhisa Asano

Fujio Yu

Yasuhiro Mihara

Hideaki Yamada

Eiji Sato

Takashi Utagawa

Takanori Akiyama

Daisuke Matsui

Atsushi Inoue

Masafumi Kameya

Yuko Oku

Akihiro Ishii

Osamu Kurahashi

Wataru Mizunashi

Tamejiro Hiyama

Hisashi Kawasaki

Megumi Shimaoka

Kozo Murao

Kohki Ishikawa

Ei-ichiro Suzuki

Nobuhisa Shimba

Shuichi Mitamura

Kenji Oki

Keiko Gondoh

Tohru Kouda

Tetsuro Nishii

Fumihiro Motojima

Kenichi Fuhshuku

Techawaree Ueatrongchit

Takuya Yamaguchi

Rie Kozutsumi

Hiroyasu Onaka

Hiroshi Kajiro

Ken-Ichi Fuhshuku

Yuko Ishida

Mohammad Dadashipour Lakmehsari Lakmehsari

Eiji c/o Mitsubishi Chemical Group Sato

Fujio c/o Mitsubishi Chemical Group Yu

Takanori c/o Mitsubishi Chemical Group Akiyama

Atsushi c/o Niigata Research Laboratory Inoue

As a method for producing a 3-hydroxyisobutyric acid ester using a biocatalyst, a method for producing a 3-hydroxyisobutyric acid ester, including a step of allowing an alcohol or phenol to act on 3-hydroxyisobutyryl-CoA in the presence of alcohol acyltransferase to produce a 3-hydroxyisobutyric acid ester is provided.

Method for producing 3-hydroxyisobutyric acid ester and methacrylic ester

A method for producing an active-form mutant enzyme, by specifying a protein of which a native form exhibits an enzyme activity but which has 10% or less enzyme activity of the native form when a gene of the protein is expressed to provide an inactive-form enzyme; determining a sequence conservation of amino acid residues in an amino acid sequence of the inactive-form enzyme and specifying amino acid residue(s) for which sequence conservation in the inactive-form enzyme is lower than sequence conservation of other amino acid(s) of the same residue; preparing a gene having a base sequence that codes for the amino acid sequence of the inactive-form enzyme in which at least one said specified amino acid residue is substituted by another amino acid with a higher sequence conservation; and expressing the gene to obtain an enzyme that exhibits an enzyme activity of the native form protein.

Method of producing an active-form mutant enzyme

Provided are a method for obtaining an HNL gene and HNL derived from a millipede other than, and preparing a practically useable amount of HNL; and a method for producing optically active cyanohydrin using this HNL. A method for producing a millipede-derived HNL gene. A method that includes the selection of a gene having a base sequence that encodes a conserved amino acid sequence TAX1DIX2G (SEQ ID NO: 15) or VPNGDKIH (SEQ ID NO: 16) of millipede-derived HNL from genes present in an organism belonging to the Diplopoda. A protein having an amino acid sequence of any of (1)-(3) and having HNL activity. (1) An amino acid sequence listed in any of SEQ ID NOS: 1, 3, 5, 7, 9, 11, 13, 83, 85, 87, or 89; (2) an amino acid sequence having amino acids deleted, substituted, and/or added in an amino acid sequence of (1); or (3) an amino acid sequence having 90% or greater identity to an amino acid sequence of (1). A method for preparing optically active cyanohydrin by causing this millipede-derived HNL to act on a reaction solvent that contains an aldehyde or the like and a substance that generates hydrogen cyanide or the like.

Hydroxynitrile lyase

A method for expressing, as a soluble protein or an active-form mutant enzyme, an enzyme that cannot be expressed as a soluble protein or an active-form enzyme in a heterologous expression system or that is obtained in a minute amount even when an active-form enzyme is expressed, the method including a technique for selecting an effective mutation site and a mutated amino acid. A new active-form mutant enzyme is also disclosed. The method involves: specifying an insoluble protein or an inactive-form enzyme; specifying a hydrophilic amino acid in a hydrophobic domain and/or a hydrophobic amino acid in a hydrophilic domain of an &#x3b1;-helix structure portion of the insoluble protein or the inactive-form enzyme and preparing a gene that codes for an amino acid sequence in which a substitution is made to the hydrophilic amino acid in the hydrophobic domain and/or the hydrophobic amino acid in the hydrophilic domain.

Provided is a method for producing a methacrylic acid ester using a biocatalyst, said method comprising a step of reacting an alcohol or a phenol with methacrylyl-CoA in the presence of an alcohol acyltransferase originated from a plant selected from the group consisting of a plant belonging to the genus, a plant belonging to the genus, a plant belonging to the genus, a plant belonging to the genus, a plant belonging to the genusand a plant belonging to the genusto thereby synthesize the methacrylic acid ester.

Method for producing methacrylic acid ester and novel methacrylic acid ester synthetase

There is provided a method for quantifying a subject substance, of which typical examples are amino acids. The method of the present invention comprises the following steps: the step of allowing an enzyme that can generate pyrophosphate by using adenosine triphosphate (ATP) as a substrate with converting the subject substance to act on the subject substance to generate pyrophosphate; the step of allowing pyruvate pyrophosphate dikinase (PPDK) to act on the generated pyrophosphate in the presence of adenosine monophosphate (AMP) and phosphoenolpyruvate (PEP) to generate ATP, phosphoric acid, and pyruvate; and the step of quantifying the generated pyruvate, and amount of the subject substance is determined on the basis of the obtained amount of pyruvate. According to the present invention, an amino acid in a biological sample containing a lot of various kinds of contaminants such as inorganic phosphoric acid and urea can be conveniently and quickly quantified without being influenced by the contaminants.

Method for quantifying amino acids with pyrophosphate

Disclosed is a method for quantifying L-tryptophan involving a step for mixing a specimen, L-tryptophan oxidase, and water, a step for allowing the obtained reaction solution to stand a predetermined period of time in the presence of oxygen, and a step for measuring the reaction product resulting from action of enzymes present in the reaction solution after allowing to stand. Also disclosed are a kit used to quantify the L-tryptophan containing L-tryptophan oxidase, and an enzyme sensor using the L-tryptophan oxidase. This method, kit and enzyme sensor use an L-tryptophan-specific enzyme, so are capable of quantifying L-tryptophan even in the presence of other amino acids.

Method of analyzing L-tryptophan in biological samples, and kit used therein

Methods are provided measuring L-lysine using a variant enzyme, an L-lysine measurement kit, and an enzyme sensor. Variant L-amino acid oxidase having a predetermined amino acid mutation, and having oxidase activity that is highly substrate-specific for L-lysine; a method for measuring L-lysine using this variant enzyme; an L-lysine measurement kit; and an enzyme sensor are also provided.

L-amino acid oxidase, method for measuring L-lysine, kit and enzyme sensor

Disclosed is a method for producing (S)-1,1,1-trifluoro-2-propanol with high optical purity and high yield by having at least one kind of microorganism, which is selected from the group consisting ofand, act on 1,1,1-trifluoroacetone. Since microorganisms found in nature are made to act in a natural state, the problems to be raised when a transformant or the like is used can be avoided in this method. Consequently, the method can be easily put in industrial practice.

[object Object]

A method for analyzing L-threonine contained in an specimen, which includes the steps of mixing a sample containing the specimen with an L-threonine dehydrogenase derived fromand a coenzyme NAD+ and analyzing the amount of NADH or 2-amino-3-oxobutyric acid after a predetermined period; an L-threonine dehydrogenase derived from, which is a novel L-threonine dehydrogenase (TDH; EC 1.1.1.103) and can be utilized in the above-mentioned analysis method; a method for preparing a gene or the like to be used in the preparation of the enzyme, or a method for preparing the enzyme; an L-threonine analysis kit which includes (A) the L-threonine dehydrogenase and (B) a coenzyme NAD+; an enzyme preparation for use in the analysis of L-threonine, which includes the L-threonine dehydrogenase contained in a buffer solution; and an enzyme sensor utilizing the L-threonine dehydrogenase.

L-threonine analysis method and L-threonine dehydrogenase

An improved hydroxynitrile lyase characterized by having a mutation of substitution of at least one amino acid residue in the amino acid sequence of a wild-type hydroxynitrile lyase with another amino acid and by its hydroxynitrile lyase activity per transformant being higher than the hydroxynitrile lyase activity per transformant into which the wild-type hydroxynitrile lyase gene is introduced; and a method for producing a hydroxynitrile lyase, comprising expressing the improved hydroxynitrile lyase in a host and recovering the improved hydroxynitrile lyase from the resultant culture.

Substitutional variants of hydroxynitrile lyase with high specific activity and methods of use

A recombinant microorganism is produced by introducing a DNA encoding an enzyme which hydrolyzes an amido bond of L-amino acid amide, especially L-2-alkylcysteine amide, and L-amino acid is produced by using cells or cell processed product of the obtained microorganism.

L-amino acid amide asymmetric hydrolase and DNA encoding the same

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Toyama, Japan

Yasuhisa Asano