Kaneka Corporation

Kanegafuchi Kagaku Kogyo Kabushiki Kaisha

Kanegafuchi Chemical Industry Co., Ltd.

Nippon Mic, Co., Ltd

Natural Clean Co., Ltd.

Yukio Yamada

Yasuhiro Ikenaka

Satomi Takahashi

Kazuyoshi Yajima

Hirokazu Nanba

Masayuki Takano

Noriyuki Kizaki

Junzo Hasegawa

Yoshihiko Yasohara

Akira Iwasaki

Kenji Inoue

Masahiro Ogura

Sakayu Shimizu

Hideaki Yamada

Yasuyoshi Ueda

Kiyoshi Watanabe

Akira Nishiyama

Takehisa Ohashi

Masaru Mitsuda

Noboru Ueyama

Makoto Miyazaki

Yoshio Shimada

Takeshi Kondo

Kazuhiko Yamada

Keiji Matsumoto

Michio Nomura

Takehiko Yamane

Yoshiro Hiraishi

Yoshifumi Yanagita

Kazuma Okubo

Yasuhiro Katayama

To provide a method for preparing optically active compounds, which mainly contain (R)-amino compounds, by microbial enzymes efficiently and inexpensively; a polypeptide having stereoselective transaminase activity which can be suitably used for the above preparation method; and a DNA encoding the polypeptide. A method for preparing an optically active amino compound, characterized in stereoselectively transaminating by acting a transaminase on an amino group acceptor, a ketone compound in the presence of an amino group donor, a primary amine; a DNA comprising a nucleotide sequence encoding a polypeptide having stereoselective transaminase activity; and a polypeptide having stereoselective transaminase activity obtainable from a culture of a microorganism belonging to the genus Arthrobacter.

Producing optically active amino compounds

This invention provides a process for producing optically active 2-[6-(hydroxymethyl)-1,3-dioxan-4-yl]acetic acid derivatives, which are of value as intermediates of drugs, from inexpensive starting materials without using any special equipment such as that required for super-low temperature reactions. A process for producing optically active 2-[6-(hydroxymethyl)-1,3-dioxan-4-yl]acetic acid derivatives which comprises

Process for producing optically active 2-[6-(hydroxymethyl)-1,3-dioxan-4-yl]acetic acid derivatives

A novel polypeptide for producing tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate, a gene encoding the polypeptide, and a method of using the polypeptide, are provided. The polypeptide has an enzyme activity to asymmetrically reduce tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate to tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate. The polypeptide comprises the amino acid sequence represented by SEQ ID NO. 1 in the Sequence Listing, or the amino acid sequence having at least one amino acid substitution, insertion, deletion, or addition thereof.

Carbonyl reductase, gene thereof and method of using the same

Process for the preparation of optically active 2-&lsqb;6-hydroxymethyl)-1,3-dioxan-4yl&rsqb;acetic acid derivatives

Relating to an enzyme capable of efficiently converting a ketone compound to an optically active amino compound by transamination, and a process for preparing an optically active amino compound using the enzyme. An (S)-&agr;-phenethylamine:pyruvate transaminase, which acts on (S)-&agr;-phenethylamine and a ketone compound, thereby catalyzing transamination for forming acetophenone and an amino compound corresponding to the ketone compound; a process for preparing an optically active amino compound using the transaminase; and a method for culturing a microorganism for producing the above transaminase, comprising adding to a medium one or more compounds selected from the group consisting of propylamine, 1-butylamine, 2-butylamine, 2-pentylamine, isopropylamine and isobutylamine as an inducer for the enzyme when a microorganism for producing (S)-&agr;-phenethylamine:pyruvate transaminase is cultured.

(S)-&agr;-phenethylamine: pyruvate transaminase

The method for preparing an optically active (R)-amino compound characterized by the method comprising stereoselectively carrying out amino group transfer by action of an (R)-form-specific transaminase in the co-presence of a ketone compound (amino acceptor), and an amino compound (amino donor) of a racemic form or an (R)-form, to give an optically active (R)-amino compound. According to the present invention, it is made possible to easily prepare at a high yield the optically active (R)-amino compounds and the like having an aryl group and the like at their 1-position, which have been conventionally difficult to prepare.

(R)-transaminase from arthrobacter

Process for producing optically active amino compounds

A shrinkage prevention agent for water washing of clothing that would conventionally have been dry cleaned. The shrinkage prevention agent is compromised of a steam or vacuum dry-distilled liquid of two or more plants selected from sagebrush, beefsteak plant, tea, plantaginales, aloe, chrysanthemum, pine, cedar, cypress. The shrinkage prevention agent is used in a wet cleaning system that includes water washing.

Wet cleaning system with shrinkage prevention agent

A DNA fragment coding for a decarbamylase protein improved in thermostability as the result of replacement of at least one base of a DNA fragment coding for a decarbamylase protein derived from a microorganism with another base and the resultant replacement of at least one of the corresponding amino acids, and its production process; a vector containing the DNA fragment; a transformant obtained by transformation with the vector; as well as a decarbamylase improved in thermostability and its production process. Also disclosed is a process for producing a D-.alpha.-amino acid, which comprises converting an N-carbamoyl-D-.alpha.-amino acid into the corresponding D-.alpha.-amino acid in an aqueous medium by the action of a decarbamylase having a thermostable temperature of 65.degree. C. or higher; and collecting the D-.alpha.-amino acid produced.

DNA coding for decarbamylase improved in thermostability and use thereof

Process for producing D-amino acids with composite immobilized enzyme

Process for the production of D-.alpha.-amino acids by hydrolysis of the

In a process for the production of a D-.alpha.-amino acid, in which an N-carbamyl-D-.alpha.-amino acid corresponding to the general formula: ##STR1## wherein R represents phenyl, hydroxy-substituted phenyl, substituted or unsubstituted alkyl, or thienyl, is converted by a microbial enzyme in an aqueous medium to a D-.alpha.-amino acid corresponding to the general formula: ##STR2## wherein R is the same as defined above, decarbamylase produced by a microorganism of the genus Comamonas, Blastobacter, Alcaligenes, Sporosarcina, Rhizobium, Bradyrhizobium or Arthrobacter is used as the enzyme converting the N-carbamyl-D-.alpha.-amino acid to the D-.alpha.-amino acid. The conversion of the N-carbamyl-D-.alpha.-amino acids to the D-.alpha.-amino acids is carried out in a neutral to alkaline pH range.

Decarbamylase isolated from comamonas or blastobacter

Decarbamylases are provided capable of producing D-.alpha.-amino acids by hydrolysis of N-carbamyl-D-.alpha.-amino acids. A source of the decarbamylases is recombinant microorganisms produced by gene manipulation methods. Decarbamylases having improved thermostability can be obtained in which amino acids at a thermostability-related site of a natural decarbamylase have been replaced with other amino acids by mutating a DNA fragment encoding the natural decarbamylase. Recombinant DNA is obtained from a vector DNA and a DNA fragment encoding a natural decarbamylase where the nucleic acid sequence encoding an amino acid at a thermostability-related site is replaced with a nucleic acid sequence encoding another amino acid. The recombinant DNA is used to produce transformants that produce thermostable decarbamylases. The decarbamylases may be immobilized in purified, partially-purified or crude form or in the form of decarbamylase-containing microbial cells on a support such as a polymer having ion exchange groups or covalent bonding groups. The presence of an antioxidant such as dithiothreitol results in an immobilized decarbamylase preparation that can be repeatedly used 30 times or more.

Recombinant decarbamylases for producing D-.alpha.-amino acids

The present invention is directed to a gene which is related to a D-N-carbamoyl-.alpha.-amino acid amidohydrolase which is an enzyme capable of converting D-N-carbamoyl-.alpha.-amino acids into D-.alpha.-amino acids; a recombinant plasmid in which a DNA fragment containing the gene is incorporated into a vector; a microorganism belonging to the genus Escherichia, Pseudomonas, Flavobacterium, Bacillus, Serratia, Corynebacterium, or Brevibacterium, which is transformed by incorporating the recombinant plasmid thereinto; a process for the production of D-N-carbamoyl-.alpha.-amino acid amidohydrolases, comprising the steps of cultivating the transformed microorganism and collecting the desired product therefrom; a D-N-carbamoyl-.alpha.-amino acid amidohydrolase obtained by the method; and a process for the production of D-.alpha.-amino acids with the aid of an action of the enzyme. The D-N-carbamoyl-.alpha.-amino acid amidohydrolase can be fixed on a support for immobilization and used as an immobilized enzyme.

Process for production of D-.alpha.-amino acids

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Kakogawa, Japan

Yukio Yamada