Kanegafuchi Kagaku Kogyo Kabushiki Kaisha

Kanegafuchi Chemical Industry Co., Ltd.

Kaneka Corporation

Kanegafuchi Kagaku Kogyo K.k.

Satomi Takahashi

Kenji Inoue

Kazuyoshi Yajima

Yukio Yamada

Yasuhiro Ikenaka

Takehisa Ohashi

Kiyoshi Watanabe

Hirokazu Nanba

Masayuki Takano

Hideaki Yamada

Noboru Ueyama

Koji Yoneda

Yasuyoshi Ueda

Yoshifumi Yanagida

Mitsunori Matsumoto

Junzo Hasegawa

Yoshio Shimada

Shigeo Hayashi

Kazuhiko Yamada

Sakayu Shimizu

Naoaki Taoka

Hideyuki Matsuda

Teruyoshi Koga

Masahiko Yamada

Makoto Kawamukai

Hirotaka Fukumitsu

Yoshihiko Yasohara

Hiroshi Awaji

Michio Nomura

Shingo Matsumoto

Takehiko Yamane

Yoshiro Hiraishi

Yoshifumi Yanagita

Hidetoshi Kutsuki

Kenichi Nishi

Namito Yoshio

Keiichi Yonetsu

Yoshiko Tari

Kazuma Okubo

Kazushige Sumino

Tomoaki Nagamachi

Yasuhiro Katayama

Yoshio Namito

Process for producing coenzyme Q10

A gene of decaprenyl diphosphate synthase, which is the key gene participating in the biosynthesis of coenzyme Q was isolated from a bacterium belonging to the family Rhizobiaceae. By transferring this gene into a microorganism such as and expressing therein, coenzyme Q can be effectively produced.

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

Method of producing 3-amino-2-hydroxy-1-propanol derivatives

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

A process for preparing 5,6-dihydro-4-hydroxy-(S)-6-methyl-thieno[2,3-b]thiopyran-7,7-dioxide having the formula (II): ##STR1## which comprises subjecting 5,6-dihydro-4-oxo-(S)-6-methyl-thieno[2,3-b]thiopyran-7,7-dioxide having the formula (I): ##STR2## to the action of a microorganism to reduce the thienothiopyran derivative having the formula (I), and collecting 5,6-dihydro-4-hydroxy-(S)-6-methyl-thieno-[2,3-b]thiopyran-7,7-dioxide having the formula (II) from the reaction mixture, wherein said microorganism belongs to the genus selected from the group consisting of Ambrosiozyma, Arthroascus, Ashbya, Candida, Cryptococcus, Hansenula, Kluyveromyces, Lipomyces, Lodderomyces, Metschnikowia, Pachysolen, Pichia, Rhodosporidium, Rhodotorula, Saccharomyces, Saccharomycopsis, Schwanniomyces, Sporidiobolus, Spolobolomyces, Stephanoascus, Trigonopsis, Trichosporon and Wingea, according to which, a simple and effective. process for preparing 5,6-dihydro-4-hydroxy-(S)-6-methyl-thieno-[2,3-b]thiopyran-7,7-dioxide.

Process for preparing thienothiopyran derivative

A process for preparing a trans-.beta.-aroylacrylic ester which comprises reacting an aryl methyl ketone and an alkyl acetal of alkyl glyoxylate in the presence of an acid catalyst with heating. This process is excellent in operability, safety and ecomony and therefore is industrially advantageous process.

Process for preparing trans-.beta.-aroylacrylic ester

A process for producing N.sup.2 -(1-(S)-carboxy-3-phenylpropyl)-L-lysil-L-proline of formula (VIII); ##STR1## N.sup.2 -(1-substituted-3-phenylpropyl)-L-lysil-L-proline derivative of formula (VII); ##STR2## and N.sup.2 -(1-carbonyl-3-phenylpropyl)-L-lysil-L-proline derivative of formula (XXVI); ##STR3## is disclosed.

Process for preparing N.sup.2 -(1-carboxy-3-phenylpropyl)-L-lysine

A novel 2,4-dihydroxyadipic acid derivative of the formula: ##STR1## wherein R.sup.1 and R.sup.4 are the same or different and each a hydrogen atom, an alkyl group, an aralkyl group, an aryl group or a silyl group, and R.sup.2 and R.sup.3 are the same or different and each a hydrogen atom or a protective group of a hydroxy group or together form a ring, which is useful as a common intermediate in the synthesis of HMG-CoA reductase inhibitor.

2,4-dihydroxyadipic acid derivative

A malonic monoester is prepared in a good yield by a single step reaction by reacting malonic acid with an alcohol in the presence of a base and an activator of malonic acid selected from the group consisting of an acyl halide or halocarbonate and an acid anhydride or dicarbonate.

Process for preparing malonic monoester

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Kobe, Japan

Satomi Takahashi