Yamasa Shoyu Kabushiki Kaisha

Yamasa Corporation

Yuichiro Midorikawa

Hiroshi Yamauchi

Hitoshi Kusakabe

Hideki Utsugi

Toshitada Noguchi

Kazuya Ishige

Kenji Soda

Tomoki Hamamoto

Akira Kuninaka

Kenjiro Kodama

Kiyoshi Okuyama

Kenji Takenouchi

Haruo Misono

A process for producing uridine diphosphate-N-acetylglucosamine (UDPAG) from uridylic acid (UMP) and N-acetylglucosamine by use of microorganism cells, characterized by adding N-acetylglucosamine kinase thereto. According to the present invention, UDPAG can be efficiently produced even when N-acetylglucosamine is used as a substrate.

Process for producing uridine diphosphate-n-acetylglucosamine

The present invention concerns a process for producing nucleosides by carrying out the reaction of a base donor, a saccharide residue donor and a phosphoric acid donor by the use of an enzyme preparation containing nucleoside phosphorylase, thereby forming an N-glycosidic bond between the base moiety of the base donor and the saccharide moiety of the saccharide residue donor, which comprises using, as the enzyme preparation containing nucleoside phosphorylase, a preparation derived from the cells of one or more kinds of microorganisms belonging to thermophiles of the genus Bacillus and having high nucleoside phosphorylase activity per unit cell weight.

Process for producing nucleosides

L-glutamic acid oxidase, which is an L-amino acid oxidase catalyzing the oxidative deamination of the .alpha.-amino group of L-glutamic acid in the presence of water and oxygen to form .alpha.-ketoglutaric acid, ammonia and hydrogen peroxide, and having a very high substrate specificity for L-glutamic acid substantially without acting on L-glutamine and L-histidine, and also having a high stability, and a microbiological method of production thereof.

L-glutamic acid oxidase and its production

The present invention consists of an analytical method for assay of L-glutamic acid in a sample by the use of an L-glutamic acid oxidase which is an L-amino acid oxidase catalyzing the oxidative deamination of the .alpha.-amino group of L-glutamic acid in the presence of water and oxygen to form .alpha.-ketoglutaric acid, ammonia and hydrogen peroxide, and having a very high substrate specificity for L-glutamic acid substantially without acting on L-glutamine and L-histidine, and also having a high stability, a reagent for analysis to practice the analytical method, a kit for analysis comprising the reagent, and a biosensor employing the enzyme.

Use of novel L-glutamic acid oxidase

An L-lysine .alpha.-oxidase, that is, a novel L-amino acid oxidase having very high substrate-specificity to L-lysine is produced by culturing a specific microorganism belonging to Trichoderma in a medium.

L-Lysine .alpha.-oxidase

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Choshi, Japan

Yuichiro Midorikawa