Kyowa Hakko Kogyo Co., Ltd.

Takayuki Uwajima

Kinya Fujishiro

Osamu Terada

Kazuo Aisaka

Hiroko Akita

Yoshiaki Shimizu

Akira Mihara

Toshiaki Nagai

Mayumi Ando

Kenichi Mochida

Kenichiro Takayama

Tamotsu Eguchi

Yukihiro Kuge

Takashi Oshiro

A process for producing cholesterol oxidase from a recombinant microorganism, the microorganism itself and its recombinant plasmid are disclosed. The cholesterol oxidase has a particular amino acid sequence, a high substrate affinity and a working pH in the acidic range. The gene for this cholesterol oxidase was derived from . The cholesterol oxidase is used for the quantitative determination of cholesterol.

Cholesterol oxidase

A cholesterol oxidase having a particular amino acid sequence and having a high substrate affinity and a working pH in an acidic range is produced by Brevibacterium sterolicum.

A process for producing cholesterol oxidase from a recombinant microorganism, the microorganism itself and its recombinant plasmid are disclosed. The cholesterol oxidase has a particular amino acid sequence, a high substrate affinity and a working pH in the acidic range. The gene for this cholesterol oxidase was derived from Brevibacterium sterolicum. The cholesterol oxidase is used for the quantitative determination of cholesterol.

A process for producing cholesterol oxidase from a recombinant microorganism, the microorganism itself and its recombinant plasmid are disclosed. The cholesterol oxidase has a particular amino acid sequence, a high substrate affinity and a working pH in the acidic range. The gene for this cholesterol oxidase was derived from Brevibacterium sterolicum.

A novel acetylpolyamine amidohydrolase is described. The enzyme specifically hydrolyzes the amino bond in acetylputrescine, acetylcadaverine, acetylspermidine and acetylspermine with strong substrate affinity. The enzyme is preferably produced by culturing a microorganism belonging to the genus Mycoplana, and is used in the quantitative determination of polyamine contained in a living body sample, which is useful for cancer diagnosis.

Novel acetylpolyamine amidohydrolase

The invention relates to a process for producing L(-)-tetrahydrofolic acid which comprises allowing dihydrofolate reductase to act upon dihydrofolic acid in the presence of (1) NADP or NADPH, and (2) glucose and glucose dehydrogenase. L(-)-tetrahydrofolic acid is useful as the intermediate for L(-)-leucovarin.

Process for producing L(-)-tetrahydrofolic acid

Neuraminidase is produced by culturing a neuraminidase producing microorganism belonging to the genus Micromonospora. The neuraminidase is useful for the quantitative determination of a sialic acid-containing substance in a sample.

Process for producing neuraminidase

Process for producing bilirubin oxidase

The present invention provides a process for producing N-acetylneuraminate lyase using a microorganism constructed by recombinant DNA techniques.

Process for producing N-acetylneuraminate lyase

Disclosed is a new enzyme, aldehyde oxidase, which catalyzes the oxidation of an aldehyde to a corresponding acid but does not have any catalytic action upon other substrates. Also disclosed is a fermentative process from producing the enzyme.

Novel aldehyde oxidase and process for producing same

Glycerol oxidase is an oxidizing enzyme of glycerol characterized by its ability to oxidize glycerol in the presence of oxygen to form hydrogen peroxide and glyceraldehyde. This enzyme is produced by cultivation of a microorganism belonging to the genus Aspergillus or the genus Neurospora in a nutrient medium.

Glycerol oxidase and process for the production thereof and method for

Glycerol oxidase II is an oxidizing enzyme of glycerol characterized by its ability to oxidize glycerol in the presence of oxygen to form hydrogen peroxide and glyceraldehyde. This action of the present enzyme is the same as that of the enzyme glycerol oxidase I disclosed in U.S. application Ser. No. 897,695 filed on Apr. 19, 1978. However, this enzyme has characteristic properties in substrate specificity, optimum and stable pH, optimum temperature for action, substrate affinity (Michaelis constant glycerol). This enzyme is produced by culturing a microorganism belonging to the genus Penicillium.

Glycerol oxidase and process for the production thereof

Creatinine desimidase is produced by fermentation of microorganisms belonging to the genera Brevibacterium, Corynebacterium, Pseudomonas and Arthrobacter. The enzyme is recovered from the microbial cells and culture liquor. The enzyme is used for the quantitative determination of creatinine in a sample.

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Machida, Japan

Takayuki Uwajima