Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: Novel bilirubin oxidase inactive against phenol, catechol, and hydroquinone, and a process for preparing said enzyme by recovering it from a culture liquor of bilirubin oxidase producing microorganisms belonging to the genus Coprinus, Trametes, Coriolus, Pholiota, Pleurotus, Lenzites, or Fomitopsis. This enzyme can decompose bilirubin when added to a bilirubin-containing solution, and makes it possible to assay bilirubin by measuring a decrease in absorption in the visible region of the reaction solution. Thus, it can be used for assaying bilirubin and for removing it from a sample to avoid its interference in determining a substrate or an enzyme activity.

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

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: Cholesterol esterase is prepared by fermentation of a microorganism capable of producing cholesterol esterase and belonging to the genus Pseudomonas. Cholesterol esterase is useful for the determination of total serum cholesterol.