Abstract: There is provided a dried L-glutamate oxidase composition containing an L-glutamate oxidase, which is stable even if it is stored for such a long term as one year or longer. The composition is a dried composition, preferably lyophilized product, containing an L-glutamate oxidase and a disaccharide. A preferred example of the disaccharide is lactose. Content of the disaccharide per 100 U of the L-glutamate oxidase is preferably 0.5 to 50 mg.

Abstract: There is provided a dried L-glutamate oxidase composition containing an L-glutamate oxidase, which is stable even if it is stored for such a long term as one year or longer. The composition is a dried composition, preferably lyophilized product, containing an L-glutamate oxidase and a disaccharide. A preferred example of the disaccharide is lactose. Content of the disaccharide per 100 U of the L-glutamate oxidase is preferably 0.5 to 50 mg.

Abstract: The present invention provides a novel L-glutamate oxidase, a gene encoding the enzyme, and a method for producing the enzyme. By use of a gene encoding the enzyme, L-glutamate oxidase can be readily prepared at low costs through a recombinant DNA technique. The novel L-glutamate oxidase has the following physicochemical properties: (A) action: catalyzing the following reaction: L-glutamic acid+O2+H2O??-ketoglutaric acid+H2O2+NH3; (B) substrate specificity: being specific to L-glutamic acid; (C) molecular weight and subunit structure: molecular weight as determined through SDS-polyacrylamide gel electrophoresis of 70,000±6,000, molecular weight as determined through gel filtration of 140,000±10,000, and being a dimer formed of the same subunits having a molecular weight of 70,000±6,000; (D) optimum pH: around pH 6.0 to 8.5; (E) heat stability: being stable up to 60° C. at a pH of 7.4 for 30 minutes; and (F) coenzyme: flavin adenine dinucleotide (FAD).

Abstract: The present invention provides a novel L-glutamate oxidase, a gene encoding the enzyme, and a method for producing the enzyme. By use of a gene encoding the enzyme, L-glutamate oxidase can be readily prepared at low costs through a recombinant DNA technique. The novel L-glutamate oxidase has the following physicochemical properties: (A) action: catalyzing the following reaction: L-glutamic acid+O2+H2O??-ketoglutaric acid+H2O2+NH3; (B) substrate specificity: being specific to L-glutamic acid; (C) molecular weight and subunit structure: molecular weight as determined through SDS-polyacrylamide gel electrophoresis of 70,000±6,000, molecular weight as determined through gel filtration of 140,000±10,000, and being a dimer formed of the same subunits having a molecular weight of 70,000±6,000; (D) optimum pH: around pH 6.0 to 8.5; (E) heat stability: being stable up to 60° C. at a pH of 7.4 for 30 minutes; and (F) coenzyme: flavin adenine dinucleotide (FAD).

Abstract: The present invention provides a novel L-glutamate oxidase, a gene encoding the enzyme, and a method for producing the enzyme. By use of a gene encoding the enzyme, L-glutamate oxidase can be readily prepared at low costs through a recombinant DNA technique.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: L-lysine contained in a sample can be efficiently determined by using the L-lysine .alpha.-oxidase. The preferred enzyme is 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.

Abstract: The enzyme pterin deaminase may be used as an antitumor agent, and can be produced from cultures of the fungal genera Aspergillus, Mucor, Rhizopus, and Penicillium.