Abstract
L-Glutamate oxidase, a novel L-glutamic acid oxidizing enzyme, has been found in the culture broth of Streptomyces violascens. The enzyme has been purified 914-fold by precipitation with ammonium sulfate, affinity chromatography on L-glutamic acid-Sepharose 6B and L-glutamine-Sepharose 6B, hydroxyapatite chromatography and gel filtration on Sephadex G-100. The purified enzyme showed a single band on polyacryl-amide disc gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be about 60000. The purified enzyme exhibited a characteristic flavoprotein spectrum. The enzyme catalyzed the oxidation of L-glutamic acid and L-glutamine without a requirement for any exogenous cofactor.
