Abstract
The properties of L-glutamate oxidase, a novel L-glutamic acid oxidizing enzyme from Streptomyces violascens H82-N-SY7 were examined. The enzyme showed absorption maxima at 280, 390 and 470 nm and a marked shoulder at 490 nm, and contained 1 mol of flavin-adenine dinucleotide (FAD) per mol of enzyme. Enzyme activity was inhibited by Ag+, Hg2+, p-chloromercuribenzoate (PCMB) and N-bromosuccinimide. The enzyme catalyzed the oxidation of L-glutamic acid using molecular oxygen as a primary electron acceptor and produced α-ketoglutaric acid, NH3 and hydrogen peroxide according to the following schema : L-glutamic acid+H2O+O2→α-ketoglutaric acid+NH3+H2O2. L-Glutamate oxidase was used in a specific and sensitive determination procedure for L-glutamic acid.
