[Extracellular L-glutamate oxidase from Streptomyces sp. Z-11-6: preparation of it and its properties].
Mutagenesis induced with nitrous acid and subsequent selection allowed a genetically stable mutant strain, Streptomyces sp. Z-11-6, to be obtained, whose L-glutamate oxidase activity was 40-fold higher than that of the original natural isolate and was as great as 1.6-1.8 units/ml of culture liquid. A procedure for the isolation and purification of the enzyme was developed; the biochemical properties of the enzyme were studied. Out of 20 amino acids tested (including D-glutamate), the glutamate oxidase from Streptomyces sp. Z-11-6 was active only with L-glutamate. This allows the concentration of L-glutamate to be determined in the presence of other amino acids. Calcium chloride at a concentration of 0.1-0.5% promoted the secretion of the extracellular glutamate oxidase.
Sukhacheva
M V
MV
Department of Microbiology, Biological Faculty, Moscow State University, Vorob'evy gory, Russia.
Netrusov
A I
AI
D000594:Amino Acid Oxidoreductases / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000378:metabolism*; D018533:Biomass; D002614:Chelating Agents / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000494:pharmacology; D016296:Mutagenesis; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity; D013696:Temperature
D002614:Chelating Agents; D004791:Enzyme Inhibitors; D008670:Metals; D000594:Amino Acid Oxidoreductases; C023061:L-glutamate oxidase