Abstract
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 fromStreptomyces 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.
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Sukhacheva, M.V., Netrusov, A.I. Extracellular L-glutamate oxidase ofStreptomyces sp. Z-11-6: Obtainment and properties. Microbiology 69, 17–20 (2000). https://doi.org/10.1007/BF02757250
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DOI: https://doi.org/10.1007/BF02757250