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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 7, No. 3, 2004, pp. 277-284
Bioline Code: ej04031
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 7, No. 3, 2004, pp. 277-284

 en Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
Wachiratianchai, Supawadee; Bhumiratana, Amaret & Udomsopagit, Suchat


An extracellular L-glutamate oxidase (GLOD) was purified from soil-isolated Streptomyces sp 18G. The enzyme had a molecular weight of approximately 120,000 and consisted of two identical subunits, each with a molecular weight of 61,000. The isoelectric point was pH 8.5 and the enzyme had an optimal pH between 7.0-7.4. GLOD showed the maximum activity at 37°C. The GLOD activity was stable at pH ranging from 6.5 to 7.0 for 1 hr. Among 21 amino acids tested for substrate specificity, L-glutamate was almost exclusively oxidized. D-glutamate and L-aspartate were oxidized but only to extents of 0.79% and 0.53%, respectively.

L-glutamate, L-glutamate oxidase, purification, screening, Streptomyces

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