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Vol 7, No 3 (2004)
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Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G | Wachiratianchai | Electronic Journal of Biotechnology
doi: 10.2225/vol7-issue3-fulltext-14
Electronic Journal of Biotechnology, Vol 7, No 3 (2004)

Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G

Supawadee Wachiratianchai, Amaret Bhumiratana, Suchat Udomsopagit



Abstract

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 37ºC. 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.




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ISSN:  0717-3458

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