Publication: Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
Issued Date
2004-12-15
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ISSN
07173458
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2-s2.0-12444262200
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Mahidol University
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SCOPUS
Bibliographic Citation
Electronic Journal of Biotechnology. Vol.7, No.3 (2004), 274-281
Suggested Citation
Supawadee Wachiratianchai, Amaret Bhumiratana, Suchat Udomsopagit Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G. Electronic Journal of Biotechnology. Vol.7, No.3 (2004), 274-281. doi:10.2225/vol7-issue3-fulltext-14 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/21109
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Title
Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
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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 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.