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

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dc.contributor.authorSupawadee Wachiratianchaien_US
dc.contributor.authorAmaret Bhumiratanaen_US
dc.contributor.authorSuchat Udomsopagiten_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherThailand National Science and Technology Development Agencyen_US
dc.date.accessioned2018-07-24T03:35:59Z
dc.date.available2018-07-24T03:35:59Z
dc.date.issued2004-12-15en_US
dc.description.abstractAn 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.en_US
dc.identifier.citationElectronic Journal of Biotechnology. Vol.7, No.3 (2004), 274-281en_US
dc.identifier.doi10.2225/vol7-issue3-fulltext-14en_US
dc.identifier.issn07173458en_US
dc.identifier.other2-s2.0-12444262200en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/21109
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=12444262200&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleIsolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18Gen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=12444262200&origin=inwarden_US

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