Supawadee WachiratianchaiAmaret BhumiratanaSuchat UdomsopagitMahidol UniversityThailand National Science and Technology Development Agency2018-07-242018-07-242004-12-15Electronic Journal of Biotechnology. Vol.7, No.3 (2004), 274-281071734582-s2.0-12444262200https://repository.li.mahidol.ac.th/handle/20.500.14594/21109An 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyImmunology and MicrobiologyArticleSCOPUS10.2225/vol7-issue3-fulltext-14