Thermostable glutamate dehydrogenase from a commensal thermophile, Symbiobacterium toebii; overproduction, characterization, and application

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dc.contributor.authorJae Seok Ha-
dc.contributor.authorK Kim-
dc.contributor.authorJae Jun Song-
dc.contributor.authorJin-Woo Bae-
dc.contributor.authorSeung Goo Lee-
dc.contributor.authorSang Chul Lee-
dc.contributor.authorHaryoung Poo-
dc.contributor.authorC S Shin-
dc.contributor.authorM H Sung-
dc.date.accessioned2017-04-19T09:00:24Z-
dc.date.available2017-04-19T09:00:24Z-
dc.date.issued2003-
dc.identifier.issn1381-1177-
dc.identifier.uri10.1016/j.molcatb.2003.06.008ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6276-
dc.description.abstractA gene encoding glutamate dehydrogenase (GDH) was found in the genome sequence of a commensal thermophile, Symbiobacterium toebii. The amino acid sequence deduced from the gdh I of S. toebii was well conserved with other thermostable GDHs. The gdh I which encodes GDH consisting of 409 amino acids was cloned and expressed in E. coli DH5α under the control of a highly constitutive expression (HCE) promoter in a pHCE system. The recombinant GDH was expressed without addition of any inducers in a soluble form. The molecular mass of the GDH was estimated to be 263kDa by Superose 6 HR gel filtration chromatography and 44kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicating that the GDH was composed of hexameric form. The optimal temperature and pH of the purified enzyme were 60°C and 9.0, respectively, and the purified GDH retained more than 75% of its original activity after an incubation at 70°C for 30min. Although NADP(H) was the preferred cofactor, S. toebii GDH was able to utilize either NADP(H) or NAD(H) as coenzyme.-
dc.publisherElsevier-
dc.titleThermostable glutamate dehydrogenase from a commensal thermophile, Symbiobacterium toebii; overproduction, characterization, and application-
dc.title.alternativeThermostable glutamate dehydrogenase from a commensal thermophile, Symbiobacterium toebii; overproduction, characterization, and application-
dc.typeArticle-
dc.citation.titleJournal of Molecular Catalysis B: Enzymatic-
dc.citation.number3-
dc.citation.endPage240-
dc.citation.startPage231-
dc.citation.volume26-
dc.contributor.affiliatedAuthorJae Seok Ha-
dc.contributor.affiliatedAuthorJae Jun Song-
dc.contributor.affiliatedAuthorJin-Woo Bae-
dc.contributor.affiliatedAuthorSeung Goo Lee-
dc.contributor.affiliatedAuthorSang Chul Lee-
dc.contributor.affiliatedAuthorHaryoung Poo-
dc.contributor.alternativeName하재석-
dc.contributor.alternativeName김광-
dc.contributor.alternativeName송재준-
dc.contributor.alternativeName배진우-
dc.contributor.alternativeName이승구-
dc.contributor.alternativeName이상철-
dc.contributor.alternativeName부하령-
dc.contributor.alternativeName신철수-
dc.contributor.alternativeName성문희-
dc.identifier.bibliographicCitationJournal of Molecular Catalysis B: Enzymatic, vol. 26, no. 3, pp. 231-240-
dc.identifier.doi10.1016/j.molcatb.2003.06.008-
dc.subject.keywordglutamate dehydrogenase-
dc.subject.keywordoverproduction-
dc.subject.keywordregeneration system-
dc.subject.keywordsymbiobacterium toebii-
dc.subject.keywordthermostability-
dc.subject.localglutamate dehydrogenase-
dc.subject.localoverproduction-
dc.subject.localOver-production-
dc.subject.localOverproduction-
dc.subject.localregeneration system-
dc.subject.localsymbiobacterium toebii-
dc.subject.localSymbiobacterium toebii-
dc.subject.localThermostability-
dc.subject.localthermostability-
dc.description.journalClassN-
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Research on National Challenges > Infectious Disease Research Center > 1. Journal Articles
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