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Title 

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

Authors 

Jae Seok HaK KimJae Jun SongJin-Woo BaeSeung Goo LeeSang Chul LeeHaryoung PooC S ShinM H Sung

Publisher 

Elsevier

Issue Date 

2003

Citation 

Journal of Molecular Catalysis B:Enzymatic, vol. 26, no. 3, pp. 231-240

Keywords 

glutamate dehydrogenaseoverproductionregeneration systemsymbiobacterium toebiithermostabilityamino acidsbacteriagel permeation chromatographybacterial enzymerecombinant enzyme

Abstract 

A 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.

ISSN 

1381-1177

Link 

http://dx.doi.org/10.1016/j.molcatb.2003.06.008

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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