Cloning, characterization and molecular docking of a highly thermostable ß-1,4-glucosidase from Thermotoga petrophila.
Biotechnol Lett
; 34(9): 1703-9, 2012 Sep.
Article
en En
| MEDLINE
| ID: mdl-22714267
ABSTRACT
A genomic DNA fragment, encoding a thermotolerant ß-glucosidase, of the obligate anaerobe Thermotoga petrophila RKU-1 was cloned after PCR amplification into Escherichia coli strain BL21 CodonPlus. The purified cloned enzyme was a monomeric, 51.5 kDa protein (by SDS-PAGE) encoded by 1.341 kb gene. The estimated K (m) and V (max) values against p-nitrophenyl-ß-D-glucopyranoside were 2.8 mM and 42.7 mmol min(-1) mg(-1), respectively. The enzyme was also active against other p-nitrophenyl substrates. Possible catalytic sites involved in hydrolyzing different p-nitrophenyl substrates are proposed based on docking studies of enzyme with its substrates. Because of its unique characters, this enzyme is a potential candidate for industrial applications.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bacterias Anaerobias
/
Glucano 1,4-beta-Glucosidasa
Idioma:
En
Revista:
Biotechnol Lett
Año:
2012
Tipo del documento:
Article
País de afiliación:
Pakistán