Expression, purification and enzymatic characterization of Bacillus polymyxa beta-glucosidase gene( bglA ) in Escherichia coli / 生物工程学报
Chinese Journal of Biotechnology
; (12): 741-744, 2004.
Article
em Zh
| WPRIM
| ID: wpr-249943
Biblioteca responsável:
WPRO
ABSTRACT
The beta-glucosidase encoding gene bglA was cloned from Bacillus polymyxa 1.794. The bglA gene was inserted in expression vector pET28a(+) and transformed into Escherichia coli BL21 (DE3), finally the recombinant strain BL1979 was obtained. Induced by IPTG, the expression P-glucosidase activity reached to 24.7 IU/mL. The optimum temperature and optimum pH of the recombinant expression P-glucosidase in BL1979 were 37 degrees C and 7.0 respectively,the purity can reach to 92.7%. Analysis of the fusion protein by nondenaturing gradient gel electrophoresis, we found the fusion protein exists in dimmer, tetramer,hexamer and octamer, they all have hydrolase activity.
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Plasmídeos
/
Bacillus
/
Proteínas Recombinantes
/
Beta-Glucosidase
/
Escherichia coli
/
Genética
/
Metabolismo
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2004
Tipo de documento:
Article