Purification of a ginsenoside-Rb1 hydrolase from Helix snailase / 生物工程学报
Chinese Journal of Biotechnology
; (12): 929-933, 2005.
Article
em Zh
| WPRIM
| ID: wpr-237048
Biblioteca responsável:
WPRO
ABSTRACT
Through a combination of twice DEAE chromatography by NaCl stepwise and gradient elution with gel filtration chromatography, a kind of ginsenoside-Rb1 hydrolase from crude Helix snailase was separated. The hydrolase was purified to apparent homogeneity on SDS-PAGE. It was estimated that the purified hydrolase was consisted of four identical subunits with a molecular mass of 110-115 kD by SDS-PAGE and gel filtration chromatography. The Km and Vmax values for ginsenoside-Rb1 were calculated to be 0.790 mmol/L and 10.192 micromol/(min x mg) of protein respectively. The ginsenoside-Rb1 hydrolase could only hydrolyze the glycosidic bond at the C20 position of ginsenoside-Rb1 into ginsenoside-Rd.
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Catálise
/
Química
/
Ginsenosídeos
/
Caracois Helix
/
Hidrolases
/
Metabolismo
Limite:
Animals
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2005
Tipo de documento:
Article