Purification of a ginsenoside-Rb1 hydrolase from Helix snailase / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 929-933, 2005.
Artículo
en Chino
| WPRIM
| ID: wpr-237048
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:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Catálisis
/
Química
/
Ginsenósidos
/
Caracoles Helix
/
Hidrolasas
/
Metabolismo
Límite:
Animales
Idioma:
Chino
Revista:
Chinese Journal of Biotechnology
Año:
2005
Tipo del documento:
Artículo
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