Purification of a ginsenoside-Rb1 hydrolase from Helix snailase.
- Author:
Xin LIU
1
;
Yu CUI
;
Ling YANG
;
Sheng-Li YANG
Author Information
1. Lab of Pharmaceutical Resource Discovery, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Catalysis;
Ginsenosides;
metabolism;
Helix (Snails);
enzymology;
Hydrolases;
chemistry;
isolation & purification;
metabolism
- From:
Chinese Journal of Biotechnology
2005;21(6):929-933
- CountryChina
- Language:Chinese
-
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.
