[Purification of a ginsenoside-Rb1 hydrolase from Helix snailase].
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.
Liu
Xin
X
Lab of Pharmaceutical Resource Discovery, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Cui
Yu
Y
Yang
Ling
L
Yang
Sheng-Li
SL
D000818:Animals; D002384:Catalysis; D036145:Ginsenosides / Q000378:metabolism*; D006372:Helix, Snails / Q000201:enzymology*; D006867:Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
D036145:Ginsenosides; C442759:ginsenoside Rb1; D006867:Hydrolases