Purification and characterization of ginsenoside-alpha-L-rhamnosidase.
In this paper the ginsenoside-alpha-(1-->2)-L-rhamnosidase from microorganisms was purified and characterized. The enzyme hydrolyzed the 6-C, alpha-(1-->2)-L-rhamnoside of 20(S) and 20(R)-ginsenoside Rg2 to produce the 20(S) and 20(R)-ginsenoside Rh1, but hardly hydrolyzed the alpha-rhamnoside of pNPR. The enzyme molecular weight was about 53 kDa. The optimum temperature of enzyme reaction was 40 degrees C, and the optimum pH was 5.
Yu
Hongshan
H
Department of Food Science and Biotechnology, Dalian Institute (College) of Light Industry, Ganjingzi-qu, PR China.
Gong
Jinmei
J
Zhang
Chunzhi
C
Jin
Fengxie
F
D020095:Absidia / Q000201:enzymology*; D005285:Fermentation; D036145:Ginsenosides; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D012503:Saponins / Q000378:metabolism*
D036145:Ginsenosides; D012503:Saponins; D006026:Glycoside Hydrolases; C022525:alpha-L-rhamnosidase