Purification and characterization of ginsenoside-α-L-rhamnosidase

Abstract

In this paper the ginsenoside-α-(1→2)-L-rhamnosidase from microorganisms was purified and characterized. The enzyme hydrolyzed the 6-C, α-(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 α-rhamnoside of pNPR. The enzyme molecular weight was about 53 kDa. The optimum temperature of enzyme reaction was 40°C, and the optimum pH was 5. © 2002 Pharmaceutical Society of Japan.