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.