Purification and characterization of ginsenoside-alpha-L-rhamnosidase

Chem Pharm Bull (Tokyo). 2002 Feb;50(2):175-8. doi: 10.1248/cpb.50.175.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Absidia / enzymology*
  • Fermentation
  • Ginsenosides
  • Glycoside Hydrolases / isolation & purification*
  • Glycoside Hydrolases / metabolism
  • Molecular Weight
  • Saponins / metabolism*

Substances

  • Ginsenosides
  • Saponins
  • Glycoside Hydrolases
  • alpha-L-rhamnosidase