Purification and characterization of ginsenoside-α-arabinofuranase hydrolyzing ginsenoside Rc into Rd from the fresh root of Panax ginseng

The ginsenoside-alpha-arabinofuranase that hydrolyzes the alpha-(1--> 6)-arabinofuranosyl at 20-C sugar moiety of the ginsenoside Rc to ginsenoside Rd was isolated from the ginseng root, and the enzyme was purified and characterized. The enzyme purified to homogeneity in SDS polyacrylamide get electrophoresis, and its molecular weight was about 86 kDa. The optimum temperature of the ginsenoside-alpha-arabinofuranase was 50 degreesC, and the optimum pH was 5.0. The saponin enzyme was stable at less than 60 degreesC, and pH 4.0-6.0. Ca2+, Mg2+, Zn2+, and Fe3+ ions had hardly effect on ginsenoside-a-arabinofuranase activity, while Cu2+ inhibited enzyme activity. (C) 2002 Published by Elsevier Science Ltd.