In this paper, the saponin enzymatic hydrolysis of ginsenoside Rg3 was studied. The $ginsenoside-{eta}-glucosidase$ from FFCDL-48 strain mainly hydrolyzed the ginsenoside Rg3 to Rh2, the enzyme from FFCDL-00 strain hydrolyzed Rg3 to the mixture of Rh2 and protopanaxadiol (aglycon). The $ginsenoside-{eta}-glucosidase$ from FFCDL-48 strain was purified with a column of DEAE-Cellulose to one spot in the SDS polyacrylamide gel electrophoresis. During the purification, the enzyme specific acitvity was increased about 10 times. The purified $ginsenoside-{eta}-glucosidase$ can hydrolyze the Rg3 to Rh2, but do not hydrolyze the $p-nitrophenyl-{eta}-glucoside$ which is a substrate of original exocellulase such as ${eta}-glucosidase$ of cellulose. The molecular weight of $ginsenoside-{eta}-glucosidase$ was 34,000, the optimal temperature of enzyme reaction was $50^{circ}C,$ and the optimal pH was 5.0.