In An invertase (EC 3.2.1.26) was extracted from Korean giseng (Panax ginseng C.A. Meyer) with distilled tvater The ginseng invertase was purified about 62.6 folds purified by procedures including ammonium sulfate fractionation , DEAE-cellulofine chromatography and gelfiltrations through Sephadex G-75 and the recovery of enzyme activity was 11.1%. The homogeneity of the purified enzyme was probed by polyacrylamide gel disc electrophoresis. The purifled enzyme was divided into two different subunits by treating with a mixture of SDS and 2-mercautoethanol, and the molecular weight of the large subunit was estimatedtobe 116,000 and that of the small one to be 14,000. The optimal VH and temperature of the enzyme were pH 6 and 45$^{circ}C$, respectively. The enzyme hydrolyzed specifically the hydrolyzation of the -fructofuranosides such as sucrose, raffinose and inulin. The Km values of the enzyme for sucrose and raffinose were determined to be 0.85 and 0.6 mM, respectively.