고려인삼(Panax ginseng C.A.Meyer) 중의 invertase를 증류수로 추출한 후 황산암모늄분획, DEAE-cellulofine column chromatography, Sephadex G-75 gel 여과 및 재 gel 여과, streptomycin sulfate 처리 등의 과정을 거쳐서 정제하였다. 효소의 정제율은 약 62,6배였으며 효소활성 수율은 11.1%였다. 정제 invertase는 polyacrylamide gel disc 전기영동에 의하여 균일성이 확인되었으며 high performance liquid chromatography(HPLC)에 의하여 분자량은 약 135,000으로 계산되었다. SDS와 2-mercaptoethanol 처리에 의하여 2개의 각기 다른 subunit로 분리되었으며 이들 중 큰 subunit의 분자량은 116,000이고 작은 subunit는 14,000이었다. 정제효소의 효소반응 최적 pH와 온도는 pH6.0과 45℃이었다. 정제효소는 sucrose, raffinose, inulin 등의 β-D-fructoside 결합을 가진 기질에 특이적으로 작용하여 전형적인 β-D-fructofuranosidase의 특징을 나타내었다. Sucrose와 raffinose의 Km 값은 각각 0.85mM 및 0.6mM이었다.

An invertase (EC 3.2, 1.26) was extracted from Korean giseng (Panax ginseng C.A.Meyer) with distilled water. The ginseng invetase was purified about 62.6 folds purified by procedures including ammonium sulfate fractionation, DEAE-cellulofine chromatogaphy and gel-filtrations through Sephadex G-75 and the recovery of enzyme activity was 11.1%. The homogeneity of the purified enzyme was proved by polyacrylamide gel disc electrophoresis. The purified enzyme was divided into two different subunits by treating with a mixture of SDS and 2-mercaptoethanol, and the molecular weight of the large subunit was estimated to be 116,000 and that of the small one to be 14,000. The optimal pH and temperature of the enzyme were pH 6 and 45℃, 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.