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The anticancer activity of ginseng originated mainly from lipid-soluble components. The hexane extract of ginseng marc (HEGM) showed a potent inhibitory activity on human hepatoma (HepG2, GI 50 = 41.7 lg/ml) and breast (MCF-7, GI 50 = 54.4 lg/ml) cancer cell proliferation in vitro in a concentration-dependent manner as did the hexane extract of ginseng (HEG), with GI 50 values of 21.1 lg/ml in HepG2 and 41.2 lg/ml in MCF-7. The water extract of ginseng (WEG) possessed a low anticancer activity against both cancer cell lines, but the hexanesoluble fraction of WEG (HSF/WEG) showed a potent anticancer activity against HepG2 (GI 50 = 38.7 lg/ml) and MCF-7 cells (GI 50 = 51.1 lg/ml). The hexane extraction in ginseng was a very promising protocol for the maximum recovery of the anticancer active components in high concentrations. Also the adoption of hexane extraction after water extraction of ginseng was successful in the effective utilization of the residual lipid-soluble anticancer active components in ginseng marc.

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Immobilization of a protease, Flavourzyme, by covalent binding on various carriers was investigated. Lewatit R258-K, activated with glutaraldehyde, was selected among the tested carriers, because of the highest immobilized enzyme activity. The optimization of activation and immobilization conditions was performed to obtain high recovery yield. The activity recovery decreased with increasing carrier loading over an optimal value, indicating the inactivation of enzymes by their reaction with uncoupled aldehyde groups of carriers. The buffer concentrations for carrier activation and enzyme immobilization were optimally selected as 500 and 50 mM, respectively. With increasing enzyme loading, the immobilized enzyme activity increased, but activity recovery decreased. Immobilization with a highly concentrated enzyme solution was advantageous for both the immobilized enzyme activity and activity recovery. Consequently, the optimum enzyme and carrier loadings for the immobilization of Flavourzyme were determined as 1.8 mg enzyme/mL and 0.6 g resin/mL, respectively.

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