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Various aspects of fungus-originated 0-apiosidase were studied. The production of the enzyme on various carbon sources by fungi appeared to be inducible as it was only produced when apiin, an apiosylglucoside, was present in the culture medium. The influence of apiin concentration, nitrogen source, and surfactants on enzyme production was studied. The enzyme was partially purified by filtration chromatography on Ultrogel AcA44 and ion-exchange chromatography on DEAE-Sepharose CLGB. The molecular weight of this enzyme was 38 OOO; K , and V,, values for p-nitrophenyl O-Dapiofuranoside were, respectively, 16 mM and 0.192 nkat/mg of protein. With regard to activity, the optimum p H and temperature were, respectively, 5.6 and 50 "C. The optimum p H of stability was 7. Na+, Mgz+, MnZ+, Cu+, Cu2+ have an inhibitor effect on 0-apiosidase activity. Conversely, the enzyme was inhibited neither by glucose nor by ethanol. The effect of 0-apiosidase toward apiosylglucosides of terpenols, grape flavor precursors, was tested.

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