• KSBB Journal
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• v.13 no.1
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• pp.1-5
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• 1998

A $\beta$-fructofuranosidase of garlic (Allium sativum L. ; Seosan) was purified by ammonium sulfate fractionation and gel filtration chromatography with a recovery of 8.3%. The molecular mass of the purified enzyme was estimated to be 79kDa by SDS-PAGE, which revealed two subunits of 41kDa and 38kDa. Maximum enzyme activity was observed at pH 5.0 and 40$^\circ C$ and the enzyme was stable over the pH range of 4.0-6.0 and below 50$^\circ C$. The Km value for sucrose was 15.5mM and the enzyme activity was significantly inhibited by bivalent metal ions(Hg$^2+$, Cu$^2+$, Cd$^2+$) and EDTA.