• Applied Biological Chemistry
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• v.45 no.4
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• pp.212-217
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• 2002

We purified polyphenols from persimmon leaf and tested their biological activity. The 60% acetone extract was lyophilized and applied to test enzyme inhibition of glucosyltransferase and tyrosinase. GTase was 82.4% inhibited at $1.8{\times}10^{-1}$ mg/ml and tyrosinase 21.7% inhibited at 0.8 mg/ml. The acetone extract was fractionated into F-1, 2, 3, 4, 5 by Sephadex Q-50 gel filtration and the fraction-1 and 2 showed higher enzyme inhibition activity than the other fractions. To the Proteinase K treatment and autoclaving of the two fractions had no effect on the enzyme activity, but these results suggested that active fraction was not protein but phenol ring completed compounds. By Sephadex LH-20, MCI-gel and Bondapak $C_{18}$ column chromatographies, compouds 1, 2, 3 and 4 from F-1 fraction, compounds 5 and 6 from F-2 fraction and compounds 7 , 8 from F-3 fraction were purified and re-crystallized. The purified compounds was assumed to be condensed tannins of frame flavan-3-ol frame on the basis of color reagent reaction and to be a mixture of monomer, dimer and trimer according to TLC analysis.