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KMID : 0370219860300050220
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Yakhak Hoeji
1986 Volume.30 No. 5 p.220 ~ p.227
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Polyphenol Oxidase of Tea Leaf in Korea
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Abstract
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Polyphenol oxidase was purified from an extract of tea leaf by ammonium sulfate fractionation followed by Sephadex G-150 column chromatography, which resulted in a 67-fold increase in specific activity. The enzyme had optimum pH 6. 5 and was relatively heat stable. The substrate specificity of the tea leaf PPO showed high affinity toward pyrogallol and catechol. Potassium cyanide, sodium diethyldithiocarbamate, L-cysteine, 2-mercaptoethanol and ascorbic acid were potent inhibitors.
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