Tea Leaf Polyphenol Oxidase (Part 1):Solubilization and Properties of the Structurally Bound Polyphenol Oxidase in Tea Leaves

概要

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A large part of the polyphenol oxidase was solubilized from tea leaf homogenate by addition of Tween-80. After filtration of the solubilized polyphenol oxidase fraction through a Sephadex G-25 column and the fractionation of the filtrate with ammonium sulfate, the specific activity of the solubilized enzyme increased about 4 to 5 times as much as that of tea leaf homogenate. Optimum pH of the solubilized enzyme was 5.5, and was almost the same as that of water insoluble enzyme in the acetone powder. The minimum concentration required for the maximum activity were about 5×10-3M, 4.3×10-3M, and 3×10-3M for (+)-catechin (-)-epigallocatechin and (-)-epigallocatechin gallate, respectively. (+)-catechin showed the highest activity among them. The enzyme activity was inhibited by potassium cyanide and sodium diethyldithiocarbamate.
日本茶業技術協会の論文