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Abstract
Polyphenoloxidase was isolated from tea leaf, Camellia sinensis (L.) O. Kuntze grown in Turkey and its biochemical characteristics were studied. Polyphenoloxidase was extracted and partially purified by ion-exchange chromatography on a column packed with diethyaminoethyl cellulose. The optimum temperature and pH of polyphenoloxidase were found to be 30oC and 6.0, respectively. Heat stability of tea leaf polyphenoloxidase decreased as the temperatures increased from 30 to 80oC. Tea leaf polyphenoloxidase contained several phenolic compounds as substrate and sensitive to inhibitors such as ascorbic acid, cysteine, oxalic acid, and citric acid.
ACKNOWLEDGMENT
The author would like to thank Professor Dr. Leif H. Skibsted for supplying laboratory facilities for this study.