Partial purification and characterization of polyphenoloxidase from Turkish tea leaf (Camellia Sinensis L.)

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 30°C and 6.0, respectively. Heat stability of tea leaf polyphenoloxidase decreased as the temperatures increased from 30 to 80°C. Tea leaf polyphenoloxidase contained several phenolic compounds as substrate and sensitive to inhibitors such as ascorbic acid, cysteine, oxalic acid, and citric acid. Copyright © Taylor & Francis Group, LLC.