Abstract
The isolation and purification of polyphenol oxidase from purple eggplant ( Solanum melongena L.) is described. A 15-fold purified preparation has been obtained with 15% yield by a procedure involving (NH 4) 2SO 4 precipitation, DEAE cellulose chromatography and Sephadex G 100 gel filtration. The enzyme has an optimum pH of 6·4 and a molecular weight of 79 000 ± 5000. Inhibition studies with sodium diethyl dithiocarbamate and potassium cyanide and dialysis against the latter show that the enzyme requires copper. Eggplant polyphenol oxidase exhibits only a catecholase activity and presents a great affinity for catechol and caffeic acid. This latter compound is no doubt its natural substrate. These results show that conversely to tomato, where a polyphenol oxidase activity was tightly bound to the peroxidase, in the case of eggplant there is a true polyphenol oxidase enzyme.
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