Partial Purification and Characterization of Polyphenol Oxidase from Cocoyam, Xanthosoma sagittifolium

Polyphenol oxidase has been partially purified from Xanthosomasagittifolium. The enzyme showed activity towards pyrogallol,DL-ß-3,4-dihydroxyphenylalanine (DOPA) and catechol.Of these three, pyrogallol was the best substrate. The effectsof various compounds as inhibitors of the reaction catalysedby the enzyme were tested. p-Nitrophenol competitively inhibitedthe binding of both catechol and pyrogallol to the enzyme. Inhibitionby the substrate analogue, p-cresol was of the mixed type whilethiourea and diethyldithiocarbamate inhibited the enzyme uncompetitively.The approximate molecular weight of the enzyme determined bygel filtration was 47 000.