Characterization of Rhodanese from Cassava Leaves and Tubers

Rhodanese activity has been established in the leaves, in thepeel, and in the flesh of the tuberous part of Manihot esculentaCrantz. The pattern of distribution of enzyme activity is shownto follow that of the concentration of the cyanogenic glucosideestimated on the basis of HCN released. For the first time,the presence of rhodanese is reported in higher plant tissuesother than the leaves. Identity has been established betweenrhodanese from peel, leaves, and flesh of the cassava plant.The enzyme is inhibited by cyanide in the absence of thiosuiphateor cysteine. Rhodanese is suggested to play a role in the detoxificationof cyanide in cassava.     

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.