Purification of latent phenolase from broad-bean (Vicia faba) leaves

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Abstract
Latent phenolase from broad-bean leaves may be removed from pigments and the major protein components of the leaf juice in one operation by gradient elution from a column of diethylaminoethylcellulose. Rechromatography of the enzyme on the same adsorbent yields a preparation of high catecholase activity in 90% overall yield. Unlike other known active phenolases the enzyme released from a broad-bean leaf extract by Teepol is adsorbed strongly on diethylaminoethylcellulose.