Purification and characterization of polyphenol oxidase in redhaven peaches

Abstract

Polyphenol oxidase from Redhaven peaches ( Prunus persica BATSCH) was purified by column chromatography on, Phenyl Sepharose, ECTEOLA Cellulose, Hydroxylapatite, and benzoylated DEAF Sephadex. The partially purified enzyme showed two major bands on, disc gel electrophoresis when stained for polyphenol oxidase activities, proteins, glycoproteins, and lipoproteins. Thin layer isoelectric focusing data indicated a pI between p H 4.5 and 5.5. The purified enzyme was stable for two months in buffered 20 % sucrose, glycerol, or ethylene glycol solutions at −15°C. Digestion of the enzyme with carbohydrases and proteases generated new isoenzymic forms of the enzyme.