Properties of Polyphenol Oxidase from Prunus salicina (Red)

Polyphenol oxidase in Prunus salicina(Red) was extracted, some properties and its partially purification were investigated as follows; Polyphenol oxidase was purified about 15 folds after ammonium sulfate saturation and about 64 folds after Sephadex G-100 column chromatography. Polyphenol oxidase showed optimum pH for activity at 6.5 and optimum temperature at at and high affinity to catechol in o-diphenol compounds. Thermal stability were about 85% and 75% of initial polyphenol oxidase activity remained after heating at for 5 minutes and 30 minutes respectively. The Michaelis constant of the enzyme was 2.58mM. L-cysteine, glutathione, ascorbic acid and potassium cyanide appeared to be most effective inhibitors. EDTA showed a slight inhibition.