摘要:Polyphenol oxidase (PPO) from white cherry fruit (Starks Gold) was extracted and purified through (NH4)2SO4 precipitation, dialysis and ion exchange chromatography. The enzyme showed two peaks with PPO activity on toyopearl 650 m column, which were denoted as isoenzyme a and isoenzyme b. A 3.9 fold purification of isoenzyme a with a recovery of 34.9 % and 76.7 fold purification of isoenzyme b with a recovery of 54.3 % were achieved. Ph optima of isoenzyme a and b were 4.5 and 4.98, respectively. The temperature optima for enzyme activity were found to be 20°C for isoenzyme a and 30°C for isoenzyme b. The affinity of isoenzyme b for catechol as substrate was higher than that of isoenzyme a. Activation energies and z values were found to be 22.1°C (r2= 0.883) and 98.5 kj/mol (r2= 0.878) for isoenzyme a and 13.9°C (r2= 0.990) and 157.1 kj/mol (r2= 0.989) for isoenzyme b, respectively. Inhibitory effect of l-cysteine and sodium disulphide differed from each other.