In this study, polyphenol oxidase (PPO) was extracted from Prunus domestica and partially purified by ammonium sulfate precipitation, hydrophobic interaction chromatography, and ion exchange chromatography. The final purification step revealed a 32.81-fold purification, and the molecular mass was estimated to be 65 kDa by SDS-PAGE. The purified PPO showed enzymatic activity mainly toward five substrates, namely catechol, catechin, 4-methyl catechol, chlorogenic acid, and L-3,4-dihydroxyphenylalanine, whereas it showed no activity toward caffeic acid, ferulic acid, p-coumaric acid, p-cresol, and L-tyrosine. The optimum pH and temperature values were 6.0 and 25 degrees C, respectively. The enzyme showed high stability in the pH range of 5.0-7.0 and in the temperature range of 25-65 degrees C. The most effective inhibitors of this enzyme were found to be ascorbic acid and L-cysteine. The thermal inactivation followed a first-order kinetic model, with activation energy of E-a 150.46 +/- 1.29 kJ/mol. PPO extracted from plum showed stability at high pressure, with enzyme activation at 500 MPa. (C) 2017 Elsevier Ltd. All rights reserved.