Polyphenoloxidase (PPO) was extracted from Solanum tuberosum Jasim by various chromatographic methods and was subsequently purified and characterized. PPO was purified upto 78-fold from the crude extract. SDS-PAGE profile of the enzyme showed a major subunit of PPO with molecular weight of 40 kDa. The optimum pH and temperature for the maximum activity of PPO was 6.5 and $25^{circ}C$, respectively. The enzyme was found to be quite stable between 10 and $40^{circ}C$, whereas it was almost inactivated at $70^{circ}C$ when incubated for 30 min. Substrate specificity study indicated that catechol was the most suitable substrate for PPO isolated from purple-fleshed potato with a $K_m$ value of 21.1 mM. The most effective inhibitor was ascorbic acid, followed by L-cysteine, citric acid, EDTA, and boric acid. Studies on the effect of metal ion on PPO activity showed that magnesium and copper were inhibitory, while iron and zinc ions increased the activity of PPO.