Crude enzyme of polyphenol oxidase was obtained from garlic. This enzyme actively oxidized triphenols such as pyrogallol and gallic acid, although it showed very weak activity on diphenols such as catechol and chlorogenic acid among the phenolic compounds tested. The optimum pH of the enzyme was 6.5 which was slightly higher than that of the garlic itself (pH 6.0). The enzyme was stable relatively at heat treatment. Sodium metabisulfite inhibited the enzyme activity at the concentration of 1mM, and KCN, L-ascorbic acid and thiourea also inhibited the enzyme action. Mg^(++) activated the enzyme activity. Cu^(++) activated slightly the enzyme action at low concentration (1mM), but inhibited at high concentration (10mM).