Polyphenol oxidase (PPO) was extracted from the cuttlefish ink with pH 7.2 sodium phosphate extraction buffer. The crude enzyme extract was fractionated with solid ammonium sulfate of 30%-80% saturation. After dialysis, the enzyme solution was purified by DEAE Sepharose CL 6B column chromatography and Sephadex G 150 column chromatography respectively. A 10.78 fold purification of PPO was obtained. The result from polyacrylamide gel electrophoresis of purified enzyme indicated that only one band was found using silver stain and PPO activity stain, respectively.