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ABSTRACT

Stable and highly active polyphenoloxidase (PPO) extracts were obtained using polyvinylpyrrolidone, Amberlite XAD-4, Triton X-100, and protease inhibitor in pH 5.25 buffer. Citrate and phosphate prevented binding of PPO to pectin. Phenyl sepharose chromatography resolved PPO into two isozymes (PPO-F1 and PPO-F2) both separated from pectin. PPO-F1 had a molecular weight of 111,000, did not penetrate the running gel during electrophoresis, and was bound by concanavalin suggesting that it contained carbohydrate. PPO-F2 resolved into two peaks during DEAE-chromatography, had a molecular weight of 34,500, and resolved into two bands during electrophoresis.