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Abstract ▼ AI-Helper

The present work was undertaken to investigated the purification and characterization of polyphenol oxidase (PPO ; EC 1.10.3.1) in sweet potato, particularly the number of PPO isozymes, and PPO properties such as pH optimum, heat stability, substrate specificity, kinetics, and inhibitor studies. The...

The present work was undertaken to investigated the purification and characterization of polyphenol oxidase (PPO ; EC 1.10.3.1) in sweet potato, particularly the number of PPO isozymes, and PPO properties such as pH optimum, heat stability, substrate specificity, kinetics, and inhibitor studies. The purification achieved was 23.1 fold from crude extract with a yield of 41.5%. Eight PPO isozymes and twelve PPO isozymes were detected by disc polyacrylamide gel electrophoresis and isoelectric focusing, respectively. The specific activity of each isozyme separated by isoelectric focusing was in the range of $6,000{\sim}46,700U/mg$. This enzyme was sweet below $65^{\circ}C$ and the pH optimum of PPO occurred at 6.0-6.5. The substrate specificity of sweet potato PPO showed the high affinity toward the odiphenolic compounds. Km and Vmax for catechol were found to be 6.7 mM and $20{\triangle}A/min$, me protein, respectively. Inhibitor studies indicated that dithiothreitol was the most potent among the inhibitors used in the present work.