• Journal of the Korean Society of Food Science and Nutrition
• /
• v.30 no.5
• /
• pp.844-847
• /
• 2001

Factors affecting thermostability of polyphenol oxidase (PPO) from potato were studied for the purpose of providing useful information for food processing operations. The enzyme was most stable at pH 7.0 and it was inhibited to 70% after heat treatment at 8$0^{\circ}C$ for 1 min. The z-value for the thermal inactivation of the PPO was 12.17$\pm$0.58$^{\circ}C$. The thermostability of the enzyme was reduced by addition of sodium chloride. And the activity was inhibited by addition of reducing reagents such as 2-mercaptoethanol and dithiothreitol.