Some Properties of the Polyphenol Oxidase from Potatoes (Solanum tubersum L.) and Inhibiting Effect of the Polyphenol Oxidase by Sulfites

This study was aimed at obtaining elementary data on enzymatic browning of potato and potato products and examining the inhibitory method of browning. Therefore, we extracted polyphenol oxidase from potatoes(Solanum tubersum L.), and investigates its general properties and inhibiting effects of its activity with the different concentrations of sulfites(). The optimum pH and temperature of polyphenol oxidase were observed to be 6.5 and respectively. The polyphenol oxidase at PH5 was very stable, and the activity of polyphenol oxidase between pH was estimated to be relatively high, showing of its activity at pH5. The polyphenol oxidase was very stable when heated at for one hour, and almost 50% of enzyme activity was decreased when heated at for twelve minutes. At 0.1mM concentrating of sulfites the relative activity of polyphenol oxidase was 98% in all the three cases of sulfites. Thus sulfites at 0.1mM concentration was found to have little inhibiting effect on polyphenol oxidase activity. At 1mM concentration of sulfites showed the lowest 36% relative activity among the three. At 5mM concentration of sulfites, the relative activity of was the lowest 14%.