Effects of hydrogen peroxide$(H_2O_2)$ on polyphenol oxidase (PPO) in Perillae Folium were investigated. The inactivation of this enzyme was dependent on $H_2O_2$ concentration. and the initial lag period was not shown. Preincubation of Perillae Folium PPO with $H_2O_2$ in the absence of a substrate resulted in rapid loss of enzymatic activity. The inactivation of PPO by $H_2O_2$ dependents temperature and pH. OH radical scavengers such as mannitol and sodium formate did not protect the enzyme against inactivation by $H_2O_2$. Substrate analogue such as phenylalanine protected the enzyme against inactivation by $H_2O_2$. and copper chelator such as sodium azide also protected the enzyme.