Abstract: Peroxidase is closely related to the scavenging of reactive oxygen species (ROS) and the adaptive response to stresses in plants. In order to further explore the role of peroxidase in stress resistance mechanism of crops, POD protein was isolated from leaves of Dongxiang wild rice by extraction, salting out, dialysis and column chromatography, the purified protein was detected by active gel electrophoresis with polyacrylamide gel and the enzymatic characteristics of POD were studied by the guaiacol method. The results showed a component of POD1 isozyme with a specific activity of 568.80 U/mg was obtained about 16.49-fold from leaves of Dongxiang wild rice via extraction with phosphate buffer buffer, precipitation by ammonium sulfate of 40%-80% saturation, and separation by Sephadex G-100 chromatography, which was detected to be a homogeneous component by polyacrylamide gel electrophoresis (PAGE). The detection of enzyme kinetics showed that the POD enzyme had Km of 1.26 mmol/(L?min) and Vmax of 17.51 mmol/(L?min) with the optimum pH of 5.0 and optimum temperature of 35℃-45℃. Cu2+ and Zn2+ had strong activation effects on POD activity, while Fe3+ had inhibition effect, and POD activity was inhibited by 20% of methanol, ethanol and acetone. This study provided foundation for further insights on POD antioxidant function and cold resistance physiology of Dongxiang wild rice.