Soluble peroxidase in pericarp of litchi (Litchi chinensis sonn. Cv. Heiye) fruit was extracted by phosphate buffer and purified by ammonium sulfate precipitation, ion exchange chromatography using DEAE Sephadex A-50 column, and gel filtration using Sephadex G-100 column. The specific activity of the purified enzyme increased 65.70 fold over the crude extract with 45.66% recovery. The effects of pH and temperature on activity of peroxidase(POD) were assayed. The K_m for H₂O₂ and 4-methylcatechol were determined by Lineweaver-Burk plots. Several compounds including phonelic compounds were used as the substrates of the enzyme for specificity study. The effects of various inhibitors on this peroxidsae were also assayed.