Abstract A basic heme-peroxidase (WsP) was purified to homogeneity from wheat (Triticum aestivum) seed by consecutive treatments consisting of ammonium sulfate fractionation，ion exchange chromatograph On FPLC-Source30s and gel filtration chromatograph on FPLC-Superdex G75。The specific activity of purified peroxidase was 3912 U／mg，The protein was exhibited a molecular mass of 37kDa.．Spectral analysis of the enzyme revealed the presence of the Soret band with a max at 399 nm。 The most adaptive pH and optimum temperature of peroxidase was pH5.0 at and 40℃。 The best oxidation concentration of H2O2 for peroxidase was 14 mM/L。
