The manganese peroxidase (MnP) was isolated and purified from Schizophyllum sp. F17 on pinewood solid-state cultures. Fractionation of MnP was performed by Sephadex G-75 gel filtration chromatography followed by DEAE-cellulose anion exchange chromatography. This purification attained 3.8% activity yield with a purification factor of 9.2. According to data on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), the molecular weight of the enzyme was 48.7 kDa. The enzyme was a glycoprotein with 18% of its weight in carbohydrates. The optimum pH and temperature of purified MnP for oxidation of DMP were 6.8 and 35 degrees C, respectively. This enzyme was stable in the pH range 4.0-7.0, at 25 degrees C for 1 h incubation period. The effects of possible inhibitors and activators of enzyme activity were investigated. The K-m values of MnP for Mn2+, H2O1, guaiacol, ABTS and DMP were 35.2, 6.7, 13.1, 47.8 and 122.9 mu M at pH 4.5, respectively. The azo dyes such as Congo Red, Orange G and Orange IV were efficiently decolorized using the MnP purified. (c) 2007 Elsevier Inc. All rights reserved.