Abstract
A novel manganese peroxidase of Rhizoctonia sp. SYBC-M3 (R-MnP) was purified by (NH4)2SO4 fractionation, DEAE-cellulose-32 column chromatography, and Sephadex G100 column chromatography. The molecular mass of R-MnP was determined to be approximately 40.4 kDa by SDS-PAGE. The optimum temperature and pH for R-MnP were 55°C and 4.5, respectively. R-MnP was highly stability when the temperature was below 50°C. R-MnP could retain about 60% of its activity when the pH was between 4 and 6.5. However, R-MnP activity was inhibited by Fe3+, Cu2+, and Co3+ as well as increased by Zn2+ and Ca2+. R-MnP demonstrated oxidation of DMP, ABTS, veratryl alcohol, and guaiacol. The K m values of RMnP for H2O2 and Mn2+ were 25.3 and 53.9 μmol/L, respectively.
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