Abstract
A novel manganese peroxidase (MnP) was isolated from an indigenous fungal species Schizophyllum commune strain IBL-06 that was grown in pre-optimized solid state culture using banana stalk as substrate. The MnP was purified by (NH4)(2)SO4 fractionation, dialysis and Sephadex G-100 gel filtration chromatography to achieve 1.8 fold purification with 22% enzyme yield and 506 U/mg specific activity. A homogenous single band of 40 kDa for purified MnP was obtained after gel documentation of Native-PAGE that was further confirmed on SDS-PAGE. Characterization of MnP revealed that the pH and temperature optima of S. commune IBL-06 MnP were 5 and 40 degrees C, respectively. S. commune MnP showed high substrate (MnSO4) affinity and catalytic efficiency with corresponding kinetic constants K-m and V-max values of 0.4 mM and 410 mM/min, respectively. The purified enzyme was activated by CuSO4 and MnSO4 and inhibited by CaCl2, EDTA, TEMED, beta-Marcaptoethanol, AgNO3 and Pb(NO3)(2) (most inhibitory). (C) 2013 Friends Science Publishers