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Lignin peroxidase was produced from Schyzophyllum commune IBL-06 through solid state fermentation of an abundantly available agro-industrial waste, banana stalk, under pre-optimized conditions. LiP was fractionated by 65% saturation with NH4SO4 and dialysis to 1.5-fold purification. The enzyme was further purified by Sephadex G-100 gel filtration chromatography to 2.34 fold with specific activity of 468 U/mg. A single band of 80 kDa was obtained on native gel while on sodium dodecyl sulphate polyacrilamide gel electrophoresis (SDS-PAGE), and two bands having molecular weight of 33 & 47 kDa were obtained, suggesting that LiP was a two polypeptide oligomeric protein. The present LiP from S. commune IBL-06 was optimally active at pH 5 and 35°C. The stability assay showed that LiP retained activity in an acidic pH range of 4 to 6 and a temperature of 25 to 45°C after 24 h of incubation. Lignin peroxidase oxidized the vertry alcohol and showed kinetic constants KM and Vmax values of 0.46 mM and 388 mM/min, respectively. All organic and inorganic compounds inhibited S. commune LiP, but EDTA, β-Marcaptoethanol, and Pb(NO3)2 were the most inhibitory.