Lignin perixodase from culture filtrate of a new lignolytic fungal strain Hexagona tenuis MTCC-1119 has been purified to homogeneity using a simple procedure. The molecular wt of the enzyme has been found to be 48 kDa using SDS-PAGE analysis. The enzymatic characteristics like Km, pII and temperature optima of the enzyme using veratryl alcohol. n-propanol and H2O2 as substrate has been determined. The Km values have been found to be 70 mu M, 80 mu M and 530 mu M for veratryl alcohol, H2O2 and n-propanol respectively. The pH and temperature optima were 3 and 30 degrees C respectively. The enzyme retains 50% of its activity in 10% of the water miscible organic solvents acetone, dioxane, diethyl ether, acetonitrile and dimethyl formamide in aqueous medium. The inhibition of the enzyme by acetone has been found to be reversible and uncompetitive with inhibition constant K-1 values 2 72 mM 2 96 mM and 0 34 mM using veratryl alcohol, hydrogen peroxide and n-propanol as the substrates respectively.
