Characterization of Lignin Peroxidase from Cryptococcus neoformans for Bioremediation of Pulp and Paper Mill Effluent

Abstract

Eight fungal strains (F1–F8) isolate from the sediment core and degraded wood of the Pulp and Paper Mill effluent and Phanerochaete chrysosporium are tested for different cellulolytic (CMcase, FPase, Xylanases) and lignolytic (lignin peroxidase) enzyme activity in pulp. F-3 (Cryptococcus neoformans) strain shows higher enzyme activity compare to other fungi isolated from effluent. Weight loss, cellulose loss, and organic carbon contents are found maximum in F-3 (C. neoformans) strain. Reducing sugar, protein content, and color removing potential are also higher in C. neoformans. The culture extract of F-3 strain grows in presence of pulp fractionated into five protein fractions has indicated two fractions of molecular weight, 38,000 and 40,000 Da, having lignin peroxidase activity. Lignin peroxidase has optimum activity at pH 2–3 and temperature 20–30 °C, maximum activity at 6–48 mM veratryl alcohol concentration and 256 mM H2O2, however, sodium azide inhibits the enzyme activity. Different metals (CoCl2, HgSO4, CaCl2, SnCl2, FeSO4, CuSO4, and ZnSO4) also affect the lignin peroxidase activity. Characterization study is performed for significant analysis.