PJB-2024-57
PURIFICATION AND IN-DEPTH CHARACTERIZATION OF A LACCASE ENZYME PRODUCED BY CO-CULTURING OF LOCALLY ISOLATED ASPERGILLUS NIGER AND ASPERGILLUS ORYZAE
Asma Zafar
Abstract
Present study aimed to assess the potential of co-culturing of two locally isolated fungal strains, Aspergillus niger and Aspergillus oryzae, for enhanced production of laccase enzyme for possible use in industrial applications. Both strains were investigated individually as well as collectively to produce laccase enzyme after their confirmed identification under optimal conditions. Maximum production of laccase enzyme (35.5±0.025 U/mL) was observed when both strains were co-cultured at 28°C using 10% wheat bran as substrate having pH 6 after 72 hours. The enzyme was purified to homogeneity through ammonium sulfate precipitation and gel filtration chromatography. The molecular mass of purified laccase enzyme from both fungal strains was observed as almost 65 kDa using SDS-PAGE. Purified laccase enzyme showed great stability (60%) upto 70°C for 4 hours and pH 9.0 for 3 hours. The enzyme exhibited stability even in the presence of highest concentrations of solvents and diverse inhibitors. The presence of divalent ions also seemed to enhance the enzymatic activity whereas EDTA showed a negative impact on it. All the characteristics recorded in this research proved laccase enzyme a capable nominee for industrial utilization.
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