A Novel Approach to Delignify Lignocellulosic Materials by Using Ligninolytic Enzyme Consortium

Abstract

Lignin biodegradation is an attractive approach for producing value-added products. These valuable products are produced by the processing and refining of lignocellulosic residues. A set of ligninolytic enzymes including lignin peroxidase (LiP), manganese-dependent peroxidase (MnP), and laccase (Lac) were individually produced from Ganoderma lucidum, Trametes versicolor, and Pleurotus ostreatus. Solid state fermentation under pre-optimized culture conditions with varying ratios of enzymes were used for the delignification of lignocellulosic biomass residues. The fungal enzymes were purified in four steps including ammonium sulfate precipitation, dialysis, ion exchange chromatography, and gel filtration chromatography. The purified enzymes were subsequently used in varying ratios (with each containing 200 U/mL) for the delignification of wheat straw, sugarcane bagasse, and rice straw. The consortium of enzymes caused the removal of 58.5%, 46%, and 52% of the lignin from the wheat straw, sugarcane bagasse, and rice straw, respectively, at LiP: MnP: Lac ratios of 1:2:2, 1:1:2, and 2:1:2. The best delignification was observed in wheat straw (58.5%), exposing 76.54% cellulose content. The results suggested that the ligninolytic enzymes are effective catalysts for the selective partial delignification of lignocellulosic biomass residues. After delignification these lignocellulosic residues could be utilized as cost-effective substrates for the production of enzymes, biofuels, and other industrially significant products.

Keywords

• Ligninolytic enzymes
• Delignification
• Enzyme Consortium
• Lignocellulosic substrates