Proteomic Approaches for Ligninolytic Enzymes Production for Enhancing Sugarcane Biomass Conversion Efficiency

Sugarcane is an efficient C4 energy cane. The lignocellulosic biomass is fermented for the production of second-generation biofuel. Lignin, a complex heteropolymer hinders biomass biodegradation in two ways either by acting as a protective cover to polysaccharides against enzymatic depolymerization resulting in biomass recalcitrance or by binding to saccharification enzymes thereby affecting hydrolysis. Hence lignin degradation challenges cost-effective bioethanol production. Delignification enzymes such as lignin peroxidase, manganese peroxidase, and laccase from microbial consortium are currently utilized in bioethanol industries. Microbial enzymes from recombinant microorganisms with optimal physiochemical properties to overcome expensive pre-treatment processes are attempted to increase sugar yields. To harness the maximum breakdown of lignocellulosic biomass, research on engineering novel enzymes through the manipulation of amino acid residues has received more attention to overproduce targeted enzymes for better cocktails. Proteomic approaches are utilized to study the genetics and expression status of microbes at specific conditions for the biodegradation of lignocellulose biomass. Proteomic analysis on the secretome of lignocellulosic biomass-degrading microorganisms and different commercial cocktails on biomass hydrolysis is in progress way in the identification of novel and potential genes to synthesize better formulation of targeted enzyme cocktails for efficient delignification. This chapter summarizes biodegradation of lignin by microorganisms-producing ligninolytic enzymes such as laccases, lignin peroxidase (LiP), manganese peroxidase (MnPs), versatile peroxidase (VP), and dye-decolorizing peroxidase (DyP), identification of new lignin hydrolyzing microbes and on proteomic and transcriptome analysis of lignocellulolytic enzymes for enhanced sugarcane bagasse delignification.