Comparison of lignocellulosic enzymes between Ascomycetes (Trichoderma) and basidiomycetes (Ganoderma) species using proteomic approaches

Abstract Wood decomposing ascomycetes and basidiomycetes group of fungi are the most valuable microbes on the earth’s ecosystem that recycle the source of carbon and are also essential for the biorefinery industries. To understand the robustness of the enzymes and their metabolic pathways of both groups of fungi, we performed label-free quantification of the total proteins of four fungal species. The study suggests two groups, i.e. ascomycetes (Trichoderma citrinoviride and Thermoascus aurantiacus) and basidiomycetes (Ganoderma lucidum MDU-7 and G. lucidum) possess diverse repository of enzymes. These fungi show a comparable quantity of protein abundance [T. citrinoviride (285), T. aurantiacus (206), G. lucidum MDU-7 (102), G. lucidum (242)]. The differentially regulated proteins of ascomycetes and basidiomycetes analyzed through heat map shows upregulated and downregulated proteins [25 differentially expressed proteins in T. citrinoviride (8.62 % up-regulated and 91.37 % down-regulated) and G. lucidum (5.74 % up-regulated and 94.25 % down-regulated)] by using the normalized PSMs and log2fold change. The identified proteins were similarly matched to the CAZymes family-like glycoside hydrolase (GH family), carbohydrate-binding module (CBM family) with auxiliary activities and also involve in the hydrolysis of carbohydrate, lignin, xylan, polysaccharides, peptides, and oxidoreductase activity that helps in antioxidant defence mechanism. The results of lignocellulolytic enzymes (laccases, cellulases, xylanases) from two different divisions of fungi and their proteomics study gives a better understanding of the uses of enzyme cocktails in carbon recycling and other biorefinery processes.