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Comparative Study
. 2023 Dec 14;80(1-2):21-32.
doi: 10.1515/znc-2023-0125. Print 2025 Jan 29.

Comparison of lignocellulosic enzymes and CAZymes between ascomycetes (Trichoderma) and basidiomycetes (Ganoderma) species: a proteomic approach

Affiliations
Comparative Study

Comparison of lignocellulosic enzymes and CAZymes between ascomycetes (Trichoderma) and basidiomycetes (Ganoderma) species: a proteomic approach

Akshay Shankar et al. Z Naturforsch C J Biosci. .

Abstract

Wood decomposing ascomycetes and basidiomycetes group of fungi are the most valuable microbes on the earth's ecosystem that recycles the source of carbon; therefore, they are essential for the biorefinery industries. To understand the robustness of the enzymes and their metabolic pathways in the fungal system, label-free quantification of the total proteins was performed. The fungi showed a comparable quantity of protein abundance [Trichoderma citrinoviride (285), Thermoascus aurantiacus (206), Ganoderma lucidum MDU-7 (102), G. lucidum (242)]. Differentially regulated proteins of ascomycetes and basidiomycetes were analyzed, and their heatmap 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 peptide-spectrum match (PSMs) and log2fold change. These proteins were similarly matched to the carbohydrate active enzymes family (CAZymes) like glycoside hydrolase (GH family), carbohydrate-binding module (CBM family) with auxiliary activities, and also involved in the hydrolysis of carbohydrate, lignin, xylan, polysaccharides, peptides, and oxido-reductase activity that helps in antioxidant defense mechanism. The lignocellulolytic enzymes from two different divisions of fungi and proteomics studies gave a better understanding of carbon recycling and multi-product lignocellulosic biorefinery processes.

Keywords: CAZymes; ascomycetes; basidiomycetes; glycoside hydrolase; oxido-reductase; proteomics.

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