In silico studies of fungal xylanase enzymes: structural and functional insight towards efficient biodegradation of lignocellulosic biomass

Xylanolytic enzyme can successfully and efficiently breakdown xylans to fermentable carbohydrates to create useful chemicals or fuels for use in a range of industrial sectors such as food, animal feed, biofuel, pulp, and paper. In the current investigation, molecular modeling and docking analysis were performed using xylanase enzymes from 17 different fungal species with 5 substrates such as d -xylose, xylobiose, xylotriose, xylotetrose, and xylopentose to identify the active site residues and binding affinity of those complexes. Among all, 4 fungal species such as Aspergillus niger , Orpinomyces sp., Neocallimastix patriciarum , and Botrytis fuckeliana showed the maximum molecular interaction and binding affinity toward different substrate, i.e., − 5.4 ( d -xylose), − 6.7 (xylobiose), − 8.2 (xylotriose), − 8.1 (Xylotetrose), and − 5 (xylopentose) kcal/mol. These four complexes were used for the simulation studies to determine its constancy of the enzyme–substrate complexes. Thus, Botrytis fuckeliana with xylobiose ligand and N. patriciarum with xylotetrose can substantially involve in xylan degradation toward bioethanol production from lignocellulosic biomass.