IN-SILICO ALANINE SCANNING ANALYSIS ON THE CATALYTIC RESIDUES OF A NOVEL Β-GLUCOSIDASE FROM TRICHODERMA ASPERELLUM UC1

Currently, the catalytic residue of highly prolific fungal β-glucosidase (BGL) Trichoderma asperellum UC1 remains unvalidated. The study used alanine scanning method to confirm residues BGL as Glu165, Asp226, and Glu423. This cancels out all intermolecular hydrogen bonds with substrates, lignin, hemicellulose, cellulose. Results revealed an overall decline in stability energy-minimized mutant enzymes' compared wild-type BGL. enzyme registered lower PROCHECK (91.0%), ERRAT (93.09%), Verify-3D (98.92%) values, comparison 90.2%, 92.09%, 98.06%, BGL, respectively. UC1-substrate complexes were less stable than enzyme, which exhibited higher binding energies for docked lignin (−7.4% kcal mol-1), cellulose (−7.2 hemicellulose mol-1). Binding corresponding substrates at −7.9 mol-1, −8.1 −7.8 mol-1. An interesting observation was that changed substrate preference order based on calculated energies. bound preferentially lignin>cellulose=hemicellulose, while selective cellulose>lignin>hemicellulose. Hence, findings convey high likelihood Asp 256, Glu423 are T. UC1.