Structural insight into the fungal β-glucosidases and their interactions with organics

Abstract Fungal β-glucosidases (BGLs) have unceasingly utilized for industrial applications and recently, they possess a crucial role in bioethanol production. To engineer the BGLs, understanding their structures, intermolecular interactions and molecular docking is requisite, which is carried out in this work based on the glycosyl hydrolase (GH) family. Among 12 BGLs, protein sequence, structure, and conserved sites of GH1 BGLs are evidently diverged to GH3 BGLs. Even biophysical and chemical features of GH1 BGLs are utterly varied from GH3 BGLs, wherein pI, instability index, aliphatic index, surface & buried area, thermostability and thermodynamics are included. On the contrary, aromatic, charged, polar, and hydrophobic residues are significantly higher in GH1 BGLs as compared to that of GH3 BGLs. Moreover, molecular docking of BGLs with 12 substrates and 5 inhibitors revealed that the GH3 BGLs efficiently bound with laminaribose, gentibiose, aryl- and cello-substrates than GH1 BGLs; however, GH3 BGLs are noticeably inhibited by glucose, glucono-δ-lactone, methanetriamine. So, structural insight of BGLs provides an explicit knowledge regarding the catalytic residues, biophysical chemistry and notable binding ligands, which are most important factors for enzyme engineering.