Docking study of b-glucosidase b (bglb) from p. polymyxca with cellobiose and cellotetrose

Abstract

Beta-glucosidase (3.2.1.21) plays an essential role in the removal of non-reducing terminal glucosyl residues from sacharides and glycosides. Recently, beta-glucosidase has been of interest for biomass conversion that acts in synergy with two other enzymes, endo-glucanase and exo-glucanase. However, there is not much information regarding the molecular interactions of beta-glucosidase with cellobiose. Thus, this study reports on the binding modes between beta-glucosidase from glycoside hydrolase family 1 namely BglB with cellobiose and cellotetrose via molecular docking method. Further analysis on the hydrophobic interactions revealed the key residues involved in forming hydrogen bonds (h-bond) with the substrates. The active residue were identified to be Gln22, Glu167, Glu356, Glu402 and Trp402 .These findings may provide valuable insigths in designing beta-glucosidase with higher cellulose-hydrolyzing efficiency.