Docking study of ß-glucosidase B (BglB) from P. polymyxca with cellobiose and cellotetrose

• Main Authors: Mazlan, Nur Shima Fadhilah, Ahmad Khairudin, Nurul Bahiyah
• Format: Conference or Workshop Item
• Published: 2013
• Subjects: QD Chemistry
• Online Access: http://eprints.utm.my/id/eprint/37570/
• Institution: Universiti Teknologi Malaysia

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.