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Docking Study of β-glucosidase B (BglB) from P. Polymyxca with Cellobiose and Cellotetrose

Nur Shima Fadhilah Mazlan1 and Nurul Bahiyah Ahmad Khairudin2
1.Malaysia-Japan International Institute of Technology
2.Universiti Teknologi Malaysia Kuala Lumpur, Malaysia
Abstract—Beta-glucosidase ( 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.

Index Terms—beta-glucosidase, binding site, molecular docking, cellobiose, protein ligand interaction

Cite: Nur Shima Fadhilah Mazlan and Nurul Bahiyah Ahmad Khairudin, "Docking Study of β-glucosidase B (BglB) from P. Polymyxca with Cellobiose and Cellotetrose," Journal of Medical and Bioengineering, Vol. 3, No. 2, pp. 78-83, June 2014. Doi: 10.12720/jomb.3.2.78-83
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