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Binding mode study of ß-glucosidase B from P. polymyxca with cellobiose and laminaribiose

Mazlan, Nur Shima Fadhilah and Ahmad Khairudin, Nurul Bahiyah (2013) Binding mode study of ß-glucosidase B from P. polymyxca with cellobiose and laminaribiose. In: International Conference of Computational Chemistry and Biology (ICCCB 2013), 2013.

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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 laminaribiose 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 important residues were reported to be Gln22, Glu167, Tyr298, Glu356, Glu402, and Trp410. These findings may provide valuable insigths in designing beta-glucosidase with higher cellulose-hydrolyzing efficiency.

Item Type:Conference or Workshop Item (Paper)
Subjects:Q Science
Divisions:Malaysia-Japan International Institute of Technology
ID Code:39564
Deposited By: Liza Porijo
Deposited On:30 Jun 2014 16:00
Last Modified:27 Sep 2017 10:32

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