title: Molecular docking study of Beta-glucosidase with cellobiose, cellotetraose and cellotetriose.
abstract: Beta-glucosidase (3.2.1.21) plays an essential role in the removal of non-reducing terminal glucosyl residues from glycosides. Recently, beta-glucosidase has been of interest for biomass conversion that acts in synergy with two other enzymes, endoglucanase and exo-glucanase. However, there is not much information available on the catalytic interactions of beta-glucosidase with its substrates. Thus, this study reports on the binding modes between beta-glucosidase from glycoside hydrolase family 1 namely BglB with cellobiose, cellotetraose and cellotetriose via molecular docking simulation. From the results, the binding affinities of BglB-cellobiose, BglB-cellotetraose, and BglB-cellotetriose complexes were reported to be -6.2kJ/mol , -5.68 kJ/mol and -5.63 kJ/mol, respectively. The detail interactions were also been investigated that revealed the key residues involved in forming hydrogen bonds (h-bond) with the substrates. These findings may provide valuable insigths in designing beta-glucosidase with higher cellobiose-hydrolyzing efficiency.
authors.affiliation: Malaysia Japan International Institute of Technology, Universiti Teknologi Malaysia Kuala Lumpur, Malaysia.
authors.forename: Nurul Bahiyah Ahmad
authors.initials: NB
authors.lastname: Khairudin
authors.forename: Nur Shima Fadhilah
authors.initials: NS
authors.lastname: Mazlan
keywords: Beta-glucosidase; binding mode; cellobiose; cellotetraose; cellotetriose; molecular docking