Binding mode study of ß-glucosidase B from P. polymyxca with cellobiose and laminaribiose
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,...
Saved in:
| Main Authors: | , |
|---|---|
| Format: | Conference or Workshop Item |
| Published: |
2013
|
| Subjects: | |
| Online Access: | http://eprints.utm.my/id/eprint/39564/ |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | 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. |
|---|