Binding mode study of β-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,...
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| Format: | Article |
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2013
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| author | Azman, M. Md. Nor, Hasanan Hainin, Mohd. Rosli Yaacob, Haryati Ismail, Che Ros Mazlan, Nur Shima Fadhilah Ahmad Khairudin, Nurul Bahiyah |
| author_facet | Azman, M. Md. Nor, Hasanan Hainin, Mohd. Rosli Yaacob, Haryati Ismail, Che Ros Mazlan, Nur Shima Fadhilah Ahmad Khairudin, Nurul Bahiyah |
| author_sort | Azman, M. |
| collection | ePrints |
| description | 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. |
| first_indexed | 2024-03-05T19:23:37Z |
| format | Article |
| id | utm.eprints-47826 |
| institution | Universiti Teknologi Malaysia - ePrints |
| last_indexed | 2024-03-05T19:23:37Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | utm.eprints-478262017-08-14T00:31:03Z http://eprints.utm.my/47826/ Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose Azman, M. Md. Nor, Hasanan Hainin, Mohd. Rosli Yaacob, Haryati Ismail, Che Ros Mazlan, Nur Shima Fadhilah Ahmad Khairudin, Nurul Bahiyah TP Chemical technology 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. 2013-12 Article PeerReviewed Azman, M. and Md. Nor, Hasanan and Hainin, Mohd. Rosli and Yaacob, Haryati and Ismail, Che Ros and Mazlan, Nur Shima Fadhilah and Ahmad Khairudin, Nurul Bahiyah (2013) Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose. International Journal of Chemical Engineering and Applications, 4 (6). pp. 410-414. ISSN 2010-0221 https://www.researchgate.net/publication/272950243_Binding_Mode_Study_of_b-glucosidase_B_from_P_Polymyxca_with_Cellobiose_and_Laminaribiose |
| spellingShingle | TP Chemical technology Azman, M. Md. Nor, Hasanan Hainin, Mohd. Rosli Yaacob, Haryati Ismail, Che Ros Mazlan, Nur Shima Fadhilah Ahmad Khairudin, Nurul Bahiyah Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose |
| title | Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose |
| title_full | Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose |
| title_fullStr | Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose |
| title_full_unstemmed | Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose |
| title_short | Binding mode study of β-glucosidase b from p.Polymyxca with cellobiose and laminaribiose |
| title_sort | binding mode study of β glucosidase b from p polymyxca with cellobiose and laminaribiose |
| topic | TP Chemical technology |
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