General Information
    • ISSN: 2010-0221
    • Frequency: Bimonthly
    • DOI: 10.18178/IJCEA
    • Editor-in-Chief: Prof. Dr. Shen-Ming Chen
    • Executive Editor: Mr. Ron C. Wu
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Editor-in-chief
Prof. Dr. Shen-Ming Chen
National Taipei University of Technology, Taiwan
 

IJCEA 2013 Vol.4(6): 410-414 ISSN: 2010-0221
DOI: 10.7763/IJCEA.2013.V4.336

Binding Mode Study of β-glucosidase B from P. Polymyxca with Cellobiose and Laminaribiose

Nur Shima Fadhilah Mazlan and Nurul Bahiyah Ahmad Khairudin
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.

Index Termsβ-glucosidase, molecular docking, enzymatic hydrolysis

The authors are with the Malaysia-Japan International Institute of Technology, Universiti Teknologi Malaysia Kuala Lumpur, Jalan Semarak, 54100, Wilayah Persekutuan, Malaysia (e-mail: nsfadhilah2@live.utm.my, nurulbahiyah@ic.utm.my).

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Cite: Nur Shima Fadhilah Mazlan and Nurul Bahiyah Ahmad Khairudin, "Binding Mode Study of β-glucosidase B from P. Polymyxca with Cellobiose and Laminaribiose," International Journal of Chemical Engineering and Applications vol. 4, no. 6, pp. 410-414, 2013.

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