ISSN: 0973-7510

E-ISSN: 2581-690X

Ibrahim Ali Noorbatcha , Ahmad Sidqi Harithuddin and Hamzah Mohd Salleh
BioProcess and Molecular Engineering Research Unit (BPMERU), Department of Biotechnology Engineering, Kuliyyah of Engineering, International Islamic University Malaysia, P.O Box 10, 50728, Kuala Lumpur, Malaysia.
J Pure Appl Microbiol. 2014;8(Spl. Edn. 1):859-863
© The Author(s). 2014
Received: 08/01/2014 | Accepted: 24/03/2014 | Published: 31/05/2014

Currently, most of the demand for energy relies on petroleum products. Nevertheless, the issues of energy security, economics and environment has led to the breakthrough of biofuel cells (BFCs) technology as one of the promising solution to the problems. However, the performance of BFCs need to be improved in order to compete with the existing technologies. One way to improve the efficiency of BFCs is to ensure that the enzyme used as the catalyst in BFCs, in this case, pyranose 2-oxidase (P2Ox) has better binding characteristic and more reactive. For this purpose, studies on three-dimensional (3-D) structure of P2Ox enzyme can offer insights on the structure-function correlations. Unfortunately, at present there is no available crystal structure of P2Ox from Phanerochaete chrysosporium (PcP2Ox). Thus, in this study homology modelling was used as the reliable alternative method to predict the 3-D structure of PcP2Ox enzyme and thus provide necessary information to improve the efficiency of the enzyme.


Homology modelling, Pyranose-2-oxidase, Phanerochaete chrysosporium

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© The Author(s) 2014. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.