Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium

Currently, most of the demands for energy relied 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...

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Main Authors:	Ibrahim Ali , Noorbatcha, Harithuddin, Ahmad Sidqi, Ramli, Siti Khairani, Othman, Raihan, Mohd. Salleh, Hamzah
Format:	Conference or Workshop Item
Language:	English English
Published:	2013
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/34145/ http://irep.iium.edu.my/34145/3/ICBIOE_2013_Cover_Page_till_Table_of_contents.pdf http://irep.iium.edu.my/34145/9/Homology_P2Ox_-_ICBioE2013_proceedings_pp590-593.pdf

id	iium-34145
recordtype	eprints
spelling	iium-341452014-01-15T01:19:22Z http://irep.iium.edu.my/34145/ Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium Ibrahim Ali , Noorbatcha Harithuddin, Ahmad Sidqi Ramli, Siti Khairani Othman, Raihan Mohd. Salleh, Hamzah TP248.13 Biotechnology Currently, most of the demands for energy relied 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 broad substrate specificity. For this purpose, studies on three-dimensional (3-D) structure of P2Ox enzyme can offer insights on the structurefunction correlations. Unfortunately, at present there is no available crystal structure of P2Ox from P. chrysosporium (PcP2Ox). Thus, in this study homology modelling was used as the reliable alternative method to predict the 3-D structure of PcP2Ox enzyme. The structural information obtained here can provide necessary information to model and design more efficient PcP2Ox. 2013-07-02 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/34145/3/ICBIOE_2013_Cover_Page_till_Table_of_contents.pdf application/pdf en http://irep.iium.edu.my/34145/9/Homology_P2Ox_-_ICBioE2013_proceedings_pp590-593.pdf Ibrahim Ali , Noorbatcha and Harithuddin, Ahmad Sidqi and Ramli, Siti Khairani and Othman, Raihan and Mohd. Salleh, Hamzah (2013) Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium. In: International Conference on Biotechnology Engineering (ICBioE 2013), 2 – 4 Jul 2013, Kuala Lumpur, Malaysia.
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Ibrahim Ali , Noorbatcha Harithuddin, Ahmad Sidqi Ramli, Siti Khairani Othman, Raihan Mohd. Salleh, Hamzah Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium
description	Currently, most of the demands for energy relied 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 broad substrate specificity. For this purpose, studies on three-dimensional (3-D) structure of P2Ox enzyme can offer insights on the structurefunction correlations. Unfortunately, at present there is no available crystal structure of P2Ox from P. chrysosporium (PcP2Ox). Thus, in this study homology modelling was used as the reliable alternative method to predict the 3-D structure of PcP2Ox enzyme. The structural information obtained here can provide necessary information to model and design more efficient PcP2Ox.
format	Conference or Workshop Item
author	Ibrahim Ali , Noorbatcha Harithuddin, Ahmad Sidqi Ramli, Siti Khairani Othman, Raihan Mohd. Salleh, Hamzah
author_facet	Ibrahim Ali , Noorbatcha Harithuddin, Ahmad Sidqi Ramli, Siti Khairani Othman, Raihan Mohd. Salleh, Hamzah
author_sort	Ibrahim Ali , Noorbatcha
title	Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium
title_short	Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium
title_full	Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium
title_fullStr	Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium
title_full_unstemmed	Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium
title_sort	homology modeling of pyranose 2-oxidase from phanerochaete chrysosporium
publishDate	2013
url	http://irep.iium.edu.my/34145/ http://irep.iium.edu.my/34145/3/ICBIOE_2013_Cover_Page_till_Table_of_contents.pdf http://irep.iium.edu.my/34145/9/Homology_P2Ox_-_ICBioE2013_proceedings_pp590-593.pdf
first_indexed	2023-09-18T20:49:16Z
last_indexed	2023-09-18T20:49:16Z
_version_	1777409884127494144

Homology modeling of Pyranose 2-Oxidase from Phanerochaete Chrysosporium

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