Computational studies on thermal stability of Endoglucanase

Enhancing the functionalities and properties of enzymes via computational prediction is an emerging technology. In order to design new thermostable enzymes, we have employed molecular dynamics (MD) simulation techniques to find out the dynamics factors responsible for the thermal stability of known...

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Main Authors:	Ibrahim Ali , Noorbatcha, Waesoho, Shukree, Hamzah, Mohd. Salleh
Format:	Conference or Workshop Item
Language:	English
Published:	2012
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/28577/ http://irep.iium.edu.my/28577/1/EG_IRIIE2012_poster.pdf

id	iium-28577
recordtype	eprints
spelling	iium-285772013-02-13T11:56:26Z http://irep.iium.edu.my/28577/ Computational studies on thermal stability of Endoglucanase Ibrahim Ali , Noorbatcha Waesoho, Shukree Hamzah, Mohd. Salleh TP248.13 Biotechnology Enhancing the functionalities and properties of enzymes via computational prediction is an emerging technology. In order to design new thermostable enzymes, we have employed molecular dynamics (MD) simulation techniques to find out the dynamics factors responsible for the thermal stability of known endoglucanases (EG). Mesophilic endoglucanases from Fusarium oxysporum (EGFO) and thermophilic endoglucanase from Humicola insolens (EGHI) with known crystal structures and enzyme activity, are used to compare their dynamical behaviors at 40°C and 60°C using MD simulation in aqueous media. It has been found that the Root Mean Square Derivation (RMSD) backbone of EGFO tends to increase more rapidly at higher temperatures, where as the RMSD values for EGHI either remains similar or decreases at higher temperature. The RMSD helices of EGFO also have the behavior similar to that RMSD backbone. The secondary structure conformation at the residues position 225 to 231 of EGFO changes significantly at higher temperature where as conformation of EGFO at these positions is maintained as the temperature is increased. The EGHI shows salt-bridge interactions and hydrophobic interactions in these regions. Hence we propose these two factors are crucial for the thermal stability of endoglucanase. Using this information we have carried out several in silico mutations on EGFO with the objective of designing more thermostable endoglucanase and found that the dynamic behavior of newly designed mutants are consistent with our conclusions. We propose that the new quintuple mutant obtaining by mutating at the positions T224E/G229A/S230F/S231E/N321R is more themostable than EGFO or EGHI. 2012-02-21 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/28577/1/EG_IRIIE2012_poster.pdf Ibrahim Ali , Noorbatcha and Waesoho, Shukree and Hamzah, Mohd. Salleh (2012) Computational studies on thermal stability of Endoglucanase. In: IIUM Research, Invention and Innovation Exhibition IRIIE 2012, 21-22 February 2012, Kuala Lumpur, Malaysia.
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Ibrahim Ali , Noorbatcha Waesoho, Shukree Hamzah, Mohd. Salleh Computational studies on thermal stability of Endoglucanase
description	Enhancing the functionalities and properties of enzymes via computational prediction is an emerging technology. In order to design new thermostable enzymes, we have employed molecular dynamics (MD) simulation techniques to find out the dynamics factors responsible for the thermal stability of known endoglucanases (EG). Mesophilic endoglucanases from Fusarium oxysporum (EGFO) and thermophilic endoglucanase from Humicola insolens (EGHI) with known crystal structures and enzyme activity, are used to compare their dynamical behaviors at 40°C and 60°C using MD simulation in aqueous media. It has been found that the Root Mean Square Derivation (RMSD) backbone of EGFO tends to increase more rapidly at higher temperatures, where as the RMSD values for EGHI either remains similar or decreases at higher temperature. The RMSD helices of EGFO also have the behavior similar to that RMSD backbone. The secondary structure conformation at the residues position 225 to 231 of EGFO changes significantly at higher temperature where as conformation of EGFO at these positions is maintained as the temperature is increased. The EGHI shows salt-bridge interactions and hydrophobic interactions in these regions. Hence we propose these two factors are crucial for the thermal stability of endoglucanase. Using this information we have carried out several in silico mutations on EGFO with the objective of designing more thermostable endoglucanase and found that the dynamic behavior of newly designed mutants are consistent with our conclusions. We propose that the new quintuple mutant obtaining by mutating at the positions T224E/G229A/S230F/S231E/N321R is more themostable than EGFO or EGHI.
format	Conference or Workshop Item
author	Ibrahim Ali , Noorbatcha Waesoho, Shukree Hamzah, Mohd. Salleh
author_facet	Ibrahim Ali , Noorbatcha Waesoho, Shukree Hamzah, Mohd. Salleh
author_sort	Ibrahim Ali , Noorbatcha
title	Computational studies on thermal stability of Endoglucanase
title_short	Computational studies on thermal stability of Endoglucanase
title_full	Computational studies on thermal stability of Endoglucanase
title_fullStr	Computational studies on thermal stability of Endoglucanase
title_full_unstemmed	Computational studies on thermal stability of Endoglucanase
title_sort	computational studies on thermal stability of endoglucanase
publishDate	2012
url	http://irep.iium.edu.my/28577/ http://irep.iium.edu.my/28577/1/EG_IRIIE2012_poster.pdf
first_indexed	2023-09-18T20:42:06Z
last_indexed	2023-09-18T20:42:06Z
_version_	1777409433871056896

Computational studies on thermal stability of Endoglucanase

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