Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase

Phytase is added to animal feeds to improve phosphorus absorption and reduce phosphorus excretion of swine and poultry. It hydrolyses phytate, which is a major form of storage of cereal grains and legumes in commercial animal feeds, into myo-inositol and inorganic phosphate. Adequate thermostabil...

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Main Authors:	Ibrahim Ali , Noorbatcha, Sultan, A. M., Amid, Azura, Hamzah, Mohd. Salleh
Format:	Article
Language:	English
Published:	INSI Publications 2012
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/17995/ http://irep.iium.edu.my/17995/ http://irep.iium.edu.my/17995/1/B_Amyl_Phyt_AJBAS_2012_Jan_6_109-116.pdf

id	iium-17995
recordtype	eprints
spelling	iium-179952016-12-15T07:39:45Z http://irep.iium.edu.my/17995/ Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase Ibrahim Ali , Noorbatcha Sultan, A. M. Amid, Azura Hamzah, Mohd. Salleh TP248.13 Biotechnology Phytase is added to animal feeds to improve phosphorus absorption and reduce phosphorus excretion of swine and poultry. It hydrolyses phytate, which is a major form of storage of cereal grains and legumes in commercial animal feeds, into myo-inositol and inorganic phosphate. Adequate thermostability of phytase is necessary for field application as diets for swine and poultry are normally pelleted at high temperatures (60-80°C). In this study, Molecular Dynamics simulation (MD) was used to study the effect of calcium metal ions on the thermostability of Bacillus amyloliquefacience phytase. MD simulations of the enzyme in the calcium-loaded and calcium-free states were performed at 60°C (333 K) and 80°C (353 K) in water as the solvent medium, for duration of 4 ns. Root mean square deviations (RMSD) of calcium-bound residues, backbone atoms, and other secondary structures were found to be lower in the presence of calcium ions at both temperatures. In addition, calcium-loaded enzyme was found to have fewer numbers of hydrogen bonds and salt bridges at both temperatures, yet calcium-loaded enzyme remains more thermostable due to network of electrostatic interactions induced by calcium binding. The binding effect of calcium ions becomes weaker at 80°C and the small increase of binding effect offered by the calcium ions at higher temperatures in not sufficient enough to maintain the activity at this temperature. It is proposed that suitable mutations at the coil region would lead to increase in the stability of the enzyme at high temperatures. Key words: Bacillus amyloliquefaciens phytase, Molecular Dynamics simulation, calcium ions, thermostability, RMSD, hydrogen bonds, salt bridges. INSI Publications 2012-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/17995/1/B_Amyl_Phyt_AJBAS_2012_Jan_6_109-116.pdf Ibrahim Ali , Noorbatcha and Sultan, A. M. and Amid, Azura and Hamzah, Mohd. Salleh (2012) Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase. Australian Journal of Basic and Applied Sciences, 6 (1). pp. 109-116. ISSN 1991-8178 http://www.insipub.com/ajbas/2012/January/109-116.pdf
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 Sultan, A. M. Amid, Azura Hamzah, Mohd. Salleh Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase
description	Phytase is added to animal feeds to improve phosphorus absorption and reduce phosphorus excretion of swine and poultry. It hydrolyses phytate, which is a major form of storage of cereal grains and legumes in commercial animal feeds, into myo-inositol and inorganic phosphate. Adequate thermostability of phytase is necessary for field application as diets for swine and poultry are normally pelleted at high temperatures (60-80°C). In this study, Molecular Dynamics simulation (MD) was used to study the effect of calcium metal ions on the thermostability of Bacillus amyloliquefacience phytase. MD simulations of the enzyme in the calcium-loaded and calcium-free states were performed at 60°C (333 K) and 80°C (353 K) in water as the solvent medium, for duration of 4 ns. Root mean square deviations (RMSD) of calcium-bound residues, backbone atoms, and other secondary structures were found to be lower in the presence of calcium ions at both temperatures. In addition, calcium-loaded enzyme was found to have fewer numbers of hydrogen bonds and salt bridges at both temperatures, yet calcium-loaded enzyme remains more thermostable due to network of electrostatic interactions induced by calcium binding. The binding effect of calcium ions becomes weaker at 80°C and the small increase of binding effect offered by the calcium ions at higher temperatures in not sufficient enough to maintain the activity at this temperature. It is proposed that suitable mutations at the coil region would lead to increase in the stability of the enzyme at high temperatures. Key words: Bacillus amyloliquefaciens phytase, Molecular Dynamics simulation, calcium ions, thermostability, RMSD, hydrogen bonds, salt bridges.
format	Article
author	Ibrahim Ali , Noorbatcha Sultan, A. M. Amid, Azura Hamzah, Mohd. Salleh
author_facet	Ibrahim Ali , Noorbatcha Sultan, A. M. Amid, Azura Hamzah, Mohd. Salleh
author_sort	Ibrahim Ali , Noorbatcha
title	Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase
title_short	Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase
title_full	Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase
title_fullStr	Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase
title_full_unstemmed	Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase
title_sort	molecular dynamics study of the effect of calcium ions on the thermostability of bacillus amyloliquefaciens phytase
publisher	INSI Publications
publishDate	2012
url	http://irep.iium.edu.my/17995/ http://irep.iium.edu.my/17995/ http://irep.iium.edu.my/17995/1/B_Amyl_Phyt_AJBAS_2012_Jan_6_109-116.pdf
first_indexed	2023-09-18T20:27:02Z
last_indexed	2023-09-18T20:27:02Z
_version_	1777408485276778496

Molecular dynamics study of the effect of calcium ions on the thermostability of Bacillus Amyloliquefaciens Phytase

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