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 thermostabili...

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Main Authors:	Noorbatcha, Ibrahim Ali, Sultan, A. M., Amid, Azura, Mohd. Salleh, Hamzah
Format:	Conference or Workshop Item
Language:	English
Published:	2011
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/3974/ http://irep.iium.edu.my/3974/ http://irep.iium.edu.my/3974/1/MD_Study_of_the_Effect_of_Ca_ions_on_the_Thermostability_of_B_amyloliquefaciens_Phytase_pg299-301.pdf

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recordtype	eprints
spelling	iium-39742011-11-16T02:17:47Z http://irep.iium.edu.my/3974/ Molecular dynamics study of the effect of Calcium Ions on the thermostability of Bacillus amyloliquefaciens Phytase Noorbatcha, Ibrahim Ali Sultan, A. M. Amid, Azura Mohd. Salleh, Hamzah 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 with and without calcium ions were performed at 60°C and 80°C in water as the solvent medium, for duration of 2 ns. Root mean square deviations(RMSD) of backbone atoms are found to be lower in the presence of calcium ions at both the temperatures. In addition, RMSD values for individual residues of phytase at both calcium states and temperatures revealed that all residues that showed high RMSD values are located in turns or coils at the outer surface of the enzyme. As a result, these residues are the most susceptible to heating, hence produce high fluctuations. 2011-05-17 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/3974/1/MD_Study_of_the_Effect_of_Ca_ions_on_the_Thermostability_of_B_amyloliquefaciens_Phytase_pg299-301.pdf Noorbatcha, Ibrahim Ali and Sultan, A. M. and Amid, Azura and Mohd. Salleh, Hamzah (2011) Molecular dynamics study of the effect of Calcium Ions on the thermostability of Bacillus amyloliquefaciens Phytase. In: International Conference on Biotechnology Engineering, ICBioE’11, 17-19 May, 2011 , Kuala Lumpur. http://www.iium.edu.my/icbioe/2011/
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 Noorbatcha, Ibrahim Ali Sultan, A. M. Amid, Azura Mohd. Salleh, Hamzah 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 with and without calcium ions were performed at 60°C and 80°C in water as the solvent medium, for duration of 2 ns. Root mean square deviations(RMSD) of backbone atoms are found to be lower in the presence of calcium ions at both the temperatures. In addition, RMSD values for individual residues of phytase at both calcium states and temperatures revealed that all residues that showed high RMSD values are located in turns or coils at the outer surface of the enzyme. As a result, these residues are the most susceptible to heating, hence produce high fluctuations.
format	Conference or Workshop Item
author	Noorbatcha, Ibrahim Ali Sultan, A. M. Amid, Azura Mohd. Salleh, Hamzah
author_facet	Noorbatcha, Ibrahim Ali Sultan, A. M. Amid, Azura Mohd. Salleh, Hamzah
author_sort	Noorbatcha, Ibrahim Ali
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
publishDate	2011
url	http://irep.iium.edu.my/3974/ http://irep.iium.edu.my/3974/ http://irep.iium.edu.my/3974/1/MD_Study_of_the_Effect_of_Ca_ions_on_the_Thermostability_of_B_amyloliquefaciens_Phytase_pg299-301.pdf
first_indexed	2023-09-18T20:11:59Z
last_indexed	2023-09-18T20:11:59Z
_version_	1777407539228442624

Molecular dynamics study of the effect of Calcium Ions on the thermostability of Bacillus amyloliquefaciens Phytase

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