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...
| Main Authors: | , , , |
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| Format: | Proceeding Paper |
| Language: | English |
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2011
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| Online Access: | 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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| 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 |
| building | IIUM Repository |
| collection | Online Access |
| 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.
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| first_indexed | 2025-11-14T14:27:04Z |
| format | Proceeding Paper |
| id | iium-3974 |
| institution | International Islamic University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T14:27:04Z |
| publishDate | 2011 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | iium-39742021-06-29T02:22:18Z 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 Proceeding Paper 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/ |
| 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 |
| title | 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_short | 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 |
| topic | TP248.13 Biotechnology |
| 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 |