Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study

Abstract Molecular dynamics simulation was used to study the dynamic differences between native Aspergillus niger PhyA phytase and a mutant with 20 % greater thermostability. Atomic root mean square deviation, radius of gyration, and number of hydrogen bonds and salt bridges are examined to det...

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Main Authors: Noorbatcha, Ibrahim Ali, Sultan, Anas Mufid Nasri, Mohd. Salleh, Hamzah, Amid, Azura
Format: Article
Language:English
Published: Springer 2013
Subjects:
Online Access:http://irep.iium.edu.my/30144/
http://irep.iium.edu.my/30144/1/PhyA_Phytase_PJ_%282013%29_32-309-316.pdf
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author Noorbatcha, Ibrahim Ali
Sultan, Anas Mufid Nasri
Mohd. Salleh, Hamzah
Amid, Azura
author_facet Noorbatcha, Ibrahim Ali
Sultan, Anas Mufid Nasri
Mohd. Salleh, Hamzah
Amid, Azura
author_sort Noorbatcha, Ibrahim Ali
building IIUM Repository
collection Online Access
description Abstract Molecular dynamics simulation was used to study the dynamic differences between native Aspergillus niger PhyA phytase and a mutant with 20 % greater thermostability. Atomic root mean square deviation, radius of gyration, and number of hydrogen bonds and salt bridges are examined to determine thermostability factors. The results suggest that, among secondary structure elements, loops have the most impact on the thermal stability of A. niger phytase. In addition, the location rather than the number of hydrogen bonds is found to have an important contribution to thermostability. The results also show that salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly.
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spelling iium-301442021-07-14T09:27:52Z http://irep.iium.edu.my/30144/ Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Mohd. Salleh, Hamzah Amid, Azura TP248.13 Biotechnology Abstract Molecular dynamics simulation was used to study the dynamic differences between native Aspergillus niger PhyA phytase and a mutant with 20 % greater thermostability. Atomic root mean square deviation, radius of gyration, and number of hydrogen bonds and salt bridges are examined to determine thermostability factors. The results suggest that, among secondary structure elements, loops have the most impact on the thermal stability of A. niger phytase. In addition, the location rather than the number of hydrogen bonds is found to have an important contribution to thermostability. The results also show that salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly. Springer 2013-05-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/30144/1/PhyA_Phytase_PJ_%282013%29_32-309-316.pdf Noorbatcha, Ibrahim Ali and Sultan, Anas Mufid Nasri and Mohd. Salleh, Hamzah and Amid, Azura (2013) Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study. Protein Journal, 32. pp. 309-316. ISSN 1572-3887 http://link.springer.com/article/10.1007%2Fs10930-013-9489-y 10.1007/s10930-013-9489-y
spellingShingle TP248.13 Biotechnology
Noorbatcha, Ibrahim Ali
Sultan, Anas Mufid Nasri
Mohd. Salleh, Hamzah
Amid, Azura
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
title Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
title_full Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
title_fullStr Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
title_full_unstemmed Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
title_short Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
title_sort understanding thermostability factors of aspergillus niger phya phytase: a molecular dynamics study
topic TP248.13 Biotechnology
url http://irep.iium.edu.my/30144/
http://irep.iium.edu.my/30144/
http://irep.iium.edu.my/30144/
http://irep.iium.edu.my/30144/1/PhyA_Phytase_PJ_%282013%29_32-309-316.pdf