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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Springer
2013
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| Subjects: | |
| Online Access: | 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 |
| Summary: | 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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