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Updated: May 11, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
I A Noorbatcha1, A M Sultan, H M Salleh
1BioProcess and Molecular Engineering Research Unit BPMERU, Department of Biotechnology Engineering, Faculty of Engineering, International Islamic University Malaysia, Jalan Gombak, 53100 Kuala Lumpur, Malaysia. ibrahiman@iium.edu.my
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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