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

doi:10.1007/s10930-013-9489-y

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Article

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

The protein journal - 1 Apr 2013

Noorbatcha I A, Sultan A M, Salleh H M, Amid Azura

Abstract excerpt

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...

Topics

6-Phytase
Amino Acid Substitution
Aspergillus niger
Enzyme Stability
Fungal Proteins
Hydrogen Bonding
Molecular Dynamics Simulation
Mutation

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Open in PubMed

Identifiers

PMID: 23636517
DOI: 10.1007/s10930-013-9489-y

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