ArticleThe protein journal2013
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study.
Article in The protein journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- Structural and Functional Characterization of Obesumbacterium proteus Phytase: A Comprehensive In-Silico Study.Molecular biotechnology · 2025Article
- Cold-adapted characteristics and gene knockout of alkyl hydroperoxide reductase subunit C in Antarctic Psychrobacter sp. ANT206.World journal of microbiology & biotechnology · 2024Article
- Bioprocess for Production, Characteristics, and Biotechnological Applications of Fungal Phytases.Frontiers in microbiology · 2020Review
- Insights into the unfolding pathway and identification of thermally sensitive regions of phytase from Aspergillus niger by molecular dynamics simulations.Journal of molecular modeling · 2015Article
- Biochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability.International journal of molecular sciences · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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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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