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Integrative structural and computational biology of phytases for the animal feed industry


Nezhad, Nima Ghahremani and Raja Abd Rahman, Raja Noor Zaliha and Normi, Yahaya M. and Oslan, Siti Nurbaya and Mohd Shariff, Fairolniza and Leow, Adam Thean Chor (2020) Integrative structural and computational biology of phytases for the animal feed industry. Catalysts, 10 (8). pp. 1-24. ISSN 2073-4344


Resistance to high temperature, acidic pH and proteolytic degradation during the pelleting process and in the digestive tract are important features of phytases as animal feed. The integration of insights from structural and in silico analyses into factors affecting thermostability, acid stability, proteolytic stability, catalytic efficiency and specific activity, as well as N-glycosylation, could improve the limitations of marginal stable biocatalysts with trade-offs between stability and activity. Synergistic mutations give additional benefits to single substitutions. Rigidifying the flexible loops or inter-molecular interactions by reinforcing non-bonded interactions or disulfide bonds, based on structural and roof mean square fluctuation (RMSF) analyses, are contributing factors to thermostability. Acid stability is normally achieved by targeting the vicinity residue at the active site or at the neighboring active site loop or the pocket edge adjacent to the active site. Extending the positively charged surface, altering protease cleavage sites and reducing the affinity of protease towards phytase are among the reported contributing factors to improving proteolytic stability. Remodeling the active site and removing steric hindrance could enhance phytase activity. N-glycosylation conferred improved thermostability, proteases degradation and pH activity. Hence, the integration of structural and computational biology paves the way to phytase tailoring to overcome the limitations of marginally stable phytases to be used in animal feeds.

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Official URL or Download Paper: https://www.mdpi.com/2073-4344/10/8/844

Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Institute of Bioscience
DOI Number: https://doi.org/10.3390/catal10080844
Publisher: Multidisciplinary Digital Publishing Institute
Keywords: Thermostability; Acid stability; Proteolytic stability; Improved activity; Microbial phytases
Depositing User: Ms. Nuraida Ibrahim
Date Deposited: 18 Aug 2021 09:35
Last Modified: 18 Aug 2021 09:37
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3390/catal10080844
URI: http://psasir.upm.edu.my/id/eprint/89418
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