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

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,...

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Main Authors: Nezhad, Nima Ghahremani, Raja Abd Rahman, Raja Noor Zaliha, Normi, Yahaya M., Oslan, Siti Nurbaya, Mohd Shariff, Fairolniza, Leow, Adam Thean Chor
Format: Article
Language:English
Published: Multidisciplinary Digital Publishing Institute 2020
Online Access:http://psasir.upm.edu.my/id/eprint/89418/1/FEED.pdf
http://psasir.upm.edu.my/id/eprint/89418/
https://www.mdpi.com/2073-4344/10/8/844
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spelling my.upm.eprints.894182021-08-18T09:37:22Z http://psasir.upm.edu.my/id/eprint/89418/ Integrative structural and computational biology of phytases for the animal feed industry Nezhad, Nima Ghahremani Raja Abd Rahman, Raja Noor Zaliha Normi, Yahaya M. Oslan, Siti Nurbaya Mohd Shariff, Fairolniza Leow, Adam Thean Chor 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. Multidisciplinary Digital Publishing Institute 2020 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/89418/1/FEED.pdf 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 https://www.mdpi.com/2073-4344/10/8/844 10.3390/catal10080844
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description 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.
format Article
author Nezhad, Nima Ghahremani
Raja Abd Rahman, Raja Noor Zaliha
Normi, Yahaya M.
Oslan, Siti Nurbaya
Mohd Shariff, Fairolniza
Leow, Adam Thean Chor
spellingShingle Nezhad, Nima Ghahremani
Raja Abd Rahman, Raja Noor Zaliha
Normi, Yahaya M.
Oslan, Siti Nurbaya
Mohd Shariff, Fairolniza
Leow, Adam Thean Chor
Integrative structural and computational biology of phytases for the animal feed industry
author_facet Nezhad, Nima Ghahremani
Raja Abd Rahman, Raja Noor Zaliha
Normi, Yahaya M.
Oslan, Siti Nurbaya
Mohd Shariff, Fairolniza
Leow, Adam Thean Chor
author_sort Nezhad, Nima Ghahremani
title Integrative structural and computational biology of phytases for the animal feed industry
title_short Integrative structural and computational biology of phytases for the animal feed industry
title_full Integrative structural and computational biology of phytases for the animal feed industry
title_fullStr Integrative structural and computational biology of phytases for the animal feed industry
title_full_unstemmed Integrative structural and computational biology of phytases for the animal feed industry
title_sort integrative structural and computational biology of phytases for the animal feed industry
publisher Multidisciplinary Digital Publishing Institute
publishDate 2020
url http://psasir.upm.edu.my/id/eprint/89418/1/FEED.pdf
http://psasir.upm.edu.my/id/eprint/89418/
https://www.mdpi.com/2073-4344/10/8/844
_version_ 1709669011862585344
score 13.211869

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