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,...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-07-01
|
| Series: | Catalysts |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4344/10/8/844 |
| _version_ | 1797561122833825792 |
|---|---|
| author | Nima Ghahremani Nezhad Raja Noor Zaliha Raja Abd Rahman Yahaya M. Normi Siti Nurbaya Oslan Fairolniza Mohd Shariff Thean Chor Leow |
| author_facet | Nima Ghahremani Nezhad Raja Noor Zaliha Raja Abd Rahman Yahaya M. Normi Siti Nurbaya Oslan Fairolniza Mohd Shariff Thean Chor Leow |
| author_sort | Nima Ghahremani Nezhad |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T18:09:51Z |
| format | Article |
| id | doaj.art-2a4ececd1fff46f481aa45b6a412dad9 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T18:09:51Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-2a4ececd1fff46f481aa45b6a412dad92023-11-20T08:09:07ZengMDPI AGCatalysts2073-43442020-07-0110884410.3390/catal10080844Integrative Structural and Computational Biology of Phytases for the Animal Feed IndustryNima Ghahremani Nezhad0Raja Noor Zaliha Raja Abd Rahman1Yahaya M. Normi2Siti Nurbaya Oslan3Fairolniza Mohd Shariff4Thean Chor Leow5Enzyme and Microbial Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor 43400, MalaysiaEnzyme and Microbial Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor 43400, MalaysiaEnzyme and Microbial Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor 43400, MalaysiaEnzyme and Microbial Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor 43400, MalaysiaEnzyme and Microbial Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor 43400, MalaysiaEnzyme and Microbial Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor 43400, MalaysiaResistance 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.https://www.mdpi.com/2073-4344/10/8/844thermostabilityacid stabilityproteolytic stabilityimproved activitymicrobial phytases |
| spellingShingle | Nima Ghahremani Nezhad Raja Noor Zaliha Raja Abd Rahman Yahaya M. Normi Siti Nurbaya Oslan Fairolniza Mohd Shariff Thean Chor Leow Integrative Structural and Computational Biology of Phytases for the Animal Feed Industry Catalysts thermostability acid stability proteolytic stability improved activity microbial phytases |
| title | 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_short | 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 |
| topic | thermostability acid stability proteolytic stability improved activity microbial phytases |
| url | https://www.mdpi.com/2073-4344/10/8/844 |
| work_keys_str_mv | AT nimaghahremaninezhad integrativestructuralandcomputationalbiologyofphytasesfortheanimalfeedindustry AT rajanoorzaliharajaabdrahman integrativestructuralandcomputationalbiologyofphytasesfortheanimalfeedindustry AT yahayamnormi integrativestructuralandcomputationalbiologyofphytasesfortheanimalfeedindustry AT sitinurbayaoslan integrativestructuralandcomputationalbiologyofphytasesfortheanimalfeedindustry AT fairolnizamohdshariff integrativestructuralandcomputationalbiologyofphytasesfortheanimalfeedindustry AT theanchorleow integrativestructuralandcomputationalbiologyofphytasesfortheanimalfeedindustry |