Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification
Engineered thermostable microbial enzymes are widely employed to catalyze chemical reactions in numerous industrial sectors. Although high thermostability is a prerequisite of industrial applications, enzyme activity is usually sacrificed during thermostability improvement. Therefore, it is vital to...
| Main Authors: | , , , , , |
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| Format: | Article |
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Elsevier
2023
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| Online Access: | http://psasir.upm.edu.my/id/eprint/109338/ |
| _version_ | 1848865345082753024 |
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| author | Nezhad, Nima Ghahremani Raja Abd Rahman, Raja Noor Zaliha M. Normi, Yahaya Oslan, Siti Nurbaya Mohd Shariff, Fairolniza Leow, Thean Chor |
| author_facet | Nezhad, Nima Ghahremani Raja Abd Rahman, Raja Noor Zaliha M. Normi, Yahaya Oslan, Siti Nurbaya Mohd Shariff, Fairolniza Leow, Thean Chor |
| author_sort | Nezhad, Nima Ghahremani |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Engineered thermostable microbial enzymes are widely employed to catalyze chemical reactions in numerous industrial sectors. Although high thermostability is a prerequisite of industrial applications, enzyme activity is usually sacrificed during thermostability improvement. Therefore, it is vital to select the common and compatible strategies between thermostability and activity improvement to reduce mutants̕ libraries and screening time. Three functional protein engineering approaches, including directed evolution, rational design, and semi-rational design, are employed to manipulate protein structure on a genetic basis. From a structural standpoint, integrative strategies such as increasing substrate affinity; introducing electrostatic interaction; removing steric hindrance; increasing flexibility of the active site; N- and C-terminal engineering; and increasing intramolecular and intermolecular hydrophobic interactions are well-known to improve simultaneous activity and thermostability. The current review aims to analyze relevant strategies to improve thermostability and activity simultaneously to circumvent the thermostability and activity trade-off of industrial enzymes. |
| first_indexed | 2025-11-15T14:03:14Z |
| format | Article |
| id | upm-109338 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T14:03:14Z |
| publishDate | 2023 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1093382024-08-05T04:05:43Z http://psasir.upm.edu.my/id/eprint/109338/ Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification Nezhad, Nima Ghahremani Raja Abd Rahman, Raja Noor Zaliha M. Normi, Yahaya Oslan, Siti Nurbaya Mohd Shariff, Fairolniza Leow, Thean Chor Engineered thermostable microbial enzymes are widely employed to catalyze chemical reactions in numerous industrial sectors. Although high thermostability is a prerequisite of industrial applications, enzyme activity is usually sacrificed during thermostability improvement. Therefore, it is vital to select the common and compatible strategies between thermostability and activity improvement to reduce mutants̕ libraries and screening time. Three functional protein engineering approaches, including directed evolution, rational design, and semi-rational design, are employed to manipulate protein structure on a genetic basis. From a structural standpoint, integrative strategies such as increasing substrate affinity; introducing electrostatic interaction; removing steric hindrance; increasing flexibility of the active site; N- and C-terminal engineering; and increasing intramolecular and intermolecular hydrophobic interactions are well-known to improve simultaneous activity and thermostability. The current review aims to analyze relevant strategies to improve thermostability and activity simultaneously to circumvent the thermostability and activity trade-off of industrial enzymes. Elsevier 2023-03-31 Article PeerReviewed Nezhad, Nima Ghahremani and Raja Abd Rahman, Raja Noor Zaliha and M. Normi, Yahaya and Oslan, Siti Nurbaya and Mohd Shariff, Fairolniza and Leow, Thean Chor (2023) Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification. International Journal of Biological Macromolecules, 232. art. no. 123440. pp. 1-13. ISSN 0141-8130; ESSN: 1879-0003 https://www.sciencedirect.com/science/article/pii/S0141813023003264?via%3Dihub 10.1016/j.ijbiomac.2023.123440 |
| spellingShingle | Nezhad, Nima Ghahremani Raja Abd Rahman, Raja Noor Zaliha M. Normi, Yahaya Oslan, Siti Nurbaya Mohd Shariff, Fairolniza Leow, Thean Chor Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification |
| title | Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification |
| title_full | Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification |
| title_fullStr | Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification |
| title_full_unstemmed | Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification |
| title_short | Recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification |
| title_sort | recent advances in simultaneous thermostability-activity improvement of industrial enzymes through structure modification |
| url | http://psasir.upm.edu.my/id/eprint/109338/ http://psasir.upm.edu.my/id/eprint/109338/ http://psasir.upm.edu.my/id/eprint/109338/ |