Improving the thermostability and substrate affinity of IsPETase through the S209H mutation, and exploring the structural role of the N-terminal: a computational study

Improving the thermostability and substrate affinity of IsPETase through the S209H mutation, and exploring the structural role of the N-terminal: a computational study

The current in silico investigation aimed to increase the thermostability of IsPETase for more efficient PET degradation. N-Truncated and S209H mutants were designed to improve the thermostability of IsPETase. The deletion of the first seven N-terminal residues in PETase (N-truncated mutant) disrupt...

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Bibliographic Details
Main Authors: Nezhad, Nima Ghahremani, Buhari, Sunusi Bataiya, Eskandari, Azadeh, Albayati, Samah Hashim, Omotayo, Oluwaloni Folusho, Leow, Thean Chor
Format: Article
Language:en
Published: Springer Science and Business Media Deutschland GmbH 2025
Subjects:
Biotechnology
Environmental Science (miscellaneous)
Online Access:http://psasir.upm.edu.my/id/eprint/122312/1/122312.pdf
http://psasir.upm.edu.my/id/eprint/122312/
https://link.springer.com/article/10.1007/s13205-025-04258-w?error=cookies_not_supported&code=919cc58b-dd8f-4cc7-8707-aec73da205cd
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http://psasir.upm.edu.my/id/eprint/122312/1/122312.pdf
http://psasir.upm.edu.my/id/eprint/122312/
https://link.springer.com/article/10.1007/s13205-025-04258-w?error=cookies_not_supported&code=919cc58b-dd8f-4cc7-8707-aec73da205cd

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