JZUS - Journal of Zhejiang University SCIENCE

Journal of Zhejiang University SCIENCE B

Accepted manuscript available online (unedited version)

Improving the thermal stability of trans-epoxysuccinate hydrolase

Author(s): Wenna BAO¹, Jinfeng YAO¹, Haifeng PAN², Ronglin ZHU¹, Xinying LI¹, Hongxiu LIAO¹
Affiliation(s): ¹School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, China; more
Corresponding email(s): haifengpan518@163.com
Key Words: trans-epoxysuccinate hydrolase; Pseudomonas koreana; Molecular dynamics simulation; Thermal stability modification

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Wenna BAO¹, Jinfeng YAO¹, Haifeng PAN², Ronglin ZHU¹, Xinying LI¹, Hongxiu LIAO¹. Improving the thermal stability of trans-epoxysuccinate hydrolase[J]. Journal of Zhejiang University Science B,in press.Frontiers of Information Technology & Electronic Engineering,in press.https://doi.org/10.1631/jzus.B2500069

@article{title="Improving the thermal stability of trans-epoxysuccinate hydrolase",
author="Wenna BAO¹, Jinfeng YAO¹, Haifeng PAN², Ronglin ZHU¹, Xinying LI¹, Hongxiu LIAO¹",
journal="Journal of Zhejiang University Science B",
year="in press",
publisher="Zhejiang University Press & Springer",
doi="https://doi.org/10.1631/jzus.B2500069"
}

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%T Improving the thermal stability of trans-epoxysuccinate hydrolase
%A Wenna BAO¹
%A Jinfeng YAO¹
%A Haifeng PAN²
%A Ronglin ZHU¹
%A Xinying LI¹
%A Hongxiu LIAO¹
%J Journal of Zhejiang University SCIENCE B
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%@ 1673-1581
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%I Zhejiang University Press & Springer
doi="https://doi.org/10.1631/jzus.B2500069"

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T1 - Improving the thermal stability of trans-epoxysuccinate hydrolase
A1 - Wenna BAO¹
A1 - Jinfeng YAO¹
A1 - Haifeng PAN²
A1 - Ronglin ZHU¹
A1 - Xinying LI¹
A1 - Hongxiu LIAO¹
J0 - Journal of Zhejiang University Science B
SP -
EP -
%@ 1673-1581
Y1 - in press
PB - Zhejiang University Press & Springer
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doi="https://doi.org/10.1631/jzus.B2500069"

Abstract
Chinese Summary
Academic Network
Reviewer Comment

Abstract: This study used molecular dynamics simulations, B-factor analysis and saturation mutagenesis screening to enhance the thermal stability of the trans-epoxysuccinate hydrolase (TESH) derived from Pseudomonas koreensis. Eleven mutants that influence this characteristic were selected, yielding 4 mutants with improved activity. Among them, mutant A142C and S178Q exhibited lower Michaelis constant (K_m) values, and their k_cat (Catalytic constant)/K_m ratios were 4.7 and 1.9 times higher than those of the wild type. The half-life at 50 ° C (T⁵⁰_1/2) values of the two mutants were increased by 107 % and 59 %, respectively, compared to the wild type. Molecular docking and molecular dynamics simulations indicated that the two mutants showed stronger substrate interaction, lower binding energy, and reduced root mean square deviation compared to the wild type, along with decreased electrostatic potential energy and increased hydrophobicity near their mutation sites. The study of protein thermal stability engineering and associated mechanisms provides a valuable reference and holds practical significance for the industrial production of meso-tartaric acid.

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