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Improving the thermal stability of trans-epoxysuccinate hydrolase
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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, 1998, -1(-1): .
@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",
volume="-1",
number="-1",
pages="",
year="1998",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B2500069"
}
%0 Journal Article
%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
%V -1
%N -1
%P
%@ 1673-1581
%D 1998
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B2500069
TY - JOUR
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
VL - -1
IS - -1
SP -
EP -
%@ 1673-1581
Y1 - 1998
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B2500069
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 (Km) values, and their kcat (Catalytic constant)/Km ratios were 4.7 and 1.9 times higher than those of the wild type. The half-life at 50 ° C (T501/2) 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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