Structural Rigidity and Nucleophilic Proximity Synergistically Enable Efficient High-Temperature Hydrolysis of Phthalate Esters by PestE.

Authors

Yebao Chen, Jingwen Rao, Wenli Liang, Liu Yang, Xiaoyan Hu, Xiaoyu Dong, Yonghua Wang, Rongkang Hu

Published in

Journal of agricultural and food chemistry. Volume 74. Issue 43. Pages 34408-34419. Nov 04, 2026.

Abstract

Phthalic acid esters (PAEs) are persistent environmental pollutants. Their industrial biodegradation demands thermostable, efficient hydrolases. We characterized PestE, a thermostable esterase hydrolyzing both dialkyl and monoalkyl PAEs. PestE retained >98% of its maximal activity in short-term assays at 80-100 °C, with minimal loss after 12 h, and retained ∼50% activity after 48 h at 80 °C, with 99.4% dibutyl phthalate degradation in 2 min. Molecular dynamics simulations indicated that hydrophobic core reorganization and increased surface hydrophilicity synergistically enhance thermostability by balancing global rigidity and local flexibility. Co-crystallization with monobutyl phthalate revealed a substrate-guiding tunnel and catalytic machinery (Ser157-His284-Asp254 triad and oxyanion hole Gly85/Gly86/Ala158) for two-step dealkylation. A key feature is the close proximity of the nucleophilic Ser157 to the substrate carbonyl carbon (2.8-3.1 Å), enabling efficient catalysis. Mutagenesis confirmed key hydrophobic residues for substrate binding and active-site stability. These findings establish PestE as a promising biocatalyst for industrial PAE degradation.

PMID:
42980388
Bibliographic data and abstract were imported from PubMed on 04 Nov 2026.

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