{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,6]],"date-time":"2026-09-06T18:13:12Z","timestamp":1788718392469,"version":"build-2803163510"},"reference-count":49,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2025,7,2]],"date-time":"2025-07-02T00:00:00Z","timestamp":1751414400000},"content-version":"vor","delay-in-days":1,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["U23A2034"],"award-info":[{"award-number":["U23A2034"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["enviromicro-journals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Environmental Microbiology"],"published-print":{"date-parts":[[2025,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Phthalate esters (PAEs) are prevalent environmental contaminants, with their biodegradation efficiently driven by microorganisms through ester bond hydrolysis. This study investigates the mechanism of Poc14, a novel family IV esterase, using x\u2010ray crystallography, bioinformatics, biochemistry and site\u2010directed mutagenesis. Phylogenetic analysis classifies Poc14 as a family IV esterase with conserved catalytic motifs crucial for its activity. Poc14 retains over 80% activity at 50\u00b0C for 4\u2009h and tolerates up to 5% methanol or DMF, though surfactants like Tweens inhibit its function. Poc14 activity is independent of metal ions, and the addition of EDTA further enhances its activity by approximately 130%. The 1.8\u2009\u00c5 crystal structure reveals a CAP domain and two substrate channels. Enzyme assays show Poc14 hydrolyses short\u2010chain diethyl phthalate (DEP) (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>\n                      <jats:italic>m<\/jats:italic>\n                    <\/jats:sub>\n                    \u2009=\u20090.068\u2009mM,\n                    <jats:italic>V<\/jats:italic>\n                    <jats:sub>\n                      <jats:italic>max<\/jats:italic>\n                    <\/jats:sub>\n                    \u2009=\u20099975\u2009\u03bcM\/min\/mg) but not long\u2010chain di(2\u2010ethylhexyl) phthalate (DEHP) due to steric hindrance. Molecular docking assessed Poc14's potential to hydrolyse DEP and DEHP after residue mutations, resulting in the Poc14\u2010AAG variant. Poc14\u2010AAG could hydrolyse one bond of DEHP and diester bonds of DEP. Our study positions Poc14 as a promising enzyme for environmental remediation, with potential for optimising DEHP degradation and exploring dimerisation effects.\n                  <\/jats:p>","DOI":"10.1111\/1462-2920.70134","type":"journal-article","created":{"date-parts":[[2025,7,2]],"date-time":"2025-07-02T09:58:48Z","timestamp":1751450328000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Molecular Insight Into the Hydrolysis of Phthalate Esters by a Family\n                    <scp>IV<\/scp>\n                    Esterase"],"prefix":"10.1111","volume":"27","author":[{"given":"Zhen","family":"Rong","sequence":"first","affiliation":[{"name":"State Key Laboratory of Submarine Geoscience, Second Institute of Oceanography Ministry of Natural Resources  Hangzhou People's Republic of 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