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These chemical dialogs shape fundamental biological processes and define interactions from cooperation to antagonism. Quorum\u2010quenching (QQ) enzymes, which degrade or modify quorum sensing (QS) molecules such as N\u2010acyl\u2010homoserine lactones (AHLs), may play a pivotal role in shaping these networks. While bacterial QQ lactonases are well\u2010characterized, fungal lactonases remain undercharacterized, including their potential to target both bacterial QS molecules and fungal secondary metabolites. Using phylogenetic and structural analysis, we identified putative lactonases from the metallo\u2010\u03b2\u2010lactamase\u2010like lactonase family in fungi and biochemically validated the activity of one of them, from\n                    <jats:italic>Aspergillus pseudonomiae<\/jats:italic>\n                    . Structural alignment between bacterial lactonases and the AlphaFold\u2010predicted structure of the fungal homolog further supports that the fungal protein is indeed a lactonase. We then applied Protein Repair One\u2010Stop Shop algorithm for stability engineering to design a variant with improved expression in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    and thermal stability. Purified enzyme demonstrated broad substrate specificity, effectively degrading various bacterial AHLs, with\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>cat<\/jats:sub>\n                    \/\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>M<\/jats:sub>\n                    values of up to 1.4\u2009\u00d7\u200910\n                    <jats:sup>5<\/jats:sup>\n                    s\n                    <jats:sup>\u22121<\/jats:sup>\n                    M\n                    <jats:sup>\u22121<\/jats:sup>\n                    . Both docking analysis and in vitro assays indicated that the enzyme could accommodate and act on the fungal secondary metabolite patulin, a mycotoxin associated with post\u2010harvest disease, showing high catalytic efficiency (1.1\u2009\u00d7\u200910\n                    <jats:sup>4<\/jats:sup>\n                    s\n                    <jats:sup>\u22121<\/jats:sup>\n                    M\n                    <jats:sup>\u22121<\/jats:sup>\n                    ). When added exogenously to microbial cultures, the enzyme reduced bacterial biofilms and impaired fungal hyphal development, with the hyphal inhibition accompanied by a concentration\u2010dependent increase in ROS. Together, these results show that this fungal enzyme functions as a dual\u2010acting lactonase, positioning it as an interference enzyme in chemical signaling of fungi and bacteria and as a means to suppress pathogens and reduce patulin contamination in food.\n                  <\/jats:p>","DOI":"10.1002\/pro.70729","type":"journal-article","created":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T01:05:49Z","timestamp":1785287149000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The characterization of a new stabilized lactonase from the endophytic fungi\n                    <i>Aspergillus pseudonomiae<\/i>\n                    with anti\u2010bacterial and anti\u2010fungal properties"],"prefix":"10.1002","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-3282-7835","authenticated-orcid":false,"given":"Dor","family":"Ben Tovim","sequence":"first","affiliation":[{"name":"Department of Oral Biology, The Goldschleger School of Dental Medicine, Gray Faculty of Medical and Health Sciences Tel Aviv University  Tel Aviv Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6380-1337","authenticated-orcid":false,"given":"Olena","family":"Trofimyuk","sequence":"additional","affiliation":[{"name":"Department of Oral Biology, The Goldschleger School of Dental Medicine, Gray Faculty of Medical and Health Sciences Tel Aviv University  Tel Aviv Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elon","family":"Yariv","sequence":"additional","affiliation":[{"name":"The Department of Biochemistry and Molecular Biology, School of Neurobiology, Biochemistry and Biophysics, George S. Wise Faculty of Life Sciences Tel Aviv University  Tel Aviv Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4703-7161","authenticated-orcid":false,"given":"Gali","family":"Prag","sequence":"additional","affiliation":[{"name":"The Department of Biochemistry and Molecular Biology, School of Neurobiology, Biochemistry and Biophysics, George S. 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