biostudies-literatureSomvilla IAustrian Science Fund FWFe17740https://www.ebi.ac.uk/biostudies/studies/S-EPMC12866861biostudies-literatureUnknown13(6)Stable chemical bonds dictate the properties of industrial chemicals and materials. Particularly the persistence of synthetic polymers like polyurethanes (PUs) contributes to the global issues of waste accumulation and environmental pollution. To accelerate the discovery and engineering of plastic-degrading biocatalysts, a genetically encoded biosensor platform is established that enzymatically converts polyfunctionalized monomers into (aliphatic) aldehydes and allows their robust detection by a bacterial luciferase. In vivo, in vitro, and hybrid applications of the investigated biosensor system facilitate the bioluminescence-based assessment of the promiscuous esterase, amidase, and urethanase activity of amidase signature family enzymes, circumventing chromatographic analysis. FurthermorAdvanced science (Weinheim, Baden-Wurttemberg, Germany)A Modular Biosensor Platform for the Detection of Plastic Monomers and the Engineering of Promiscuous Amidases Toward Challenging Substrates.PMC12866861J4231-B21J4231‐B21Bayer TMeinert HFlieger MSomvilla IMehnert KMIhrle PBoß JBottcher DSeifert MKoch LMeier HOehlschlager FBornscheuer UTfalseA Modular Biosensor Platform for the Detection of Plastic Monomers and the Engineering of Promiscuous Amidases Toward Challenging Substrates.Stable chemical bonds dictate the properties of industrial chemicals and materials. Particularly the persistence of synthetic polymers like polyurethanes (PUs) contributes to the global issues of waste accumulation and environmental pollution. To accelerate the discovery and engineering of plastic-degrading biocatalysts, a genetically encoded biosensor platform is established that enzymatically converts polyfunctionalized monomers into (aliphatic) aldehydes and allows their robust detection by a bacterial luciferase. In vivo, in vitro, and hybrid applications of the investigated biosensor system facilitate the bioluminescence-based assessment of the promiscuous esterase, amidase, and urethanase activity of amidase signature family enzymes, circumventing chromatographic analysis. Furthermor2026-01-01T00:00:00Z2026 Jan2026-07-15T14:36:40.654Z2026-07-06T03:08:39.877ZS-EPMC128668614122154010.1002/advs.202517740