ArticleChembiochem : a European journal of chemical biology2025
Biosensor-Guided Engineering of a Baeyer-Villiger Monooxygenase for Aliphatic Ester Production.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Advances in amidases and urethanases as depolymerization biocatalysts.Nature chemical biology · 2026Review
- A genetically encoded L-rhamnose biosensor for monitoring marine polysaccharide depolymerization.Applied microbiology and biotechnology · 2026Article
- A Modular Biosensor Platform for the Detection of Plastic Monomers and the Engineering of Promiscuous Amidases Toward Challenging Substrates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Screening, Characterization and Mutagenesis Breeding ofFoods (Basel, Switzerland) · 2025Article
- Biosensor-Guided Engineering of a Baeyer-Villiger Monooxygenase for Aliphatic Ester Production.Chembiochem : a European journal of chemical biology · 2025Article
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Authors and funding
9 authors.
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Abstract
Esters are valuable aroma compounds and can be produced enzymatically by Baeyer-Villiger monooxygenases (BVMOs) from (aliphatic) ketone precursors. However, a genetically encoded biosensor system for the assessment of BVMO activity and the detection of reaction products is missing. In this work, we assembled a synthetic enzyme cascade - featuring an esterase, an alcohol dehydrogenase, and LuxAB - in the heterologous host Escherichia coli. Target esters are produced by a BVMO, subsequently cleaved, and the corresponding alcohol oxidized through the artificial pathway. Ultimately, aldehyde products are detected in vivo by LuxAB, a luciferase from Photorhabdus luminescens that emits bioluminescence upon the oxidation of aldehydes to the corresponding carboxylates. This biosensor system greatly accelerated the screening and selection of active BVMO variants from a focused library, omitting commonly used low-throughput chromatographic analysis. Engineered enzymes accepted linear aliphatic ketones such as 2-undecanone and 2-dodecanone and exhibited improved ester formation.
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