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Dirk Tischler, Eric Gädke, Daniel Eggerichs, Álvaro Gómez Baraibar, Carolin Mügge, Anika Scholtissek, Caroline E. Paul

• Ene‐reductases allow regio‐ and stereoselective reduction of activated C=C double bonds at the expense of nicotinamide adenine dinucleotide cofactors [NAD(P)H]. Biological NAD(P)H can be replaced by synthetic mimics to facilitate enzyme screening and process optimization. The ene‐reductase \(\it F\)OYE‐1, originating from an acidophilic iron oxidizer, has been described as a promising candidate and is now being explored for applied biocatalysis. Biological and synthetic nicotinamide cofactors were evaluated to fuel \(\it F\)OYE‐1 to produce valuable compounds. A maximum activity of (319.7\(\pm\)3.2) U mg\(^{−1}\) with NADPH or of (206.7\(\pm\)3.4) U mg\(^{−1}\) with 1‐benzyl‐1,4‐dihydronicotinamide (BNAH) for the reduction of \(\it N\)‐methylmaleimide was observed at 30 °C. Notably, BNAH was found to be a promising reductant but exhibits poor solubility in water. Different organic solvents were therefore assayed: \(\it F\)OYE‐1 showed excellent performance in most systems with up to 20 vol% solvent and at temperatures up to 40 °C. Purification and application strategies were evaluated on a small scale to optimize the process. Finally, a 200 mL biotransformation of 750 mg (\(\it R\))‐carvone afforded 495 mg of (2\(\it R\),5\(\it R\))‐dihydrocarvone (>95 % \(\it ee\)), demonstrating the simplicity of handling and application of \(\it F\)OYE‐1.