The final objective was to combine the metal-catalyzed oxidation of alcohols with the biocatalyzed amidation in a onepot/two-steps process. More specifically, the process consisted in carrying out the oxidation step under the enzymatic reaction conditions (MOPS buffer, MgCl2, 60 °C), then to add ATP, AMFC and the enzyme, without modification of the operating conditions, in the manner of a fed-batch. For the first step, Au/CaO was used at a concentration of 0.8 % (w/v) (8 mg in 1 mL). With a 2 % (w/w) Au loading, and 10 mM alcohol substrate, this represents a substrate/active phase concentration ratio of 12, without any optimization yet performed. The tandem process was first investigated with model substrate butanol (1a) leading to the formation of 5-(butyramidomethyl)furan-2-carboxylic acid (1c). Butanol oxidation by Au/CaO was performed at 60 °C in MOPS buffer pH 8 with 5 mM MgCl2, on an axial rotary agitator to ensure optimal mixing of the heterogeneous reaction medium. The product formation was monitored by 1 H NMR and, as expected, 94% yield was obtained in 24 h (Table , Figure ). Then, TsACL, AMFC, and ATP were added, along with some MgCl2 to maintain its concentration at 5 mM despite dilution, and the reaction mixture was placed at 60 °C for an extra 24 h. A final yield of 65 % in 5-(butyramidomethyl)furan-2-carboxylic acid (1c) was achieved according to 1 H NMR monitoring, which is very similar to the 71 % yield obtained during ACL screening with this enzyme and butanoic acid (1b). This initial reaction demonstrates the feasibility of coupling the two steps. Importantly, the presence of the chemical catalyst does not significantly inhibit the enzyme.