The 9 th principle of green chemistry states: "catalytic reagents (as selective as possible) are superior to stoichiometric reagents". Catalysis is nowadays a widely implemented approach to improve the atom economy and reduce the energy required for certain chemical transformations, which are sometimes impossible without the employment of a catalyst. In this context, hybrid chemoenzymatic catalysis emerges as an outstanding strategy that takes advantage of the two different and sometimes antagonistic fields in catalysis: heterogeneous catalysis and biocatalysis. This combination can provide effective catalytic routes for processes which still need improvements to become part of a sustainable economy. Amide synthesis is one of the most important transformations in agrochemicals, pharmaceuticals and polymer industries. In recent decades, there has been growing interest in processes for obtaining amides after the ACS Green Chemistry Institute pointed out the need for more sustainable approaches for amide production as a key research area for a more environmentally friendly chemistry. The most common approach for producing amides is the nucleophilic addition of an amine to an activated carboxylic acid. However, the activating agents involved in these reactions often lead to the generation of waste and hazardous byproducts. Alternatively, biocatalysis is currently seen as a powerful tool for the sustainable synthesis of a wide range of compounds. Enzymes, owing to their biological roles, exhibit high chemo-, regio-, and often stereoselectivity. Additionally, enzymatic reactions typically occur in aqueous medium under mild conditions. Industrially, amides have been synthesized using mainly hydrolases (such as lipases, esterases, and acylases), nitriles hydratases, and transglutaminases. In addition, the repertoire of enzymes known to catalyze the amide bond formation includes thioesterases (TEs) from both polyketide synthase (PKS) and non-ribosomal peptide synthetases (NRPS) systems, stand-alone adenylation domains (SAADs), carboxylic acid reductases (CARs), amide-bond synthetases (ABSs), AMPligating enzymes and acyl-coenzyme A ligases (ACLs). ACLs are enzymes belonging to the adenylate-forming enzyme superfamily, which comprises acyl-and aryl CoA synthetases, non-ribosomal peptide synthetases, and luciferases, being responsible for a variety of biological processes. ACLs catalyze ATP-dependent formation of acyl-CoA thioesters from carboxylic acids in two-step reaction: first formation of adenylate derivative from carboxylic acid and ATP, second, nucleophilic attack of coenzyme A (HSCoA). Diversion of the native reaction by adding extra amine nucleophile in absence of HSCoA leads to the formation of amides. Thus, ACLs represent an alternative biocatalytic system for amide synthesis. Combined with upstream catalytic formation of carboxylic acids from alcohols available from renewable sources, this process offers a sustainable pathway for amide synthesis. This strategy, with sequential catalytic steps where each step is catalyzed by a different type of catalyst, here heterogeneous catalyst and biocatalyst, is called hybrid catalysis. It has the advantage of concentrating all the reagents and catalysts in one and the same reaction medium, which limits energy consumption, eliminates intermediate purification, and therefore the cost in atoms, and makes it possible to carry out the synthesis of compounds that were previously difficult to access. In particular, several studies have already demonstrated the interest of coupling gold nanoparticles with different families of enzymes for the construction of innovative reaction cascades, in particular in order to introduce chirality into new building blocks. We have recently exemplified the capacity of hybrid catalysis through the production of a new non-natural aromatic ω-amino acid, resulting from the oxidation and successive amination of 5-hydroxymethylfurfural (HMF): the 5-aminomethyl-2-furancarboxylic acid (AMFC). In addition to being a potential monomer for polymerization into new polyamides, it serves as a valuable and versatile platform molecule due to its acid and amine functions. To date, no functionalization of AMFC has yet been achieved. Grafting variable-length aliphatic chains onto one of these functions could lead to the formation of amphiphilic molecules. In such a structure, the remaining ionisable function would act as the polar head, while the aromatic ring and the long chain constitute the apolar part. In a first approach, we planned to use the amine function as anchoring point for long chain amides. To achieve this, we combined the oxidation of various alcohols into carboxylic acids using a heterogeneous chemocatalyst with the formation of amides, employing AMFC as the amine donor and catalyzed by an ACL enzyme. This approach enables us to introduce a novel hybrid system for the direct synthesis of long chain amides from AMFC and aliphatic alcohols (Scheme 1).