Simultaneous production of linear α-olefins and 2,5-furandicarboxylic acid by combining two recombinant enzymes OleT-ELP and HMFO-ELP

The enzyme OleT can utilize H 2 O 2 as the co-substrate, and this biocatalysis is an H 2 O 2 -driven enzymatic catalysis. In this work, OleT was recombinated by being fused to an elastin-like polypeptide (ELP). The recombinant enzyme OleT-ELP exhibits higher stability and resistance to H 2 O 2 interference compared to native OleT. OleT-ELP showed improved catalytic efficiency in producing α-olefins via fatty acid decarboxylation. The recombinant 5-hydroxymethylfurfural oxidase ( HMFO-ELP) catalyzes the oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-furandicarboxylic acid (FDCA), generating H 2 O 2 as a byproduct. Combining OleT-ELP with HMFO-ELP enabled simultaneous conversion of fatty acids and HMF. The in situ H 2 O 2 generated by HMFO-ELP was transferred to OleT-ELP, enhancing catalytic efficiencies for both α-olefins and FDCA production.