Co‐immobilization and Colocalization of Multi‐Enzyme Systems for the Cell‐Free Biosynthesis of Aminoalcohols

Abstract

Abstract The manufacturing of aminoalcohols is an appealing transformation for industrial biocatalysis due to their high value as building blocks in synthetic chemistry. By co‐immobilizing dehydrogenases, ω‐transaminases and oxidases on porous carriers, we fabricated and characterized a multi‐functional heterogeneous biocatalyst that was further applied to the cell‐free biosynthesis of amines and aminoalcohols from alcohols and diols, respectively. This immobilized cascade integrates both redox cofactor and amine donor recycling systems into the amino alcohol biosynthesis. Spatial co‐localization of the multi‐enzyme system significantly increases the cofactor recycling efficiency, the system productivity and the product conversion. Using this multi‐functional heterogeneous biocatalyst, we achieved 80 % conversion of alcohols into amines and accessed a palette of up to 5 aminoalcohols starting from their corresponding diols in one‐pot. The results herein presented contribute to understanding the effects of the confinement of co‐immobilized enzymes on the cascade processes.