The reduction of carbon dioxide to valuable chemicals through enzymatic processes is regarded as a promising approach for the reduction of carbon dioxide emissions. In this study, an in vitro multi-enzyme cascade pathway is constructed for the conversion of CO2 into dihydroxyacetone (DHA). This pathway, known as FFFP, comprises formate dehydrogenase (FDH), formaldehyde dehydrogenase (FaldDH), formolase (FLS), and phosphite dehydrogenase (PTDH), with PTDH serving as the critical catalyst for regenerating the coenzyme NADH. Subsequently, the immobilization of the FFFP pathway within the hydrogen-bonded organic framework (HOF-101) is accomplished in situ. A 1.8-fold increase in DHA yield is observed in FFFP@HOF-101 compared to the free FFFP pathway. This enhancement can be explained by the fact that within FFFP@HOF-101, enzymes are positioned sufficiently close to one another, leading to the elevation of the local concentration of intermediates and an improvement in mass transfer efficiency. Moreover, FFFP@HOF-101 displays a high degree of stability. In addition to the establishment of an effective DHA production method, innovative concepts for the tailored synthesis of fine compounds from CO2 through the utilization of various multi-enzyme cascade developments are generated by this work.
Keywords: biocatalysis; carbon dioxide; hydrogen‐bonded organic framework; immobilization; multienzyme.
© 2023 Wiley‐VCH GmbH.