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Enzymatic cascades play a crucial role in energy conversion and chemical transformations in living organisms. Due to enzymes’ high selectivity in catalysis and eco-friendly nature, operating enzymatic cascades in cell-free systems has the potential to improve existing chemical transformations. However, applications involving enzymes are often limited by their poor stability in cell-free environments, and the impact of immobilization on the kinetics of enzymatic cascades remains relatively underexplored, largely due to challenges in determining the support structure and controlling the enzyme immobilization process. In this work, we developed NU-1510-Cr, a chromium-based mesoporous metal–organic framework (MOF) with the mtn topology to encapsulate an enzyme cascade that oxidizes ethanol to acetaldehyde and subsequently to acetic acid. The crystalline hierarchical pores provide spatial control of the enzymes within the host, where the impact of the spatial organization on the cascaded reaction kinetics was assessed. The findings offer valuable insights for those aiming to immobilize and compartmentalize biocatalytic or chemocatalytic cascade systems and develop efficient microscale and nanoscale bioreactors.