Programmable enzyme catalysis based on multiscale confinements

doi:10.1038/s44160-025-00898-1

Programmable enzyme catalysis based on multiscale confinements

2025-10-24

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DOI：10.1038/s44160-025-00898-1

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Enzymes are powerful catalysts in nature, enabling the sustainable and efficient synthesis of complex biomolecules. The remarkable efficiency of enzymes arises from the intricately organized and spatially confined intracellular environment. Inspired by nature, researchers are increasingly applying these principles to design extracellular enzyme catalysts with enhanced performance. Multiscale confinement serves as a unifying strategy for programmable biocatalysis. This approach includes (1) confining metal atoms or catalytic residues within enzyme active sites to create artificial enzymes, (2) immobilizing enzymes on surfaces or within nanocarriers to enhance stability and efficiency and (3) restricting the diffusion of reaction intermediates to mimic substrate channelling in multienzyme complexes. This Review examines how multiscale confinement can be harnessed for superior catalyst design in organic synthesis. Recent advancements are highlighted, and current challenges, as well as future directions for this rapidly evolving field, are discussed. Inspired by nature’s spatially organized catalytic systems, multiscale confinement emerges as a powerful strategy for programmable biocatalysis. This Review highlights recent advances in designing artificial enzymes, enzyme immobilization methods and substrate channelling techniques, discussing current challenges and future directions towards efficient, sustainable enzyme catalysis for organic synthesis.

Keywords:

artificial enzymes

enzyme immobilization

substrate channelling

multiscale confinement

biocatalysis

Programmable enzyme catalysis based on multiscale confinements

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