Enzyme Surface Residues Direct Encapsulation into Metal-Organic Frameworks for Performance Regulation

Herein, we highlight the role of nitrogen-enriched surface groups on proteins in directing topological transformations of metal-organic frameworks (MOFs). Using a modified-protein-directed MOFs template synthesis (mDTS) strategy, we demonstrate that these surface modifications on cytochrome c (Cyt c) selectively induce the formation of leaf-like zeolitic imidazolate frameworks (ZIF-L). This approach not only enables a structural transition from ZIF-8 to a more open ZIF-L framework but also substantially enhances the catalytic activity and loading of Cyt c beyond traditional immobilization methods. Adjusting the concentration of the surface modifier allows for precise tuning of the Cyt c activity, allowing optimal enzyme function at specific modifier levels. Furthermore, our results reveal that surface modifications of a variety of proteins can facilitate the formation of ZIF-L, emphasizing the broad applicability of the mDTS method. This approach offers significant promise for developing highly efficient protein-MOF composites, offering transformative potential for industrial catalysis and biotechnological applications.