Multivariate Silicification‐Assisted Single Enzyme Structure Augmentation for Improved Enzymatic Activity‐Stability Trade‐Off

Abstract

The ability to finely tune/balance the structure and rigidity of enzymes to realize both high enzymatic activity and long‐term stability is highly desired but highly challenging. In this work, we propose a new concept of silica‐enzyme, referred to as “silicazyme”, where solid inorganic silica was controlled hybridization with fragile enzyme under moderate condition at single‐enzyme level, realizing simultaneous structure augmentation, long‐term stability, and high enzymatic activity preservation. A multivariate silicification approach was utilized and occurred around individual enzymes to allow conformal coating. To realize a high activity‐stability trade‐off the structure flexibility/rigidity of silicazyme was optimized by a component‐adjustment‐ternary (CAT) plot method. Moreover, the multivariate organosilica frameworks bring great advantages including surface microenvironment adjustability, reversible modification capability, and functional extensibility through the rich chemistry of silica. Overall silicazymes represent a new class of enzymes that promise to broaden their utilization in catalysis, separations, and nanomedicine.