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Multivariate Silicification‐Assisted Single Enzyme Structure Augmentation for Improved Enzymatic Activity–Stability Trade‐Off
Ist Teil von
Angewandte Chemie, 2024-07, Vol.136 (29), p.n/a
Ort / Verlag
Weinheim: Wiley Subscription Services, Inc
Erscheinungsjahr
2024
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
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. Herein, we propose the concept of the “silicazyme”, where solid inorganic silica undergoes controlled hybridization with the fragile enzyme under moderate conditions at the single‐enzyme level, thus enabling 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 the 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 with promise for catalysis, separations, and nanomedicine.
The concept of the “silicazyme” is introduced, where inorganic silica precursors are used to balance the flexibility and stability of an enzyme. The integration of the enzyme with an organosilica framework brings advantages including surface microenvironment adjustability, structure augmentation, prolonged stability, reversible modification capability, and functional extensibility, which have the potential to expand enzyme applications.