Enhancing Biocatalysis through Chiral Supramolecular Scaffolds: Insights into the Structural Adaptability of Lipase.

How to maintain high catalytic activity and stability in the process of biocatalysis is crucial, inspiring strategies to construct an appropriate catalytic microenvironment. Considering the lipase's inherent chirality and the necessity for a delicate hydrophilic-hydrophobic equilibrium, we crafted a chiral, nonaqueous catalytic microenvironment via the in situ coassembly of Boc-F L F L -NHNH 2 (Bfl) and lipase. Benefiting from the chirality and distinct Bfl-lipase interactions, the lipase@Bfl supramolecular hybrid amplifies biological functionalities and can serve as a versatile and highly efficient catalyst. Kinetic investigations and molecular docking simulations uncover the strong lipase-substrate affinity and lipase-Bfl interactions, explaining the enhanced biological effects, catalytic activity, and stability. Our study establishes a suitable microenvironment to address the chirality and hydrophobicity during catalysis and highlights the potential of artificial chiral scaffolds and catalytic medium for enhancing lipase activity.