High-loading and efficient immobilization of commercial CalA/CalB lipase blend onto tbo-COF for enhanced ester hydrolysis activity.

Lipase-catalyzed hydrolysis is generally hampered by a narrow substrate scope, poor catalytic efficiency, and surfactants are often required to form emulsions to improve enzyme-substrate contact. Developing lipase immobilization supports that achieve efficient emulsifier-free hydrolysis while retaining high loading capacity and operational stability remains a critical challenge. Herein, we report a tbo covalent organic framework (COF) as a robust support for immobilizing a commercial CalA/CalB lipase blend. Through van der Waals interactions, the COF enables an ultrahigh lipase loading of 1900 wt%. The resulting Lipase@COF exhibits expanded substrate adaptability and excellent long-term storage stability. Moreover, it delivers enhanced catalytic performance, achieving over 90% hydrolysis conversion for three plant oils within 13 h. Meanwhile, the intrinsic microenvironment of the COF alleviates hydrolysis-induced inhibitory effects and strengthens catalytic stability. This work validates 3D COFs as multifunctional scaffolds for high-performance immobilized lipases, providing a feasible strategy for ester hydrolysis and lipid modification.