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Updated: Jul 9, 2026

Surface Functionalization of Metal-Organic Frameworks for Improved Moisture Resistance
Published on: September 5, 2018
Mechanically locking enzymes in covalent organic frameworks via light-responsive nanohands for stable biocatalysis
Tiantian Wang1, Ruobing Xin2, Yang Qian1
1College of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
None:
Enzyme immobilization is pivotal to sustainable biocatalysis, yet the most widespread protocol of physical adsorption on static porous supports suffers from enzyme leakage and short catalytic lifespan. We introduce a dynamic-pore mechano-locking strategy employing tetrafluoroazobenzene-engineered covalent organic frameworks (COFs), where visible-light-mediated isomerization enables precise and reversible pore-size variation for adaptive enzyme confinement. This approach significantly enhances immobilization stability across diverse enzymes, improving the retention of horseradish peroxidase, cytochrome c, and laccase by 6.7-, 9.7-, and 1.8-fold, respectively. Mechanically locked formate dehydrogenase retained 99.2% activity after five cycles, surpassing most prior systems. In continuous-flow microreactors, productivity sustained over 22000 min, extending half-life 47-fold versus static-pore counterparts. Experimental and computational analyses reveal that synergistic pore compression and nanohands embedding during photoresponsive locking induce enzyme conformational restructuring and restricted residue mobility. This platform enables ultra-stable enzyme immobilization by orchestrating adaptive pore engineering with mechanically reinforced biocompatible interactions, unlocking broad potential for green biomanufacturing.
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