Nat Commun. 2026 Jul 7. doi: 10.1038/s41467-026-75314-z. Online ahead of print.

ABSTRACT

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.

PMID:42414308 | DOI:10.1038/s41467-026-75314-z