Authors
Wanzheng Wu, Yikang Lu, Aitao Li, Yuxia Pang, Hongming Lou, Xueqing Qiu, Zhixian Li
Published in
ACS applied materials & interfaces. Sep 14, 2026. Epub Sep 14, 2026.
Abstract
Controlling the conformation and orientation of enzymes at solid interfaces is a central challenge in the design of functional biohybrid materials, and the outcome depends sensitively on the chemistry and geometry of the enzyme-support interface. Here, a β-ketoester-functionalized keto-enamine covalent organic framework (COF) is developed as a structurally defined support for arginine-directed immobilization of unspecific peroxygenase (UPO). The crystalline periodicity and post-synthetic addressability of the COF lattice enable precise placement of anchoring groups at the enzyme-support interface. The grafted β-ketoester groups react with surface arginine residues under mild aqueous conditions, forming a robust covalent linkage without external activating agents or toxic cross-linkers. Compared with physical adsorption and lysine-directed epoxy coupling, the arginine-directed strategy offers higher enzyme loading, reduced leaching, and improved reusability, while raising the catalytic efficiency (kcat/KM) toward ABTS oxidation 1.8-fold. Spectroscopic and molecular dynamics analyses indicate that arginine-directed anchoring rigidifies the enzyme and biases the heme channel toward a more open average geometry, offering a structural rationale for the enhanced turnover. The immobilized UPO also shows improved productivity in representative hydroxylation, sulfoxidation, and halogenation reactions. These results establish the identity of the anchoring residue as a tunable interfacial design parameter for COF-supported biocatalytic materials.
PMID:
42728243
Bibliographic data and abstract were imported from PubMed on 12 Sep 2026.
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