Colloids Surf B Biointerfaces. 2026 Apr 10;265:115704. doi: 10.1016/j.colsurfb.2026.115704. Online ahead of print.
ABSTRACT
Enzyme immobilization is crucial for industrial biocatalysis but is fundamentally limited by an inherent activity-stability trade-off, where rigid protective supports often compromise catalytic efficiency through severe diffusion barriers or denaturation. To address this challenge, we developed a bioinspired “nanoarmor” via interfacial assembly on polyethylenimine-functionalized styrene maleic anhydride nanospheres (PEI-SMA). Initially, crude sucrose synthase was immobilized through electrostatic adsorption onto cationic PEI-SMA surfaces, effectively bypassing purification and mitigating denaturation caused by subsequent precursor ions. A synergistic PEI-sodium alginate (SA) system then enabled protective coating formation: PEI pre-configured the reaction sites by coordinating Zn2 + at the nanosphere interface, while SA induced instantaneous nucleation via biomimetic coordination with substoichiometric 2-methylimidazole (2-MeIm). This dual-control strategy, combining non-equilibrium ligand ratios with rapid nucleation kinetics, suppressed crystal growth and directed conformal amorphous ZIF deposition (PEI-SMA@enzyme-Sazif). This core-shell colloidal architecture circumvents diffusion limitations via its amorphous matrix while ensuring superior stabilization. The biocatalyst exhibited high activity retention (71.4%) and favorable reusability (75.7% after 5 cycles), outperforming PEI-SMA@enzyme. Furthermore, it showed significantly enhanced environmental stability, exhibiting 2.6-fold and 1.3-fold higher residual activity than the free enzyme after incubation at 60 °C and pH 5.5 for 60 min, respectively. This work illustrates how rational design of colloidal biointerfaces and interfacial biomineralization pathways can reconcile the stability-activity dilemma, enabling efficient and stable biocatalysis directly from crude enzyme extracts.
PMID:41980360 | DOI:10.1016/j.colsurfb.2026.115704