Preparation of lysozyme-imprinted mesoporous Zr-based metal-organic frameworks with remarkable specific recognition

The development of high-performance protein-imprinted materials remains challenging due to defects con-cerning high mass transfer resistance and non-specific binding, which are crucial for protein purification and enrichment. In this paper, lysozyme-imprinted mesoporous Zr-based MOF (mesoUiO-66-NH2@MIPs) with spe-cific and selective recognition of lysozyme (Lyz) were prepared by surface imprinting technology. In particular, the excellent hydrophilicity mesoporous MOFs (mesoUiO-66-NH2) with a pore size of 10 nm was prepared as a carrier for Lyz immobilization by an auxiliary modulation strategy to regulate the microporous structure of UiO-66-NH2 with the propionic acid solution, enabling massive loading of the macromolecular protein Lyz. The mesoUiO-66-NH2@MIPs reached a maximum saturation adsorption of 206.54 mg g-1 on Lyz in 20 min at 25 degrees C with an imprinting factor of 2.57 and selection factors of 2.02, 2.34, and 2.45 for cytochrome c (Cyt c), bovine serum albumin (BSA) and bovine hemoglobin (BHb), respectively. More importantly, the mesoUiO-66-NH2@MIPs could specifically recognize Lyz from the mixed protein system. The adsorption capacity of Lyz could still reach 78.55% after 5 cycles with good cyclic regeneration performance. This provides a new research option for developing and applying novel porous MOF in biomolecule imprinting technology and the specific separation of biomolecules.

Automated summary

In this study, lysozyme-imprinted mesoporous Zr-based MOF (mesoUiO-66-NH2@MIPs) with specific recognition of lysozyme (Lyz) was prepared using surface imprinting technology. The mesoUiO-66-NH2@MIPs showed excellent hydrophilicity and high loading capacity for macromolecular protein Lyz, and could specifically recognize Lyz from mixed protein systems.