Research Information System
Separation Science and Technology (Philadelphia), vol.61, no.7, pp.1077-1090, 2026 (SCI-Expanded, Scopus)
In this study, poly(hydroxyethyl methacrylate) (poly(HEMA))-based macroporous microscale cryogels (microcryogels) were synthesized and functionalized with N-methacryloyl-(L)-cysteine methyl ester (MAC) to develop an efficient adsorbent for immunoglobulin G (IgG) purification via immobilized metal affinity chromatography (IMAC). The MAC groups were coordinated with Ni2+ ions to introduce specific binding sites for IgG molecules. The prepared microcryogels exhibited highly interconnected macroporous structures, enabling rapid mass transport and effective protein adsorption. Structural and morphological characterization of the microcryogels was performed using scanning electron microscopy (SEM), energy-dispersive X-ray spectroscopy (EDX), Fourier-transform infrared spectroscopy (FT-IR), and X-ray photoelectron spectroscopy (XPS). Adsorption studies demonstrated a high IgG binding capacity of 53.05 mg·g−1, with a relative standard deviation (RSD) of 6.05%, indicating reproducibility. Selectivity experiments conducted using bovine serum albumin (BSA) and plasma proteins confirmed the high specificity of the microcryogels for IgG. This finding was further supported by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis. These results suggest that Ni2+-coordinated poly(HEMA-MAC)-Ni(II) microcryogels offer a promising platform for the selective separation and purification of IgG molecules.