Characterization and Thermodynamic Behavior of Protein Adsorption on a Macroporous Monolithic Polymeric IMAC Matrix

Polymeric monolithic structures are efficient adsorbents for purifying biomolecules. In this study, cryogel of polyacrylamide was prepared and functionalized with IDA + Cu 2+ , and was evaluated as its structure. The studies of adsorption equilibrium were developed using bovine serum albumin as a model protein and analyzed using Langmuir model. The enthalpy and entropy of adsorption were calculated by van’t Hoff analysis. The microscopy analysis confirms the porosity of the cryogels. The results of the swelling capacity, degree of expansion, porosity and high permeability show the resistance to flow in the columns produced. The increase in the temperature at 328.15 K favored the adsorption process (q max equivalent to 205.478 mg BSA/g adsorbent) and the adsorption process occurred spontaneously (ΔG 0 ads ≤ − 12.140 kJ/mol) for all temperatures studied. In regard to albumin adsorption, an interesting feature of this study is that the column produced was stable to reuse cycles.