A thermodynamic study of the binding of human serum albumin onto N,N′-diethylaminoethyl dextran microbeads

Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensors, cardiovascular implants, and chromatography. Adsorption thermodynamics has been studied on the microbeads of N,N′- diethylaminoethyl (DEAE) Dextran anion exchanger for the human serum albumin (HSA) at 25, 30, 35, 40, and 45°C. As a result, some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant (K _D), standard free energy changes (ΔG_assoc), standard entropy changes (ΔS_assoc), and standard enthalpy change (ΔH_assoc) have been evaluated. Using the linear Van't Hoff plot, ΔH_assoc value of the system for the interaction of bovine serum albumin (BSA)-adsorbed crosslinked DEAE dextran microbeads was determined as 20,650 kJ/mol.