Investigation of Isotherm, Thermodynamic, and Kinetics of Bovine Serum Albumin Adsorption onto MCM-41@LDH

The survey of protein adsorption is important due to significant application of proteins in food, medicine, biotechnology, environment, and separation science. Therefore, in the current investigation, the adsorption of bovine serum albumin (BSA) onto a functionalized mesoporous (MCM-41) using layered double hydroxide (MCM-41@LDH) was investigated under different conditions such as the amount of adsorbent, pH of the solution, contact time, and protein concentration. The optimization process was carried out using central composite design (CCD). After characterization of modified mesoporous, more investigations were conducted to assess the adsorption of BSA onto MCM-41@LDH, including adsorption isotherm, kinetics, and thermodynamic. It was revealed that Freundlich isotherm and second-order kinetics provided the best fit for support of MCM-41@LDH. The values of Gibbs free energy (ΔG°), enthalpy (ΔH°), and entropy (ΔS°) were determined as -3100.47 kJ mol-1 K-1 (at 298.15 K), -3101.12 kJ mol-1, and -0.002 kJ mol-1, respectively. According to CCD analysis and desirability function of 1.0, the optimal conditions for BSA adsorption were determined to be a pH value of 4.50, BSA concentration of 250 mg L-1, support amount of 0.016 g, and contact time of 55 min. The obtained findings can be used for purification, separation, and removal of BSA from complex samples.