Equilibrium and simulation of the operation for the adsorption of albumin proteins in an iminodiacetic-Cu bounded ion exchange resin (IMAC)

Abstract

IMAC (Immobilized Metal Affinity Chromatography) is one of most selective chromatographic techniques for protein retention. In this technique, a complexing resin containing, for example, iminodiacetic groups, is saturated with a metallic ion, and when the solution of proteins is contacted with the saturated resin; the affinity of the proteins for the metallic ions produces the retention of the protein by the support. In the present study, an iminodiacetic resin (Lewatit TP-207) was saturated with copper and the retention of bovine serum albumin and α-lactalbumin was tested. Equilibrium analysis was carried out in column, a constant separation factor isotherm being used to obtain the equilibrium constants. The kinetics was studied in batch experiments; a superficial mass transfer and a pore diffusion model were considered to obtain the mass transfer coefficient in the film and the pore diffusivity. The equilibrium is unfavorable and the kinetics very fast. Finally, breakthrough curves were obtained and modeled with a proposed column model taking into account equilibrium, kinetics and hydrodynamic parameters. The column model adequately fits the experimental breakthrough curves. This resin may be used to retain proteins from wastes from the food industry.