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

Citation
E. Arevalo et al., Equilibrium and simulation of the operation for the adsorption of albumin proteins in an iminodiacetic-Cu bounded ion exchange resin (IMAC), SEP PURIF T, 18(3), 2000, pp. 217-225
Citations number
17
Categorie Soggetti
Chemical Engineering
Journal title
SEPARATION AND PURIFICATION TECHNOLOGY
ISSN journal
13835866 → ACNP
Volume
18
Issue
3
Year of publication
2000
Pages
217 - 225
Database
ISI
SICI code
1383-5866(20000501)18:3<217:EASOTO>2.0.ZU;2-X
Abstract
IMAC (Immobilized Metal Affinity Chromatography) is one of most selective c hromatographic techniques for protein retention. In this technique, a compl exing resin containing, for example, iminodiacetic groups, is saturated wit h a metallic ion, and when the solution of proteins is contacted with the s aturated resin; the affinity of the proteins for the metallic ions produces the retention of the protein by the support. In the present study, an imin odiacetic resin (Lewatit TP-207) was saturated with copper and the retentio n of bovine serum albumin and alpha-lactalbumin was tested. Equilibrium ana lysis was carried out in column, a constant separation factor isotherm bein g used to obtain the equilibrium constants. The kinetics was studied in bat ch experiments; a superficial mass transfer and a pore diffusion model were considered to obtain the mass transfer coefficient in the film and the por e diffusivity. The equilibrium is unfavorable and the kinetics very fast. F inally, breakthrough curves were obtained and modeled with a proposed colum n model taking into account equilibrium, kinetics and hydrodynamic paramete rs. The column model adequately fits the experimental breakthrough curves. This resin may be used to retain proteins from wastes from the food industr y. (C) 2000 Elsevier Science B.V. All rights reserved.