Mathematical modeling of elution curves for a protein mixture in ion exchange chromatography and for the optimal selection of operational conditions.
Elution curves in ionic exchange chromatography (IEC) for a three-protein mixture (alpha-lactoalbumin, ovalbumin, and beta-lactoglobulin), carried out under different flow rates and ionic strength conditions, were simulated using two different mathematical models. These models were the Plate Model and the more fundamentally based Rate Model. Relatively low protein concentrations were used to avoid protein-protein interactions. Simulated elution curves were compared with experimental data not used for parameter identification. Deviation between experimental data and the simulated curves using the Plate Model was less than 0.0189 (absorbance units); a slightly higher deviation [0.0252 (absorbance units)] was obtained when the Rate Model was used. A cost function was built that included the effect of the different production stages, namely fermentation, purification, and concentration. These considered the effect on the performance of IEC; yield, purity, concentration and the time needed to accomplish the separation. Operational conditions in the IEC such as flow rate, ionic strength gradient and the operational time can be selected using this model in order to find the minimum cost for the protein production process depending on the characteristics of the final product desired such as purity and yield. This cost function was successfully used for the selection of the operational conditions as well as the fraction of the product to be collected (peak cutting) in IEC. It can be used for protein products with different characteristics and qualities, such as purity and yield, by choosing the appropriate parameters.
Shene
C
C
Department of Chemical Engineering, Universidad de la Frontera, Temuco, Chile. cshene@ufro.cl
Lucero
A
A
Andrews
B A
BA
Asenjo
J A
JA
D002852:Chromatography, Ion Exchange / Q000379:methods*; D007768:Lactalbumin / Q000737:chemistry / Q000302:isolation & purification; D007782:Lactoglobulins / Q000737:chemistry / Q000302:isolation & purification; D008962:Models, Theoretical; D010047:Ovalbumin / Q000737:chemistry / Q000302:isolation & purification; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D012984:Software; D012995:Solubility
D007782:Lactoglobulins; D011506:Proteins; D010047:Ovalbumin; D007768:Lactalbumin