Modeling of scale-down effects on the hydrodynamics of expanded bed adsorption columns.
Expanded-bed adsorption (EBA) is a technique for primary recovery of proteins starting from unclarified broths. This process combines centrifugation, concentration, filtration, and initial capturing of the proteins in a single step. An expanded bed (EB) is comparable to a packed bed in terms of separation performance but its hydrodynamics are that of a fluidized bed. Downstream process development involving EBA is normally carried out in small columns to minimize time and costs. Our purpose here is to characterize the hydrodynamics of expanded beds of different diameters, to develop scaling parameters that can be reliably used to predict separation efficiency of larger EBA columns. A hydrodynamic model has been developed which takes into account the radial liquid velocity profile in the column. The scale-down effect can be characterized in terms of apparent axial dispersion, D(axl,app), and plate number, N(EB), adapted for expanded bed. The model is in good agreement with experimental results obtained from 1- and 5-cm column diameters with buffer solutions of different viscosities. The model and the experiments show an increase of apparent axial dispersion with an increase in column diameter. Furthermore, the apparent axial dispersion is affected by an increase in liquid velocity and viscosity. Supported by visual observations and predictions from the model, it was concluded that operating conditions (liquid viscosity and superficial velocity) resulting in a bed-void fraction between 0.7 and 0.75 would provide the optimal separation efficiency in terms of N(EB).
Fenneteau
Frédérique
F
Department of Chemical Engineering, Ecole Polytechnique, Montreal, Canada.
Aomari
Hafida
H
Chahal
Parminder
P
Legros
Robert
R
D000327:Adsorption; D002498:Centrifugation / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods*; D003198:Computer Simulation; D007475:Ion Exchange Resins; D008954:Models, Biological; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D015203:Reproducibility of Results; D012212:Rheology / Q000379:methods*; D012680:Sensitivity and Specificity; D012685:Sepharose; D014462:Ultrafiltration / Q000379:methods; D014783:Viscosity
D007475:Ion Exchange Resins; D011506:Proteins; D012685:Sepharose