Experimental and theoretical study of the adsorption behavior and mass transfer kinetics of propranolol enantiomers on cellulase protein as the selector.
The thermodynamics and mass transfer kinetics of the retention of the R and S enantiomers of propranolol were investigated on a system comprising an acetic acid buffer solution as the mobile phase and the protein cellobiohydrolase I immobilized on silica as the stationary phase. The bi-Langmuir isotherm model fitted best to each set of single-component isotherm data. The monolayer capacity of the nonchiral type of adsorption sites was 22.9 mM. For the chiral type of sites, it was 0.24 mM for the R enantiomer and 0.64 mM for the S enantiomer. Peak tailing was observed, even at very low concentrations allowing operation of the low-capacity chiral sites under linear conditions. This tailing can be explained on the basis of heterogeneous mass transfer kinetics. At higher concentrations, which are often used in analytical applications, the isotherms on the chiral sites no longer have a linear behavior, and peak tailing is consequently more pronounced. Under those conditions, peak tailing originates from the combined effect of heterogeneous thermodynamics and heterogeneous mass transfer kinetics. These complex phenomena are explained and modeled using the transport-dispersive model with a solid film linear driving force model modified to account for heterogeneous mass transfer kinetics. The rate coefficient of the mass transfer kinetics was found to be concentration dependent.
Fornstedt
T
T
Department of Chemistry, University of Tennessee, Knoxville 37996-1600, USA.
Zhong
G
G
Bensetiti
Z
Z
Guiochon
G
G
D000327:Adsorption; D002480:Cellulase / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D007700:Kinetics; D008956:Models, Chemical; D011433:Propranolol / Q000737:chemistry*; D013237:Stereoisomerism; D013816:Thermodynamics
D011433:Propranolol; D002480:Cellulase