Premium
Effects of protein aggregation in isocratic nonlinear chromatography
Author(s) -
Whitley Roger D.,
Van Cott Kevin E.,
Berninger James A.,
Wang N.H. Linda
Publication year - 1991
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.690370409
Subject(s) - chemistry , myoglobin , dimensionless quantity , elution , chromatography , mass transfer , reaction rate , radius , scaling , thermodynamics , organic chemistry , catalysis , physics , geometry , computer security , mathematics , computer science
A versatile reaction‐separation (VERSE) model was developed to quantitatively simulate the behavior of chromatographic separations coupled with reactions. Detailed mass transfer and reaction mechanisms are considered. Aggregation data of myoglobin and β‐lactoglobulin A verified the model. The effects of concentration, equilibrium distribution, reaction rate, convection rate, particle radius, and relative affinity are shown for a dimerizing system. When the aggregation rate is relatively slow compared with convection and mass transfer rates, the individual forms behave as separate species in frontal, elution, and displacement chromatography. For rapid aggregation rates, the individual forms behave as a single component with an average affinity. The wave asymmetry and increased spreading due to aggregation depend on relative affinity differences. Serious error may result if aggregation is overlooked in parameter estimation using frontal or pulse analysis. The dimensionless group principles developed here are useful in scaling and predicting when peak or wave splitting or merging will occur in reaction chromatography systems.