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J Chromatogr A. 1994 Dec 2;686(2):179-92.

Sorption kinetics and breakthrough curves for pepsin and chymosin using pepstatin A affinity membranes.

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  • 1Department of Chemical Engineering, University of Wisconsin, Madison 53706-1619.


Isotherms and kinetic parameters for pepsin and chymosin sorption to immobilized pepstatin A were measured in batch experiments. The measured single-solute parameters were used in an affinity-membrane model which included competitive sorption kinetics, axial diffusion and dead volume mixing. The predictions made using the affinity-membrane model matched the experimental breakthrough curves, whereas predictions made using local-equilibrium theory were a distinct mismatch. The performance of affinity-membrane separations was dominated by slow sorption kinetics.

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