Sorption kinetics and breakthrough curves for pepsin and chymosin using pepstatin A affinity membranes.
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.
Suen
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SY
Department of Chemical Engineering, University of Wisconsin, Madison 53706-1619.
Etzel
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MR
D000327:Adsorption; D012085:Chymosin / Q000737:chemistry*; D007700:Kinetics; D008567:Membranes, Artificial; D010434:Pepsin A / Q000737:chemistry*; D010436:Pepstatins / Q000737:chemistry*; D012996:Solutions
D008567:Membranes, Artificial; D010436:Pepstatins; D012996:Solutions; C014195:Streptomyces pepsin inhibitor; D010434:Pepsin A; D012085:Chymosin; C031375:pepstatin