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