DETERMINATION OF LUMPED RATE COEFFICIENTS OF PROTEINS - EFFECT OF ADSORPTION

The equilibria and kinetics of adsorption of lysozyme and bovine serum albumin on the Fractogel-EMD tentacle-type cation exchanger and the F ractogel-TSK conventional cation exchanger have been studied experimen tally by batch stirred-tank methods. Adsorption equilibrium data corre sponded well to the Langmuir isotherm. For both proteins, the tentacle -type exchanger exhibited a higher binding capacity than the conventio nal exchanger. This is attributed to the flexibility of the functional groups in the tentacle-type exchanger which enhances optimal electros tatic interactions. The dynamic data were analyzed by a simplified rat e model which lumped mass transfer resistances and intrinsic adsorptio n kinetics into a single rate constant. For both proteins, it was foun d that the tentacle-type exchanger showed a smaller lumped rate coeffi cient than the conventional exchanger. The difference in the values of the lumped rate coefficients was shown to be due to the influence of nonlinear equilibrium constants rather than due to any difference in r ate of adsorption.