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Kinetics of macromolecules adsorption on rigid porous particles

This thesis describes an experimental and theoretical study of the kinetics of myoglobin adsorption on recently introduced rigid, porous particles, Bakerbond Wide-Pore cation-exchange and Wide-Pore hydrophobic interaction adsorbents. Theoretical models have been developed and validated which described the adsorption kinetics of smaller protein molecules on polydisperse particles. The influence of various process parameters on the adsorption rate has also been investigated. Two modes of process operation have been studied, a stirred cell and a packed bed. A three-step model of the adsorption process involving extra-particle film mass transfer, intra-particle pore diffusion and surface reaction, has been formulated for monodisperse systems in a stirred cell. A two-step model, neglecting the surface reaction, has been developed for polydisperse particles in both stirred cell and packed-bed modes of operation. The main feature of the improved two-step model, compared with previous models, is the introduction of particle size distribution. Also considered in the two-step model is the mixing chamber effect in the stirred cell sampling loop and the packed bed inlet concentration profile. The validity of the models has been verified by applying the values of the pore diffusivity obtained from the stirred cell to predict the breakthrough curves in the packed bed operations. The introduction of particle size distribution has improved the fit between the experimental data and the simulation results. Adsorption isotherms of different systems have been obtained in the experiments. Also studied was the influence of various parameters on the adsorption isotherms, including solution pH, buffer type, salt concentration and particle size. The effects of particle size distribution, effective pore diffusivity and film mass transfer coefficient on adsorption rate have been examined by simulation and curve-fitting. The validated models and the data obtained on the adsorption systems studied provide a basis for predicting the performance of protein adsorption processes.

Identiferoai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:637902
Date January 1998
CreatorsLi, Q.
PublisherSwansea University
Source SetsEthos UK
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation

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