Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.638406
Title: Ion exchange of proteins
Author: Pan, L. C.
Awarding Body: University College of Swansea
Current Institution: Swansea University
Date of Award: 1995
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Abstract:
The aims of the present work were to assess the nature and importance of the intermolecular and surface interactions in ion exchange processes at different conditions and also to develop a mathematical model for the prediction of equilibrium constants. The equilibrium uptake of two proteins (bovine serum albumin, myoglobin) on hydrophilic ion exchangers was studied at different pH values and ironic strengths. Equilibrium isotherm analysis allowed the determination of the thermodynamic equilibrium constants (K) for each condition. The affinity of the hydrophilic cellulosic ion exchanger (Whatman QA52) for bovine serum albumin was higher than for myoglobin. The maximum capacity of the ion exchanger was lower for BSA than for myoglobin under all comparable conditions. This behaviour is explained by considering the physical and chemical properties of the proteins and ion exchanger. The heats of exchange of the bovine serum albumin (BSA) at Whatman QA52 at different pH values were obtained by titration microcalorimetry (Thermometric 2277 Thermal Activity Monitor). An analysis procedure was developed to determine the standard thermodynamic functions (ΔG°, ΔH°, ΔS°) for each ion exchange process. Knowledge of these thermodynamic quantities provided further insight into the interactions that can occur during the ion exchange process. The analysis of thermodynamic data could help selection of the most effective means of manipulating process solution conditions to maximise the degree of separation. A colloid science approach for ion exchange of proteins has been developed based on electrostatic and London-van der Waals interaction energies. The approach allowed a priori prediction for the equilibrium behaviour of ion exchange of proteins at different conditions.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.638406  DOI: Not available
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