Ion exchange of amino acids at a natural organic ion exchanger: Thermodynamics and energetics.
The thermodynamics and energetics of the ion exchange of four amino acids at a cellulosic ion exchanger have been studied. Experimental work included determination of ion exchange isotherms and the use of high-sensitivity titration microcalorimetry. A rigorous thermodynamic analysis of the data was developed allowing calculation of the standard free energy, the standard enthalpy, and standard entropy of exchange, and also the differential free energy, incremental enthalpy, and incremental entropy of exchange. The results show that the relative contributions of the enthalpy and entropy to the overall free energy differ markedly for the chosen amino acids. The reasons for these differences are analyzed and discussed. A knowledge of these fundamental thermodynamic properties indicates the solution conditions likely to give enhanced affinity of the ion exchanger for selected amino acids. The experimental techniques and analysis procedures developed are generally applicable to ion exchange separations of biomolecules. (c) 1995 John Wiley & Sons, Inc.
Bowen
W R
WR
Biochemical Engineering Group, Department of Chemical Engineering, University of Wales, Swansea SA2 8PP, United Kingdom.
Moran
E B
EB