Abstract
Theoretical and experimental investigations of the use of a Cloete-Streat contactor for ion exchange of amino acids are presented. A new step pH gradient approach was developed to concentrate and recover dilute components. For short cycles, the models have to include the supernatant fluid in between stages. Agreement between theory and experiment for phenylalanine separation was excellent for isocratic experiments but only fair with pH step gradients. Slow changes in internal pH were not included in the model and appear to be the reason for the lack of agreement between theory and experiment. For lysine separation, experimental concentration factors greater than 2.5 were obtained
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