Abstract

In this study, the application of chelating resin Amberlite IRC-748 as ion-exchange absorbent for separation of bovine serum albumin ( BSA ) and bovine hemoglobin ( BHb ) mixture. The effects of pH, temperature and salt concentration on single protein adsorption and thermodynamics were investigated. Furthermore, separation factor and the kinetics properties of binary protein system were also investigated with adsorption process. Finally, it was discussed with desorption conditions. For both proteins, amount of adsorption was higher at low pH values. The results show that the amount of protein adsorbed increases as the temperature and salt concentration increase. In addition, the adsorption isotherms well fitted by the Langmuir isothermal model from the semi-reciprocal plot analysis. Utilizing Van’t Hoff relationships to analyze the experimental data for these interactions, the change in the apparent enthalpy of association for the adsorption of BSA and BHb onto IRC-748 was positive. In binary protein adsorption experiment, it could be separated completely at 40oC, pH 4.0 with 0.2 M NaCl. However, the condition at 40oC, pH 5.0 with 0.2 M NaCl showed the best adsorption selectivity. It has shown that adsorption behavior with competitive phenomenon when using the three competitive adsorption models in binary component system. In order to investigate the mechanism of adsorption and potential rate controlling step, first- and second-order kinetic equations, intraparticle diffusion model and external film mass transfer model have been used for testing experimental data. Adsorption of both proteins is best fit by second-order kinetic equation. In these adsorption conditions, the adsorption mechanism of BSA is external film diffusion controlling and BHb can be best described by intraparticle diffusion model. Aspect to desorption experiment, by using modified pH value will find that the desorption percentage of protein which adsorb at low temperature will better than high temperature.

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