EQUILIBRIUM AND KINETIC-PARAMETERS OF THE ADSORPTION OF ALPHA-CHYMOTRYPSINOGEN-A ONTO HYDROPHOBIC POROUS ADSORBENT PARTICLES

Adsorption equilibria and rate kinetics for the binding of alpha-chymotrypsinogen A onto hydrophobic porous adsorbent particles, have been investigated for three different temperatures. The results show that the amount of protein adsorbed increases as the temperature increases. The values of the parameters that characterize the mechanisms of pore diffusion and adsorption were determined. The values of the pore diffusion coefficient and the values of the time constants for the mass transfer steps of pore diffusion and adsorption suggest that the pore diffusion mechanism in the porous structure of the adsorbent particles is rate limiting. An analysis of the results of the adsorption of alpha-chymotrypsinogen A suggests that the heat of adsorption is positive, and this would indicate that the adsorption of alpha-chymotrypsinogen A onto the hydrophobic adsorbent particles used in this work is entropically driven.