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-chymo trypsinogen A onto hydrophobic porous adsorbent particles, have been i nvestigated for three different temperatures. The results show that th e amount of protein adsorbed increases as the temperature increases. T he values of the parameters that characterize the mechanisms of pore d iffusion and adsorption were determined. The values of the pore diffus ion coefficient and the values of the time constants for the mass tran sfer steps of pore diffusion and adsorption suggest that the pore diff usion mechanism in the porous structure of the adsorbent particles is rate limiting. An analysis of the results of the adsorption of alpha-c hymotrypsinogen A suggests that the heat of adsorption is positive, an d this would indicate that the adsorption of alpha-chymotrypsinogen A onto the hydrophobic adsorbent particles used in this work is entropic ally driven.