Kinetics of adsorption of denatured protein at alumina-water interface.

The kinetics of adsorption of soluble denatured protein, gelatin has been studied at the alumina-water interface as a function of protein concentration, pH, temperature and ionic strength. The rate of adsorption of gelatin has been compared with rate of adsorption of BSA denatured by 8 M urea or 0.05 M SDS. The initial stage for the adsorption process is diffusion-controlled and the surface diffusion coefficients evaluated from equations of Ward and Tordai and by Bull for globular and denatured proteins are found to be widely different from each other. The kinetic data for gelatin fit into a first order rate equation with two rate constants, k1a and k2a. Using Arrhenius equation, the activation energies delta E1* and delta E2* have been evaluated from the values of k1a and k2a respectively. The corresponding changes in values of enthalpy of activation (delta H*), entropy of activation (delta S*) and free energy of activation (delta G*) have been evaluated using Eyring's equation for absolute reaction rate. It has been found that for both gelatin and denatured BSA, in the first kinetic step delta H1* > T delta S1* and for the second step T delta S2* > delta H2.