Adsorption Kinetics of Human Serum Albumin, β-Lactoglobulin and β-Casein at a Liquid/Liquid Interface

摘要

Equilibrium and dynamic interfacial tensions of proteins, human serum albumin, β-lactoglobulin and β-casein, at the water/chloroform interface have been measured, respectively, as a function of bulk concentration by the pendent drop technique. The isotherm used to interpret the equilibrium adsorption layers takes into consideration that protein molecules undergo a change in the molar interfacial area with changing interfacial pressure [1]. A theoretical model based on a diffusion-controlled mechanism analyzes the dynamic interfacial tension data. The model is developed such that it considers the same isotherm as used for the description of the equilibrium adsorption state [2]. For changes in the conformation of adsorbed proteins no extra rate constant has been considered so far. The results are compared with respective data obtained at the water/air and water/alkane interface [3].