Quantitative description of the parameters affecting the adsorption behaviour of globular proteins

The adsorption behaviour of proteins depends significantly on their molecular properties and system conditions. To study this relation, the effect of relative exposed hydrophobicity, protein concentration and ionic strength on the adsorption rate and adsorbed amount is studied using β-lactoglobulin, ovalbumin and lysozyme. The curves of surface elastic modulus versus surface pressure of all three proteins, under different conditions (i.e. concentration and ionic strength) superimposed. This showed that the interactions between the adsorbed proteins are similar and that the adsorbed proteins retain their native state. In addition, the adsorption rate (kadsorb) was shown to scale with the relative hydrophobicity and ionic strength. Moreover, the adsorbed amount was shown to be dependent on the protein charge and the ionic strength. Based on these results, a model is proposed to predict the maximum adsorbed amount (Γmax). The model approximates the adsorbed amount as a close-packed monolayer using a hard-sphere approximation with an effective protein radius which depends on the electrostatic repulsion. The theoretical adsorbed amount was in agreement with experimental Γmax (±10%).