ABSTRACT
Interactions of surfactants with proteins are of importance in a wide variety of industrial, biological, pharmaceutical, and cosmetic systems. The evidence for the existence of protein-surfactant complexes has come from indirect methods such as surface tension, rheology, and dye solubilization, and from direct measurements of binding by dialysis and gel filtration and the use of ion-selective electrodes. Boundary tension is a simple and useful method to study interactions between a surfactant and relatively non-surface active component such as a protein or polymer. As for simple polymers, interactions of proteins with ionic surfactants can result in significant changes in their rheological properties. Information on the nature of protein-surfactant aggregates can be obtained from dye solubilization and fluorescence probe studies. The amount of surfactant bound to the protein is usually expressed in terms of moles of surfactant bound per mole of protein. The initial sharp rise has been attributed to binding to high-affinity sites on the protein.
