Interfacial properties (surface tension, σ, and critical micelle concentration, CMC) of aqueous solutions of Tween 20 (polyoxyethylene sorbitan monolaurate) and/or bovine serum albumin (BSA) were evaluated. Temperature, Tween 20 concentration in the aqueous phase, BSA/Tween 20 ratio, and aqueous phase composition [water, ethanol (0.5, 1.0, and 2.5 M), and sucrose (0.5 M)] were the variables studied. The CMC of Tween 20 was determined by surface tension measurements (Wilhelmy plate method). The existence of BSA-Tween 20 interactions was deduced from surface tension measurements. The results show that the effect of temperature on CMC depends on the aqueous phase composition, but the σ value at CMC, σ CMC , does decrease as temperature is increased. The CMC and σ CMC values also depend on the aqueous phase composition. In aqueous ethanol solutions, the CMC increases, but σ CMC decreases. However, in sucrose aqueous solutions, the CMC decreases, but there is no significant effect on σ CMC . The BSA-Tween 20 interactions at the interface depend on both Tween 20 concentration (C ) and solute in the bulk phase. In water and aqueous solutions of ethanol and sucrose, σ values decrease in the presence of protein at C < CMC but are practically independent of C at C > CMC. This is an indication that the interfacial characteristics of the mixed film are determined by either the protein or the lipid at the higher and lower protein/lipid ratio, respectively. In the intermediate region, the existence of BSA-Tween 20 interactions dominates the interfacial characteristics of mixed films.The formation of stable colloidal dispersions (emulsions, foams, etc.) is extremely important in the paint, petroleum, cosmetic, pharmaceutical, and food industries (1-3). Significant economic waste arises from the manufacture of unstable foams and emulsions. The chemical and physical properties of surface-active molecules are of great interest because they determine the colloidal stability of dispersed particles (4). Proteins stabilize foams and emulsions by forming a mechanical barrier at the interface that encapsulates the dispersed phase and resists random surface perturbations, droplet coalescence, or flocculation (5). The barrier is formed as intermolecular interactions between the adsorbed protein molecules are established. These contribute significantly to the rheological properties of the barrier and immobilize proteins in the adsorbed layer. In contrast, lipids stabilize the dispersed droplet or bubble by formation of a densely packed monomolecular layer, which is stabilized by Gibbs-Marangoni mechanisms (6). However, the presence of proteins and lipids in the same systems can result in instability as both types of surface-active molecules compete to form different types of adsorbed layers (immobile vs. mobile) (7). The distribution of proteins and lipids in food emulsions and foams is determined by competitive and cooperative adsorption between the two types of emulsifiers at the fluid-fluid interfaces, and by the nature of protein-lipi...