Influence of amphiphiles on surface energy (γ), emulsifying activity index (EAI) and emulsion stability (ES) of fatty-acid free bovine serum albumin (FAF-BSA), bovine serum albumin (BSA), and β-lactoglobulin A (β-LGA) was studied. Contact angle measurements (θ) of sessile drops of protein-surfactant mixtures were determined using water and α-bromonaphthalene as solvents of known parameters to calculate γ. All surfactants except zwitterionic Z8 increased γ. The greatest increase was by anionic SDS. All surfactants significantly reduced EAI in spite of increased γ. ES was reduced by all surfactants except cationic TDTM which, conversely, enhanced ES by up to 186% for BSA and β-LGA.