RESUMO
Understanding the interactions between surfactants and proteins is important for the formulation of consumer products as surfactant binding can alter protein activity and stability. Additionally, the structure of the protein-surfactant complex can influence surface activity, which is important for emulsion and foam development. N,N-Dimethyldodecylamine N-oxide (DDAO) is an amphoteric surfactant that is nonionic at high pH. It is often used as a foam booster in detergent formulations and for the extraction of membrane proteins. In this study, a variety of biophysical characterization methods was used to investigate the impact of DDAO at pH 8 on the structure of the globular protein ß-lactoglobulin (ßLG). Pyrene fluorescence and surface tension studies show that ßLG had minimal impact on the critical micelle concentration (CMC) of DDAO, while fluorescence and circular dichroism spectroscopy found unfolding of ßLG at concentrations of DDAO greater than the CMC. Small-angle X-ray scattering results confirm changes in the structure of ßLG at DDAO concentrations above the CMC. Taken together, DDAO behaves like nonionic and zwitterionic surfactants below its CMC with limited interaction with ßLG, while it induces protein unfolding at concentrations higher than the CMC, resulting in a protein-surfactant complex structure that resembles a protein-decorated micelle.