Aggregation of sodium dodecyl sulfate in micellar solution of beta-casein analyzed by ~1H NMR self-diffusion,relaxation and Fourier transform IR spectroscopy

摘要

Micellization of anionic sodium dodecyl sulfate (SDS) in the presence of beta-casein (beta-CN) miceles in aqueous media was studied by ~1H NMR and Fourier transform IR spectroscopy.At low concentrations SDS molecules incorporate into beta-CN micelles and modify the protein secondary structure,increasing the portion of helical domains.It was shown that SDS micelles do not appear until binding sites located in the hydrophobic core of beta-CN micelles are saturated.