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Influence of sodium dodecyl sulfate on the characteristics of bovine serum albumin solutions and foams
Author(s) -
Wei Xiaofang,
Chang Zhidong,
Liu Huizhou
Publication year - 2003
Publication title -
journal of surfactants and detergents
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.349
H-Index - 48
eISSN - 1558-9293
pISSN - 1097-3958
DOI - 10.1007/s11743-003-0252-7
Subject(s) - chemistry , pulmonary surfactant , sodium dodecyl sulfate , bovine serum albumin , critical micelle concentration , surface tension , adsorption , chromatography , random coil , sodium , micelle , inorganic chemistry , organic chemistry , aqueous solution , circular dichroism , biochemistry , physics , quantum mechanics
Results from surface tension measurements on mixed solutions of the protein bovine serum alburnin (BSA) and an anionic surfactant (SDS: sodium dodecyl sulfate) suggested that at an air‐liquid interface, adsorption was affected by the protein‐surfactant interaction and by the relative concentration of each component in solution. Two plateaus corresponding to the critical aggregation concentration (CAC) and the critical micelle concentration (CMC) of SDS, respectively, were observed in the surface tension isotherms of SDS in the presence of BSA. The CAC and CMC depended on the concentration of BSA. Effects of SDS concentration on the conformational changes of BSA were investigated by Fourier transform‐Raman spectroscopy. The results showed that the contents of α‐helix decreased while the contents of random coil increased. The presence of the anionic surfactant SDS had a negative influence on the way that proteins adsorb at an air‐liquid interface, leading to the change of behavior of protein‐stabilized film.