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Inhibition of glycinin thermal aggregation by an artificial chaperone sodium dodecyl sulphate
Author(s) -
Guo Jian,
Yang XiaoQuan,
Gu Wei,
Yuan DeBao,
Wang JinMei,
Wu NaNa
Publication year - 2012
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2011.02891.x
Subject(s) - chemistry , circular dichroism , protein aggregation , solubility , pulmonary surfactant , dynamic light scattering , sodium dodecyl sulfate , hydrophobic effect , sodium , ionic strength , soy protein , molecule , chromatography , aqueous solution , biophysics , chemical engineering , crystallography , organic chemistry , biochemistry , nanoparticle , engineering , biology
Summary Poor solubility caused by thermal aggregation usually limits the utilisation of soy proteins in food industry. In this study, the anionic surfactant, sodium dodecyl sulphate (SDS), was found to be effective in suppressing thermal aggregation of glycinin which was the main composition of the insoluble aggregates of soy proteins. Turbidity, dynamic light scattering, surface tension, circular dichroism and fluorescence spectra analysis were used to reveal the mechanism for the inhibitory of thermal aggregation by SDS. Bound to SDS, the exposed hydrophobic groups on the protein molecules were covered by the ionic head groups of SDS. The approaching of the particles was unavailable in the presence of the strong electrostatic repulsive force. Therefore, the particles remained stable and disperse. Thermal aggregation was not effectively suppressed until the binding sites which interacted with SDS on the glycinin molecules were saturated. The strategy for improving the solubility of food protein was also discussed.