Abstract
The amount and mobility of «bound» water in neutral aqueous suspensions of a commercial soy protein isolate were quantitated by means of transverse and longitudinal 17 O NMR relaxation measurements. The hydration of the same protein isolate was investigated by 1 H NMR transverse relaxation measurements. Protein-protein interactions were quantitated by fitting the 1 H NMR data by a virial expansion. Transverse 1 H NMR relaxation rates showed a linear dependence on protein activity. Data interpretation was based on the effects of the NMR measurements of the ionization of protein groups, the state of protein aggregation, and the binding of salt by the protein
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