Pulsed Low‐Resolution NMR Investigations of Protein Sols and Gels

摘要

ABSTRACTWater proton transverse (T2) relaxation measurements in whey, egg, gelatin, and soybean sols and gels were determined. T2relaxation in protein sols and gels was a single exponential process, except for oil containing sols which showed a two‐phase behavior. The relaxation rates (1/T2) increased linearly with concentration of either protein or oil. For samples containing protein which underwent an irreversible denaturation upon heating, T2relaxation times were longer in the sols than in the gels. In gels, the variation of the T2relaxation times with temperature was interpreted in terms of an exchange between labile protein protons and water proton