Premium
Pulsed Low‐Resolution NMR Investigations of Protein Sols and Gels
Author(s) -
LAMBELET P.,
BERROCAL R.,
DESARZENS C.,
FROEHLICHER I.,
DUCRET F.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb08992.x
Subject(s) - relaxation (psychology) , chemistry , denaturation (fissile materials) , proton , gelatin , phase (matter) , analytical chemistry (journal) , whey protein , resolution (logic) , chromatography , nuclear chemistry , organic chemistry , psychology , social psychology , physics , quantum mechanics , artificial intelligence , computer science
Water proton transverse (T 2 ) relaxation measurements in whey, egg, gelatin, and soybean sols and gels were determined. T 2 relaxation 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/T 2 ) increased linearly with concentration of either protein or oil. For samples containing protein which underwent an irreversible denaturation upon heating, T 2 relaxation times were longer in the sols than in the gels. In gels, the variation of the T 2 relaxation times with temperature was interpreted in terms of an exchange between labile protein protons and water protons.