Pulsed Low‐Resolution NMR Investigations of Protein Sols and Gels
- 1 May 1988
- journal article
- research article
- Published by Wiley in Journal of Food Science
- Vol. 53 (3) , 943-946
- https://doi.org/10.1111/j.1365-2621.1988.tb08992.x
Abstract
Water proton transverse (T2) relaxation measurements in whey, egg, gelatin, and soybean sols and gels were determined. T2 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/T2) increased linearly with concentration of either protein or oil. For samples containing protein which underwent an irreversible denaturation upon heating, T2 relaxation times were longer in the sols than in the gels. In gels, the variation of the T2 relaxation times with temperature was interpreted in terms of an exchange between labile protein protons and water protons.This publication has 20 references indexed in Scilit:
- Heat Gelation of Oil‐in‐Water Emulsions Stabilized by Whey ProteinJournal of Food Science, 1986
- Mobility of water in wheat flour suspensions as studied by proton and oxygen-17 nuclear magnetic resonanceJournal of Agricultural and Food Chemistry, 1986
- Studies on Egg Albumin Gelation Using Nuclear Magnetic ResonanceJournal of Food Science, 1985
- GelsScientific American, 1981
- AN ANALYSIS OF THE WATER BINDING IN GELSJournal of Food Science, 1979
- CHANGES IN SHEAR MODULUS, ULTRASTRUCTURE AND SPIN‐SPIN RELAXATION TIMES OF WATER ASSOCIATED WITH HEAT‐INDUCED GELATION OF MYOSINJournal of Food Science, 1979
- HEAT‐INDUCED GELATION OF PEANUT PROTEIN/WHEY PROTEIN BLENDSJournal of Food Science, 1978
- Steady‐state and pulsed NMR studies of gelation in aqueous agaroseBiopolymers, 1972
- Proton Magnetic Relaxation and Protein HydrationNature, 1963
- Proton Magnetic Resonance of the Water Phase of Gelatin GelsNature, 1960