Studies on Egg Albumin Gelation Using Nuclear Magnetic Resonance

ABSTRACT Pulsed nuclear magnetic resonance was used to monitor the thermophysical transition of aqueous egg albumin dispersion. Gelling, which was manifested by an increase in force required to penetrate the surface of the dispersion, was accompanied by a decrease in T 1 , the spin‐lattice relaxation time of water protons in the dispersion. There was a high, negative correlation coefficient between gel strength and T 1 . Apparent rate kinetics of the transition was fist order for changes in T 1 and zero order for changes in gel strength, with activation energies for the rate constants of 42.62 and 43.68 kcal/mole, respectively.