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KINETICS OF HEAT COAGULATION OF EGG ALBUMIN DETERMINED BY WATER BINDING AND RHEOLOGICAL MEASUREMENTS
Author(s) -
GOLDSMITH SETH M.,
TOLEDO ROMEO T.
Publication year - 1985
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/j.1745-4549.1985.tb00724.x
Subject(s) - rheology , activation energy , viscoelasticity , arrhenius equation , chemistry , thermodynamics , kinetics , relaxation (psychology) , elastic modulus , heat capacity , analytical chemistry (journal) , phase (matter) , materials science , chromatography , composite material , organic chemistry , psychology , social psychology , physics , quantum mechanics
Dynamic testing of heat coagulated egg albumin revealed that phase angle, a measure of the fluidity of a viscoelastic material, exhibits a first order change during heating in a similar manner as the changes in the spin‐lattice relaxation time (T1) of water protons measured by a pulsed nuclear magnetic resonance instrument. The absolute modulus, on the other hand, which is an index of the elastic properties exhibited a zero order change in a similar manner as the development of gel strength measured by constant rate penetrometry using an Instron universal testing instrument. Arrhenius activation energy of 29 kcal/mole for the phase angle and 38.9 kcal/mole for the absolute modulus indicate that the process of protein‐water interaction to immobilize water within the gel and that of protein‐protein interaction to form the solid gel network occur simultaneously during heating, but they proceed by different mechanisms with the latter process showing greater heat sensitivity.