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Thermostability of Hen Egg Yolk Granules: Contribution of Native Structure of Granules
Author(s) -
Anton M.,
Denmat M. Le,
Gandemer G.
Publication year - 2000
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.1365-2621.2000.tb16052.x
Subject(s) - solubility , chemistry , phosvitin , thermostability , granule (geology) , denaturation (fissile materials) , yolk , chromatography , sodium , viscosity , biochemistry , food science , organic chemistry , nuclear chemistry , biology , materials science , paleontology , protein kinase a , composite material , enzyme
ABSTRACT: To understand why protein granules resist heat treatment, we measured denaturation, viscosity, and solubility of heated native and disrupted granules and estimated the effect on their emulsifying ability. Granule disruption by sodium chloride caused protein solubility to drop dramatically and viscosity to rise sharply above 72° C. Solubility of native granules was unaffected by heat, and viscosity increased slightly. Electrophoresis revealed that, whatever the granules structure, low‐density lipoproteins (LDL) and α‐high‐density lipoproteins (α‐HDL) were denatured, whereas phosvitin and β‐HDL were resistant to heat. Disrupted granules provided weaker emulsifying ability than native granules. The structure of native granules cannot prevent protein denaturation but can avoid aggregation of LDL and α‐HDL from different granules.