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A Study of the Denaturation of Egg White Proteins during Freezing Using Differential Scanning Calorimetry
28
Citations
5
References
1981
Year
Food ChemistryProtein ChemistryBiochemistryProtein FoldingMedicineBioanalysisFoam InstabilityFood BiophysicsEgg White ProteinsFood EngineeringFood ProcessingThermodynamicsThermal ProcessingProtein RefoldingFoam Specific GravityStorage TimeBiophysicsHealth Sciences
ABSTRACT Differential Scanning Calorimetry was used to determine the effect of freezing rate, thawing conditions, storage time, and storage temperature on the enthalpy of denaturation of frozen egg white. Viscosity, foam specific gravity and foam instability of the product were also determined. Loss of enthalpy of denaturation was increased by slower freezing rates, higher thawing temperatures, higher storage temperatures, and longer storage times. Conalbumin suffered greater losses, and ovalbumin smaller losses, than egg white itself. Changes in egg white viscosity, foam specific gravity and foam instability varied depending on the processing variable tested and had no clear‐cut relation with losses in enthalpy of denaturation.
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