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Apparent Specific Heat of Chicken Breast Patties and their Constituent Proteins by Differential Scanning Calorimetry
Author(s) -
MURPHY R.Y.,
MARKS B.P.,
MARCY J.A.
Publication year - 1998
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.1365-2621.1998.tb15682.x
Subject(s) - myofibril , sarcoplasm , differential scanning calorimetry , chemistry , denaturation (fissile materials) , endothermic process , chicken breast , food science , crystallography , biochemistry , thermodynamics , nuclear chemistry , endoplasmic reticulum , physics , adsorption
ABSTRACT Chicken breast meat yielded three endothermic transitions, with peak transition temperatures of 53,70, and 79°C. Comparison with the purified protein fractions indicated that these transitions corresponded to denaturation of myofibrillar (53°C) and sarcoplasmic (70 and 79°C) proteins. The apparent specific heat profile of chicken breast meat was successfully modeled as a weighted average of the apparent specific heat of the constituent proteins. The specific heats of sarcoplasmic protein, myofibrillar protein, and chicken breast meat were strongly influenced by temperature; however, the specific heat of stromal protein was nearly constant across the temperature range considered (i.e., 10 to 100°C).