Apparent specific heat of chicken breast patties and their constituent proteins by differential scanning calorimetry

Chicken breast meat yielded three endothermic transitions, with peak transition temperatures of 53, 70, and 79 degrees C. Comparison with the purified protein fractions indicated that these transitions corresponded to denaturation of myofibrillar (53 degrees C) and sarcoplasmic (70 and 79 degrees C)...

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Bibliographic Details
Published in:Journal of food science 1998-01, Vol.63 (1), p.88-91
Main Authors: Murphy, R.Y. (University of Arkansas, Fayetteville, AR.), Marks, B.P, Marcy, J.A
Format: Article
Language:English
Subjects:
ALIMENTOS
ANIMAL TISSUES
Biological and medical sciences
CALOR ESPECIFICO
CARNE DE POLLO
CHALEUR SPECIFIQUE
CHICKEN MEAT
DENATURATION
DESNATURALIZACION
differential scanning calorimetry
FIBRAS MUSCULARES
FIBRE MUSCULAIRE
Food industries
Food science
FOODS
Fundamental and applied biological sciences. Psychology
Heat
Meat and meat product industries
MUSCLE
MUSCLE FIBRES
MUSCLE PROTEINS
MUSCLES
MUSCULOS
MYOFIBRILLAR PROTEINS
MYOFIBRILS
Poultry
PRODUIT ALIMENTAIRE
protein
PROTEINAS
PROTEINE
PROTEINS
SARCOMERES
SARCOPLASMIC PROTEINS
Scientific imaging
SPECIFIC HEAT
STROMAL PROTEINS
TEJIDOS ANIMALES
TISSU ANIMAL
VIANDE DE POULET
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Description
Summary:Chicken breast meat yielded three endothermic transitions, with peak transition temperatures of 53, 70, and 79 degrees C. Comparison with the purified protein fractions indicated that these transitions corresponded to denaturation of myofibrillar (53 degrees C) and sarcoplasmic (70 and 79 degrees 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 degrees C)
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.1998.tb15682.x