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Thermal Properties of Proteins in Chicken Broiler Tissues
Author(s) -
KIJOWSKI J.M.,
MAST M.G.
Publication year - 1988
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.1365-2621.1988.tb07706.x
Subject(s) - differential scanning calorimetry , enthalpy , myosin , chemistry , denaturation (fissile materials) , sarcoplasm , endothermic process , biochemistry , nuclear chemistry , thermodynamics , endoplasmic reticulum , physics , adsorption
The thermal behavior of breast and thigh muscles, blood and skin tissues of chicken broilers was evaluated by differential scanning calorimetry (DSC). Onset temperature of transition (T o ), maximum thermal transition (T max ) temperatures, and denaturation enthalpy (ΔH) were evaluated. Breast muscle exhibited a complex thermogram with five endothermic transitions at 57°C, 63°C, 67°C, 73°C, and 78°C at a heating rate of 10°C/min. Thigh muscle exhibited only three major transitions at 60°C, 66°C, and 76°C. Thermal curves of isolated protein fractions indicated that the thermal transitions in muscle corresponded to the denaturation of myosin, sarcoplasmic proteins, collagen and F‐actin. An increase in the heating rate from 1.0° to 40°C/min significantly elevated the onset temperature of transition and major transition temperatures, as well as the enthalpy of denaturation. Enthalpy of the muscle system heated to various end‐point temperatures, cooled and reheated, showed that myosin was completely denatured at 60°C, sarcoplasmic proteins at 70°C and actin at 80°C.