Effect of Sodium Chloride and Phosphates on the Thermal Properties of Chicken Meat Proteins

Maximum thermal transition (T max ) and denaturation enthalpy (ΔH) of water‐washed myofibrils and finely cut chicken breast muscle, treated with 1–4% NaCl and/or 0.25–1% of either pyrophosphate (PP) or tripolyphosphate (TPP), were monitored by differential scanning calorimetry. Increasing the concentration of NaCl destabilized the heat resistance of the proteins in water‐washed myofibrils and in meat specimens. Actin showed the greatest reduction of T max , a 16°C decline in the presence of 4% NaCl. In a meat system, the addition of 4% NaCl resulted in one T max instead of five transitions, as seen in untreated meat. The presence of PP and TPP, especially in concentrations of 0.25 and 0.50%, enhanced the thermal stability of myosin. Changes in denaturation temperatures of proteins were accompanied by corresponding changes in AH.