Effects of carrageenan on thermal stability of proteins from chicken thigh and breast muscles

Thermal stability of ground chicken meat and myofibrillar proteins mixed with κ-, ι-, and λ-carrageenan (CGN) at different NaCl concentrations was investigated with differential scanning calorimetry. Three transitions, characteristic of myosin head (63.3, 62.2°C), sarcoplasmic proteins/myosin tail (67.7, 68.6°C), and actin (78.3, 81.4°C), were observed for nontreated thigh and breast muscles, respectively. The influence of CGNs on the thermal transitions was dependent on salt concentrations. κ-CGN with 2.5% NaCl decreased (P < 0.05) transition temperature (T_max) of thigh myosin head and actin, while all three CGNs with or without 2.5% salt decreased (P < 0.05) T_max for breast actin. Total enthalpy of denaturation decreased slightly in the presence of κ-CGN for thigh muscles only. The gum effects on myofibril isolates were variable and were salt-dependent. The results suggested molecular interactions between the gums and meat proteins, but the response of the specific proteins to gums appeared to be muscle type-dependent.