TY - JOUR
T1 - Effects of carrageenan on thermal stability of proteins from chicken thigh and breast muscles
AU - Amako, Donatus E.N.
AU - Xiong, Youling L.
PY - 2001
Y1 - 2001
N2 - 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 (Tmax) of thigh myosin head and actin, while all three CGNs with or without 2.5% salt decreased (P < 0.05) Tmax 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.
AB - 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 (Tmax) of thigh myosin head and actin, while all three CGNs with or without 2.5% salt decreased (P < 0.05) Tmax 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.
KW - Carrageenan
KW - Chicken proteins
KW - Thermal stability
KW - Thigh and breast muscles
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U2 - 10.1016/S0963-9969(00)00161-7
DO - 10.1016/S0963-9969(00)00161-7
M3 - Article
AN - SCOPUS:0035086355
SN - 0963-9969
VL - 34
SP - 247
EP - 253
JO - Food Research International
JF - Food Research International
IS - 2-3
ER -