Studies on the thermal denaturation of meat proteins by differential scanning calorimetry
1987
Kim, Y.H. (Sunchoun National Univ., Sunchoun (Korea R.))
Thermal denaturation of proteins (Myofibrillar protein, Sarcoplasmic protein and stroma protein) in chicken breast (CB) and leg muscle (CL), pork thigh muscle (PT) and beef round muscle (BR) was analysed by differential scanning calorimetry (DSC). BR showed thermal denaturation at the highest temperature, which means the highest heat stability. In case of total enthalpy, CB (0.27 cal/g) appeared to be less thermo-stable than PT (0.30 cal/g). BR (0.33 cal/g) and CL (0.35 cal/g). Myofibrillar protein of BR was denatured at the highest temperature and total enthalpy also was highest. Sarcoplasmic proteins of CB and CL (0.32 cal/g) appeared to be more thermo-stable than those of PT (0.16 cal/g) or BR (0.17 cal/g). With stroma protein, CB (0.24 cal/g) appeared to be less thermo-stable than other three muscles (0.65-0.75 cal/g)
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