Abstract
Differential scanning calorimetry(DSC) was used to evaluate thermal denaturation of muscle proteins from beef, pork and lamb rib eye, and from chicken breast and thigh. The mammalian and the chicken thigh muscles exhibited three endothermic transitions with peak temperature maxima (Tm) near 58, 66 and 79°C, but the precise Tm's were species and pH dependent. Studies of protein fractions from chicken thigh indicated that the second transition was due to the combined effects of thermal denaturation of sarcoplasmic and connective tissue proteins and the third transition was due to actin. Chicken breast muscle demonstrated a complex thermal curve with five peaks at 57, 62, 67, 72 and 79°C (Tm). The middle three peaks were attributed to connective tissue and sarcoplasmic proteins. Myofibrils isolated from the mammalian and chicken thigh muscles gave two endothermic transitions near 60 and 70°C, whereas, chicken breast myofibrils exhibited three transitions at 53, 61 and 69°C (Tm). Differences in thermal properties of proteins between white and red muscles of chicken were greater than those between muscles obtained from the several species.
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