Dynamic Gelling Properties of Myofibrillar Protein from Skeletal Muscles of Different Chicken Partst

The rheological characteristics of myofibrillar protein from four parts of chicken carcasses were compared. During thermal gelation, pectoralis major and pectoralis minor proteins exhibited a single loss modulus (G″) peak (45 °C) and two storage modulus (G′) peaks (50 and 60°). The final G′ value as well as the gel penetration strength decreased with increasing pH from 5.87 to 6.53. These gelling parameters were lower for pectoralis minor protein than for pectoralis major protein. Thigh and drumstick proteins produced similar viscoelastic patterns during gelation, showing a G″ peak around 48 °C and a G′ peak around 51 °C. Compared to pectoralis gels, thigh and drumstick gels were substantially less elastic and more sensitive to pH within 50-60 °C. The major disparities in protein gelling behavior among the different chicken parts appeared to be relevant to the specific distribution of white and red fibers within the muscles.