Heat-induced protein gelation is the functionality that is required in restructured chicken products such as chicken frankfurters, tenders, nuggets and others in industrial practice. This is why in the present study the proteins recovered with isoelectric solubilization/precipitation (ISP) from boneless skinless chicken breast as well as skin-on bone-in drumstick were subjected to DSC tests in order to determine their thermal denaturation (Table 2 and Fig. 2). During ISP sarcoplasmic proteins are mostly lost. Therefore, the ISP-recovered proteins contain mainly myofibrillar proteins, which typically exhibit excellent thermal gelation. The functional and textural quality of meat depends on myofibrillar proteins. Myosin and actin are critical for gelation of myofibrillar
proteins. Myosin denatures at lower temperatures than actin, and
therefore, the first peak on DSC thermograms corresponds to
myosin while the second to actin (Wright, Leach, & Wilding, 1977).