Effects of temperature and method of heat treatment on myofibrillar proteins of pork

Abstract

© 2014, Serbian Chemical Society. All rights reserved. During the tests in this paper, meat processing was carried out at different temperatures in the range of 51 to 100 °C. The meat was processed by dry heat (roasting) and wet heat treatments (cooking) in water at atmospheric pressure. After heat treatment, myofibrillar proteins were extracted from solutions at constant ionic strength. Quantitative and qualitative determinations of protein fractions were performed by capillary electrophoresis. Myofibrillar proteins were also analized for fresh pork meat sample. Results obtained in fresh meat were compared with those recorded after roasting and cooking. In the fresh and thermally processed pork the following proteins were identified: myosin, light chain 3; myosin, light chain 2; troponin-C; troponin-I; myosin, light chain 1; tropomyosin; troponin-T; actin; desmin; α-actinin; C-protein; M-protein (Mβ); M-protein (Mα); heavy meromyosin-HMM. For both methods of thermal processing, with increasing heat treatment temperature, concentration of soluble protein in the extract decreases rapidly after 51 °C. Cooking treatment had a more intense effect on the proteins change and denaturation than roasting.