期刊名称：Chemical Industry and Chemical Engineering Quarterly
印刷版ISSN：1451-9372
出版年度：2014
卷号：20
期号：3
页码：407-415
DOI：10.2298/CICEQ121011023V
出版社：Association of the Chemical Engineers
摘要：During the tests in this paper, meat processing was carried out at different temperatures between the range of 51°C 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´s 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.
关键词：pork meat; cooking; roasting; protein denaturation; capillary electrophoresis
