Effect of gender and muscle type on the proteolytic pattern of myofibrillar proteins in Iranian one-humped camel meat during storage

In this study, effect of gender, muscle type (biceps femoris (BF) and longissimus thoracis (LT)) and storage time (14 days) on the proteolytic pattern of camel meat myofibrillar proteins was investigated using SDS-PAGE. Heavy chain myosin (MHC) and actin changed little during postmortem aging of muscles. Proteolysis intensity of MHC in female camels was significantly more than male ones (p<0.05). Degradation of C-protein was influenced by storage time, gender and muscle type (p<0.05). α-actinin was proteolyzed by catepsins at the second week of aging, and its breakdown was more pronounced in BF than LT muscle (p<0.05). Principal degradation of desmin occurred at the first week of storage. Troponin-T was proteolyzed by about 80% up to 5 days of storage, and muscle type and aging time significantly affected its proteolysis. The30 kDapolypeptideas a main product of Troponin-T degradation began to appear 24 h postmortem, and its band intensity increased significantly during 14 days of storage (p 0.05). In conclusion, storage time was the most important factor affecting degradation of myofibrillar proteins during storage at 4oC. Also, muscle type was a main factor at proteolysis of desmin cytoskeletal protein and some regulating proteins (α-actinin and Troponin-T).