Changes of muscle fiber structure and oxidation characteristics during mutton post-slaughter maturation
Post-slaughter maturation is an effective mean for improving the quality of meat products.This study investigated the changes in microscopic structures of muscle fibers and properties of myofibrillar proteins during post-slaughter maturation of mutton at 4 ℃ for 48 h.The results showed that during maturation,muscle fibers aggregated,the edges of fiber bundles became rough,and the distance between fibers increased.The TBARS value increased by 47.8％after 48 h of maturation,while the solubility of total protein and myofibrillar protein decreased.The hydrophobicity of myofibrillar protein and its carbonyl content increased significantly while the sulfydryl content decreased.At 0 h,12 h and 24 h of maturation,the average proportions ofα-helix,β-fold,β-corner and random coil structures were about 29％,19％,21％and 31％,respectively.The random coil structure was not detected at 48 h.Overall,during the maturation after slaughter,the muscle fiber strips degraded after polymerization.The sulfydryl proteins were more easily to oxidize in the first 12 h after slaughter,and the lipid oxidation accelerated after 12 h.The results provide a theoretical basis for analyzing the change of meat quality from the perspective of myofibrillar protein structure and oxidation during post-slaughter maturation.
万方数据
维普
