Abstract
This study was performed to compare the differences in pH, myofibril fragmentation index (MFI), total protein solubility (TPS), sarcoplasmic protein solubility (SPS), myofibrillar protein solubility (MPS), and the microstructure of seven beef muscles during aging. From the six beef carcasses of Xinjiang brown cattle, a total of 252 samples from semitendinosus (ST), longissimus thoracis (LT), rhomboideus (RH), gastrocnemius (GN), infraspinatus (IN), psoas major (PM), and biceps femoris (BF) muscles were collected, portioned, and assigned to six aging periods (1, 3, 7, 9, 11, and 14 day/s) and 42 samples were used per storage period. IN muscle showed the highest pH (p < 0.05) from 1 to 14 days and the lowest TPS (p < 0.01) from 9 to 14 days with respect to the other muscles. Moreover, the changes in IN were further supported by transmission electron microscopy due to the destruction of the myofibril structure. The highest value of MFI was tested in ST muscle from 7 to 14 days. The total protein solubility in PM, RH, and GN muscles were not affected (p > 0.05) as the aging period increased. The lowest TPS was found in the RH muscle on day 1, 3, and 7 and in the IN muscle on day 9, 11, and 14. The pH showed negative correlations with the MFI, TPS, and MPS (p < 0.01). The results suggest that changes in protein solubility and muscle fiber structure are related to muscle location in the carcass during aging. These results provide new insights to optimize the processing and storage of different beef muscles and enhance our understanding of the biological characteristics of Xinjiang brown cattle muscles.
Highlights
Meat and meat products are important nutrient-intensive foods that are widely consumed worldwide [1]
Compared to the IN muscle, the pH values in ST, longissimus thoracis (LT), psoas major (PM), and biceps femoris (BF) were lower at 1 day (p < 0.05)
The correlation coefficients of total protein solubility (TPS) with myofibrillar protein solubility (MPS) are higher than those of sarcoplasmic protein solubility (SPS), indicating that TPS was affected to a larger extent by the denaturation of MPS than that of SPS. These results suggest that pH is a more important determinant for protein solubility than myofibril fragmentation index (MFI) in this study
Summary
Meat and meat products are important nutrient-intensive foods that are widely consumed worldwide [1]. Tenderness is a critical indicator that drives their willingness to repurchase and acceptability [2,3]. There are still great variations in the tenderness between different parts of beef muscles [4,5]. In the beef industry, aging is often considered to be one of the important factors determining the ultimate tenderness of the meat [6,7]. Due to the differences between the biochemical characteristics of these muscles, they may cause different degrees of response to aging [4]. The inconsistency of the tenderness of different muscles has become the main problem that currently exists in the meat processing industry during the aging process
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