Changes in Physical Meat Traits, Protein Solubility, and the Microstructure of Different Beef Muscles during Post-Mortem Aging

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.

Lipid oxidation and protein co-oxidation in ready-to-eat meat products as affected by temperature, antioxidant, and packaging material during 6 months of storage

“…Changes in the chemical properties and protein solubility can reflect the degree of protein denaturation resulting from oxidation. 48 The reaction between lipid oxidative products and protein molecules could lead to severe chemical modification on the tertiary and quaternary protein structures. The reaction causes polypeptide chains to unfold and expose hydrophobic groups to the surroundings, increasing protein–protein aggregation and disrupting protein–water interaction, resulting in the loss of solubility.…”

“…The reaction causes polypeptide chains to unfold and expose hydrophobic groups to the surroundings, increasing protein-protein aggregation and disrupting protein-water interaction, resulting in the loss of solubility. 29,48,49 Insolubility becomes more severe with increasing storage time and temperature as well as with elevated water activity in meat and meat products. 40,50,51 As shown in Fig.…”

Molecular characterization of a novel aspartyl aminopeptidase that contributes to the increase in glutamic acid content in chicken meat during cooking

“… Nishimura et al (1990) also showed that the aminopeptidase activity of chicken muscle extract against glutamyl substrate was much higher than that of bovine muscle extract. The pH values of meat chicken and meat beef extracts are around 6 ( Kadıoğlu et al, 2019 ) and 5 to near 6 ( Feng et al, 2020 ), respectively. At pH 6, meat chicken extract showed much higher glutamic acid-releasing activity than meat beef extract.…”

Protein Markers Related to Non-halal Slaughtering Process of Rat as Mammal Animal’s Model Detected Using Mass Spectrometry Proteome Analysis

“…Each sample gave seven protein bands. M: protein marker; H1: halal method 1; H2: halal method 2; H3: halal method 3; N1: non-halal method 1; N2: non-halal method 2; N3: non-halal method 3 actin, and stromal proteins [26]. Some other possible proteins are dihydrolipoyl dehydrogenase, myosinbinding, calreticulin, and aspartate aminotransferase [24][25].…”