Impact of Tumbling Process on the Toughness and Structure of Raw Beef Meat Pieces

Tenderness is a major factor in consumer perception and acceptability of beef meat. Here we used a laboratory tumbling simulator to investigate the effectiveness of the tumbling process in reducing the toughness of raw beef cuts. Twelve Semitendinosus beef muscles from cows were tumbled according to four programs: T1 (2500 consecutive compression cycles (CC), for about 3 h), T2 (6000 CC, about 7.5 h), T3 (9500 CC, about 12 h), and T4 (13,000 CC, about 16 h). The effect of tumbling on the toughness of raw meat was assessed using compression tests (stresses measured at 20% and 80% of deformation ratios) and microscopic observations made at the periphery and centre of meat samples, and compared against non-tumbled controls. Longer tumbling times significantly reduced the stresses measured at 20% and 80% compression rates, which reflected the toughness of muscle fibres and connective tissue, respectively. At the microscopic level, longer tumbling times led to reduced extracellular spaces, increased degradation of muscle structure, and the emergence of amorphous zones. A 12-h tumbling protocol ultimately makes the best compromise between the process time demand and toughness reduction in beef Semitendinosus meat pieces.

Application of proteomics to understand the molecular mechanisms determining meat quality of beef muscles during postmortem aging

Proteomics profiling disclosed the molecular mechanism underlying beef poor meat quality. This study aimed to identify protein markers indicating the quality of beef during postmortem storage at 4°C. Beef longissimus dorsi samples were stored at 4°C. The meat water holding capacity (WHC), pH value and moisture content were determined at different time points during the storage period. The iTRAQ MS/MS approach was used to determine the proteomics profiling at 0, 3.5 and 7 d during storage at 4°C. Bioinformatics analysis was performed to investigate the potential correlated proteins associated with meat quality. Storage at 4°C gradually decreased the pH value, WHC, and hence the moisture content. The iTRAQ proteomic analysis revealed that a cluster of glycolytic enzymes including malate dehydrogenase, cytoplasmic, L-lactate dehydrogenase, phosphoglycerate mutase and pyruvate kinase, and another cluster of proteins involved in oxygen transport and binding (myoglobin) and hemoglobin complex (including Globin A1 and hemoglobin subunit alpha) were decreased during the postmortem storage. These results suggest that the decreased glycolysis, oxygen, and heme-binding activities might be associated with the beef muscle low quality and the decline of tenderness during postmortem storage at 4°C.

The Applicability of Total Color Difference ΔE for Determining the Blooming Time in Longissimus Lumborum and Semimembranosus Muscles from Holstein-Friesian Bulls at Different Ageing Times

This study was conducted to determine the optimal blooming time in beef muscles based on ΔE, and to analyze the effects of muscle type and ageing time on beef color and blooming. Beef color was determined on freshly cut longissimus lumborum (LL, n = 8) and semimembranosus (SM, n = 8) muscles on days 1, 9, and 14 of ageing during 60 min blooming at 5 min intervals. It was found that ΔE0, representing the difference in color between freshly cut muscles and subsequently analyzed samples, supported the determination of the optimal blooming time, which varied across ageing times (15, 20, 25 min for the LL muscle, and 10, 15, 20 min for the SM muscle on days 1, 9, and 14 of ageing, respectively). Beef color was affected by both muscle type and ageing. The values of color parameters increased between days 1 and 9 of ageing. The results may have practical applications because beef should be presented to consumers and restaurant owners approximately 25 min after cutting, when its color has fully developed.

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

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.