Changes of myofibrillar and centrifugal drip proteins and shear force of psoas major and minor and semitendinosus muscles from calves, heifers and cows during post-mortem ageing (2023)

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Meat Science

Volume 64, Issue 1,

May 2003

, Pages 69-75

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Changes in myofibrillar protein content and centrifugal drip proteins of psoas major and minor (PM) and semitendinosus (ST) muscles of calves, heifers and cows taken from carcasses on the 1st, 6th and 12th day of post-mortem cold storage were estimated. Washed myofibrils and centrifugal drip from muscles were analysed using SDS-PAGE 10 and 12% polyacrylamide gels. No significant changes were observed in content of contractile proteins, α-actinin and regulatory proteins (except for TN-T). There were no significant differences between muscles from investigated groups and between muscles aged in chilled conditions. The levels of titin T1 during ageing varied slightly. The 30 kDa-fraction appearance was fastest in calf, slower in heifer and slowest in cow muscles. More pronounced differences in the level of protein degradation with regards to muscle type, age of animals and time of storage were found in the centrifugal drip of meat. In the drip, the level of high molecular weight proteins was higher in muscles from young animals and in the muscles stored longer. The opposite was observed in case of 26–28 kDa proteins. Their amount in muscle drip decreased with increased storage time. The rate of proteolysis and release of cytoskeletal proteins during cold storage of muscles were related to change in shear values of roasted meat. The highest rate of protein degradation was observed in PM calf muscle and the lowest rate in ST cow muscle. The fastest tenderization process was registered in calves muscles and the slowest tenderization in cows.


Structural changes occur in bovine muscles during post-mortem storage of meat in the refrigerated conditions (Wegner et al., 2000, Will et al., 1980, Ho et al., 1996). According to Kołczak, Pospiech, Palka, and Lącki (2002) during 12 days of cold storage of meat the length of sarcomeres increases, mainly due to the enlargement of I-bands and also some changes in A-band, which took place especially in PM of veal. These structural changes are more rapid and intense in muscles from younger animals, are faster and have wider range in psoas major and minor (PM) than in semitenidinosus (ST) muscle.

The main contractile proteins of myofibrils, such as myosin and actin, do not appear to undergo degradation post-mortem at 4°C even after 56 days of cold storage (Bandman and Zdanis, 1988, Yates et al., 1983). However changes in structure of muscle fibres are considered to be caused by degradation of cytoskeletal proteins. These proteins are part of costameres binding myofibrils with sarcolemma (Huff-Lonergan et al., 1996, Robson et al., 1997, Taylor et al., 1995) and stabilise the intracellular myofibrillar protein arrangement (Taylor et al., 1995, Chiung-Ying et al., 1996, Huff-Lonergan et al., 1995), especially the Z-discs’ structure (Shimada et al., 1999, Takahashi, 1996). The changes are associated with degradation of two very large proteins: nebulin and titin, however the disappearance of smaller proteins has also been brought to the attention of investigators. Recent studies show that this disappearance and the breaks of structures near the Z-line may be related to the titin degradation at the N2 line (Boyer-Berri & Greaser, 1998) and proteolysis of desmin, which is responsible for transverse stabilisation of muscle fibrils and myofibrils (Purslow, Ertbjerg, Baron, Christensen, & Lawson, 2001).

One of the most common symptoms of proteolytic protein degradation during the cold ageing is the appearance of troponin T (TN-T) degradation products having molecular weight of about 30 kDa (Ho et al., 1994, Geesing et al., 1995, MacBride and Parrish, 1977, Penny and Dransfield, 1979). According to Penny and Dransfield (1979) they can be used as an indicator of the rate of meat ageing.

Despite many studies describing degradation of cytoskeletal proteins and TN-T, there is a lack of information on their changes in muscles, which come from animals of different maturity. The aim of this study was to describe changes in myofibrillar (including cytoskeletal) proteins and centrifugal drip proteins from PM and ST muscles of calves, heifers and cows during 12-days post-mortem cold storage and to relate the results to Warner-Bratzler shear force measurements.

Section snippets

Material and methods

PM and ST muscles were taken from left half-carcasses of female calves (3-months old), heifers (18-months old) and cows (around 8 years old) 24 h after slaughter. In each of the examined groups, analyses were carried out on muscles taken from three carcasses. Each of the muscles was divided into 3 parts, which were vacuum-sealed and stored at 4°C for 12 days.

Myofibrils from samples after 1, 6 and 12 days of cold storage were isolated and their proteins were determined using PAGE-SDS (Fritz,

Results and discussion

Electrophoresis of washed myofibrils originating from examined PM and ST muscles showed from 18 to 24 bands of proteins. Fig.1 presents their electrophoretical pattern after 1st, 6th, and 12th days of cold storage of samples taken from heifers muscles. This figure also depicts the separation of proteins from centrifugal drip of these muscles.

No significant changes were observed in the amount of the contractile proteins myosin and actin. The share of MHC (myosin heavy chains) in the fraction of


During post-mortem storage of beef muscles the degradation of myofibrillar and cytoskeletal proteins depends on muscle type and animal age. Changes of titin T1 in the fraction of washed myofibrillar proteins observed on SDS-PAGE are small. More pronounced changes occur in the fraction of 30 kDa, i.e. Tn-T degradation products. Their appearance is slower in cow than in heifer and calf muscles. Clear differences in concentration of protein degradation fractions in centrifugal drip are observed

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