Involvement of μ/m‐calpain in the proteolysis and meat quality changes during postmortem storage of chicken breast muscle

The objective of this study was to investigate the role of calpain isotypes, especially poultry‐specific μ/m‐calpain in the proteolysis and meat quality changes of chicken breast muscle during postmortem storage. Calpain activity was detected by casein zymography, while the degradation of titin, desmin and Troponin‐T was analyzed by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and western blot. Meat quality indicators such as water holding capacity and tenderness were also studied. The correlation analysis between calpain activity, proteolysis and the changes in meat quality indicators indicated that there were strong correlations for μ‐calpain during the first 12 h of storage, while such strong correlations for μ/m‐calpain were only found in samples stored from 12 h to 7 days. Our study suggested that μ‐calpain played a major role in meat quality changes while μ/m‐calpain could also be involved but played a limited role in the proteolysis and meat quality changes during 12 h to 7 days postmortem storage of chicken breast muscle.     

Calpain 3/p94 is not involved in postmortem proteolysis

Studies on the correlation between expression and/or autolysis of calpain and postmortem proteolysis in muscle have provided conflicting evidence regarding the possible role of calpain 3 in postmortem tenderization of meat. Thus, the objective of this research was to test the effect of postmortem storage on proteolysis and structural changes in muscle from normal and calpain 3 knockout mice. Knockout mice (n = 6) were sacrificed along with control mice (n = 6). Hind limbs were removed and stored at 4 degrees C; muscles were dissected at 0, 1, and 3 d postmortem and subsequently analyzed individually for degradation of desmin. Pooled samples for each storage time and mouse type were analyzed for degradation of nebulin, dystrophin, vinculin, and troponin-T. In a separate experiment, hind-limb muscles from knockout (n = 4) and control mice (n = 4) were analyzed for structural changes at 0 and 7 d postmortem using light microscopy. As an index of structural changes, fiber detachment, cracked or broken fibers, and the appearance of space between sarcomeres were quantified. Cumulatively, the results of the first experiment indicated that postmortem proteolysis of muscle occurred similarly in control and in calpain 3 knockout mice. Desmin degradation did not differ (P > 0.99), and there were no indications that degradation of nebulin, dystrophin, vinculin, and troponin-T were affected by the absence of calpain 3 in postmortem muscle. Structural changes were affected by time postmortem (P < 0.05), but not by the absence of calpain 3 from the muscles. In conclusion, these results indicate that calpain 3 plays a minor role, if any, in postmortem proteolysis in muscle.     

Micro-calpain is essential for postmortem proteolysis of muscle proteins

The objective of this investigation was to test the hypothesis that -calpain is largely responsible for postmortem proteolysis of muscle proteins. To accomplish this objective, we compared proteolysis of known muscle proteins in muscles of wild type and micro-calpain knockout mice during postmortem storage. Knockout mice (n = 6) were killed along with control mice (n = 6). Hind limbs were removed and stored at 4 degrees C. Muscles were dissected at 0, 1, and 3d postmortem and subsequently analyzed for degradation of nebulin, dystrophin, metavinculin, vinculin, desmin, and troponin T. In a separate experiment, hind limb muscles from knockout (n = 4) and control mice (n = 4) were analyzed at 0, 1, and 3 d postmortem using casein zymography to confirm that mu-calpain activity was knocked out in muscle and to determine whether or not m-calpain is activated in murine postmortem muscle. Cumulatively, the results of the first experiment indicated that postmortem proteolysis was largely inhibited in micro-calpain knockout mice. The results of the second experiment established the absence of micro-calpain in the muscle tissue of knockout mice and confirmed the results of an earlier study that m-calpain is active in postmortem murine muscle. The results of the current study show that even in a species in which m-calpain is activated to some extent postmortem, micro-calpain is largely responsible for postmortem proteolysis. This observation excludes a major role for any of the other members of the calpain family or any other proteolytic system in postmortem proteolysis of muscle proteins. Therefore, understanding the regulation of micro-calpain in postmortem muscle should be the focus of further research on postmortem proteolysis and tenderization of meat.     

Effects of available dietary carbohydrate and preslaughter treatment on glycolytic potential, protein degradation, and quality traits of pig muscles

The current study was conducted to determine the interactive effects of a glycogen-reducing diet fed to finishing pigs and length of preslaughter transportion on muscle metabolic traits, proteolysis of intermediate filament and costameric proteins, and meat quality traits. Large White gilts and barrows (n = 48) were selected at 88 kg of BW and individually fed for 21 d a diet (2.6 kg/d) either high (HC) or low (LC) in available carbohydrates. Six gilts and 6 barrows fed the HC and LC diets were subjected to 0 or 3 h of transportation on the day of slaughter. Muscle temperature and pH were measured at 0.5, 1.5, 2.5, 3.5, 4.5, 5.5, and 24 h postmortem in the LM and 24 h postmortem in the dark (STD) and light (STL) portion of the semitendinosus. At 24 h postmortem, glycolytic potential (GP) was determined in the LM, STD, and STL, as well as proteolysis of titin, nebulin, desmin, vinculin, and talin in the LM and STD. The GP was lower (P < 0.05) in muscles from LC-pigs than in muscles from HC-pigs. The LC diet also resulted in lower (P < 0.05) pH, and a darker (P = 0.03), less (P < 0.01) yellow color in the STL. The LC diet decreased (P = 0.04) cooking losses in the STL and STD. The 3-h journey further decreased (P = 0.05) the GP in the STD, regardless of the diet, but transport had no effect (P > or = 0.67) on the GP of the LM and STL. Ultimate pH of the LM was lower (P = 0.02), and both portions of the semitendinosus were darker (P = 0.01) and less yellow (P < 0.01), in pigs transported 3 vs. 0 h. In pigs transported for 3 h, intact vinculin tended to be more (P = 0.08) degraded in the LM, which coincided with lower (P = 0.04) drip losses in the LM of pigs transported for 3 compared with 0 h. Increased (P < 0.01) proteolysis of titin paralleled lower (P = 0.02) shear force values in the STD of pigs transported 3 vs. 0 h. Although the present results demonstrated the potential of a glycogen-reducing diet to alter the GP of different porcine muscles, the effect of these changes on meat quality traits was limited to higher ultimate pH and darker color in the STL. The positive effects of length of transportation on water-holding capacity (LM and STD) and meat color (STD and STL) were only partially related to the resting muscle glycogen concentration because the 3-h transport lowered the GP only in the muscle with the lowest basal glycogen concentration.     

Effects of electrical stimulation and pre‐rigor conditioning temperature on aging potential of hot‐boned beef M. longissimus lumborum

The objective of this study was to create various pH/temp decline rates in hot‐boned bull beef M. longissimus lumborum (LL) through a combination of electrical stimulation (ES) and pre‐rigor holding temperature. The relationship between the pre‐rigor interventions, the activities of µ‐calpain and small heat shock proteins (sHSP), and the impacts on meat product quality were determined. Paired LL loins from 13 bulls were hot‐boned within 40 min of slaughter, immediately ES and subjected to various holding temperatures (5, 15, 25, and 35°C) for 3 hr. The rate of muscle pH decline, sarcomere length, shear force, and proteolysis of muscle proteins were measured. ES‐25°C had a longer sarcomere length compared to non‐electrical stimulation samples. ES‐25°C and ES‐35°C samples had lower shear force values, higher µ‐calpain activity and higher desmin, troponin‐T, and sHSP degradation. The above findings suggest that pH/temp decline rates created in hot‐boned muscle impacted muscle protein proteolysis by increasing the activity of proteases and degradation of sHSP.     

Postmortem titin proteolysis is influenced by sarcomere length in bovine muscle

The calpain protease system, in particular, μ-calpain is involved in the disassembly of specific myofibrillar proteins, resulting in tenderization of meat postmortem. Given the size, complexity, and integral nature of titin to the structure of the sarcomere, it is plausible that the length of a sarcomere may alter the susceptibility of various domains of titin to cleavage by the calpains. Therefore, we hypothesized titin degradation differs in a sarcomere-length-dependent manner in beef. After slaughter, beef carcasses were split and sides were either suspended by the Achilles tendon (normal suspension, NS) or by the aitchbone (hip suspension, HS). Immediately after suspension, samples were dissected from the LM, psoas major (PM), and semitendinosus (STN) muscles to serve as 0-d controls. After 24 h, 4 steaks were removed from each muscle and randomly assigned to 1-, 4-, 7-, or 10-d aging treatments. After the assigned aging period, myofibrils were purified for determination of sarcomere length. Warner-Bratzler shear force analysis was also performed to evaluate differences in tenderness. Muscle proteins were solubilized and subjected to SDS-VAGE (vertical agarose gel electrophoresis) to evaluate titin degradation. Sarcomere lengths differed (P < 0.0001) between contralateral muscles of NS and HS carcasses. Quantification of SDS-VAGE gels revealed less (P < 0.05) intact titin in the PM muscle of NS carcasses at each aging period compared with the PM of HS carcasses. No significant differences (P > 0.05) were detected in the disappearance of intact titin among suspension methods in the LM or STN. These data demonstrate that suspension method alters proteolysis of titin and suggest an increase in sarcomere length may contribute to the susceptibility of titin to postmortem proteolysis in beef.     

Rigor temperature and meat quality characteristics of lamb longissimus muscle

The present experiment was conducted to determine the effect of muscle temperature during the prerigor and early postrigor period on meat tenderness, postmortem proteolysis, calpain system activity, water-holding capacity, and color. Lamb longissimus muscle (n = 14) from the right and left carcass sides was excised immediately after dressing, divided into an anterior and posterior sample, vacuum-packaged, and stored overnight at 5 to 35 degrees C. Further storage, up to 14 d postmortem, was at 2 degrees C. Tenderness at 1 d postmortem, tenderization during further storage, and postmortem proteolysis were negatively affected by overnight incubation above 25 degrees C. This effect could be explained by an effect of temperature on muscle contraction and activity of the calpain system. Muscle contraction was at a minimum after incubation at 15 degrees C. Water-holding capacity was negatively affected by incubation above 25 degrees C. Color scores improved with increasing incubation temperature at 1 d postmortem. However, after 14 d of postmortem storage, no differences in color scores were observed. Based on the present results and results of other groups, a temperature around 15 degrees C at the onset of rigor seems optimal to maximize tenderness without having detrimental effects on water-holding capacity or color.     

Differential protein profiles in duck meat during the early postmortem storage period

The present study was designed to investigate proteomic differences in duck breast muscle during the early postmortem storage period. The meat quality was evaluated at 0 hr and 24 hr postmortem at 4°C in Pekin ducks, black Muscovy ducks and Mule ducks. Differentially expressed proteins were detected by two‐dimensional gel electrophoresis (2‐DE) and matrix‐assisted laser desorption ionization‐time‐of‐flight mass spectrometry (MALDI‐TOF/TOF MS) at 0 hr and 24 hr postmortem in the three duck breeds. The results showed that 53 proteins spots were differentially expressed at 0 hr and 24 hr postmortem at 4°C in Pekin ducks, 75 spots in black Muscovy ducks, and 72 spots in Mule ducks. A total of 30 (10 spots for each breed) were selected for identification by mass spectrometry. Seven proteins were identified in Pekin ducks, eight in black Muscovy ducks and seven in Mule ducks. Moreover, the above results obtained by 2‐DE and MALDI‐TOF/TOF MS were confirmed by western blotting. To our knowledge, this study is the first to provide insights into the protein profiles of ducks during postmortem storage and provides a better understanding of the biochemical processes that contribute to duck meat quality.     

Effect of two dietary concentrate levels on tenderness, calpain and calpastatin activities, and carcass merit in Waguli and Brahman steers

The objective of this study was to compare carcass characteristics of a newly introduced breed, the Waguli (Wagyu x Tuli), with the carcass characteristics of the Brahman breed. Brahman cattle are used extensively in the Southwest of the United States because of their tolerance to adverse environmental conditions. However, Brahman carcasses are discounted according to the height of their humps because of meat tenderness issues. The Waguli was developed in an attempt to obtain a breed that retained the heat tolerance of the Brahman but had meat quality attributes similar to the Wagyu. Twenty-four animals were used. Six steers from each breed were fed a 94% concentrate diet and 6 steers from each breed were fed an 86% concentrate diet. Eight steers, 2 from each group, were harvested after 128 d, after 142 d, and after 156 d on feed. Waguli steers had larger LM, greater backfat thickness, greater marbling scores, and greater quality grades than the Brahman steers (P < 0.05). The Japanese Wagyu breed is well known for its highly marbled and tender meat, and these traits are also present in the Waguli. The Waguli had significantly lower Warner-Bratzler shear force values than the Brahman steers after 7 and 10 d of postmortem aging (P < 0.05); this difference decreased after 14 d postmortem (P = 0.2), when tenderness of the slower aging Brahman had increased to acceptable levels. Toughness of the Brahman has been associated with high levels of calpastatin in Brahman muscle, and the Waguli LM had significantly less calpastatin activity (P = 0.02) at 0 h postmortem than the Brahman LM. At 0-h postmortem, the total LM calpain activity did not differ between the Brahman and Waguli (P = 0.57). Neither diet nor days on feed had any significant effect on the 0-h postmortem calpain or at 0-h postmortem calpastatin activity, nor an effect on Warner-Bratzler shear-force values. In conclusion, LM muscle from the Waguli steers had a high degree of marbling, lower shear force values, and low calpastatin activity, all of which are related to more tender meat.     

Combined effect of epinephrine and exercise on calpain/calpastatin and cathepsin B and L activity in porcine longissimus muscle.

The objective of the study was to improve the understanding of the relationship between the effect of epinephrine plus exercise and meat tenderness. The calpain, calpastatin, and cathepsin B + L activities and postmortem proteolysis in porcine longissimus muscle were studied. The muscle glycogen stores were depleted in five pigs by s.c. injection of epinephrine (.3 mg/kg) at 15 h antemortem and exercise on a treadmill (5 min, 3.8 km/h) immediately before slaughter. Antemortem injection of epinephrine and treadmill exercise resulted in higher ultimate pH (6.32 vs 5.66 in control) and decreased (P < .05) thaw loss, cooking loss, and shear force values. The muscle energy depletion treatment increased (P < .05) the muscle mu-calpain activity measured 42 min postmortem, and at 24 h mu-calpain activity was still approximately 50% greater in the high ultimate pH group. Also, as the ratio of mu-calpain to calpastatin increased (P < .01), the overall proteolytic potential of the calpain system were greater. These observations suggest that the muscle energy level may influence the activity of the calpain system in the living animal. The high ultimate pH group showed lower (P < .001) cathepsin B + L activity in the myofibrillar and the soluble fractions after 8 d of storage, suggesting that the increased ultimate pH increased the stability of the lysosomal membrane and thereby reduced the release of cathepsins from the lysosomes during storage. The SDS-PAGE showed increased (P < .001) degradation of a 39-kDa band in the epinephrine and exercise-treated samples. Degradation products at 30, 31, and 32 kDa were labeled by troponin-T antibody in western blot. An appearing 24-kDa band was identified as a troponin-I degradation product in western blot. The proteolytic degradation pattern of myofibrillar proteins during storage differed in control and treated samples, supporting the hypothesis that calpain-mediated proteolysis was affected after treatment, resulting in meat with high ultimate pH.     

Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses

Postmortem proteolysis in skeletal muscle and factors affecting this process were examined in pork, lamb and beef longissimus muscles (LM) to determine the cause of differences in meat tenderness among these species. Fat thickness differed among species in the following order: pork greater than beef greater than lamb. The following patterns were observed for rate of temperature and pH decline: lamb greater than pork greater than beef and pork greater than beef greater than lamb, respectively. At 1 d postmortem, pork was the most tender, followed by beef and lamb, respectively. Between 1 and 14 d of postmortem storage, lamb LM was the most improved in tenderness, followed by beef and pork, respectively. Species did not differ (P greater than .05) in LM collagen solubility. Pork LM from fed pigs had the highest (P less than .05) level of cathepsins B + L and cystatin(s) activities, whereas no differences (P greater than .05) were observed among the species for cathepsin B activity. The lowest (P less than .01) Ca2(+)-dependent protease (CDP)-II and CDP inhibitor activities were observed in pork LM. Beef LM had the highest CDP inhibitor activity (P less than .05) but was intermediate in CDP-II activity. No differences were observed among species for CDP-I activity. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of myofibrils isolated at 0, 1 and 14 d postmortem indicated that by d 1, desmin hydrolysis was most extensive in pork muscle, followed by lamb and beef.(ABSTRACT TRUNCATED AT 250 WORDS)     

钙蛋白酶系统在肌肉生长和肉品嫩化方面的研究

钙蛋白酶系统主要由钙蛋白酶(calpain)及钙蛋白酶抑制蛋白(calpastatin)组成,calpain是存在于细胞质中的依赖于Ca2+的中性蛋白酶,calpastatin是钙蛋白酶的内源抑制蛋白。近年的研究表明,calpain是细胞质中主要的蛋白水解酶,在肌原纤维蛋白降解中起着重要的作用。肌肉增长和宰后嫩度的变化与蛋白质水解程度密切相关。因此,钙蛋白酶系统的活性会影响畜禽肌肉增长和肉的嫩度。文中综述了钙蛋白酶系统各种酶的结构及其如何在肌肉生长和肉的嫩化中起作用。     

Optimization of goose breast meat tenderness by rapid ultrasound treatment using response surface methodology and artificial neural network

The aim of this study was to develop a prediction model on tenderization of goose breast meat by response surface methodology (RSM) and artificial neural network (ANN). The experiments were operated on the basis of a three‐level, three‐variable (ultrasound power, ultrasound time, and storage time) Box‐Behnken experimental design. Under RSM and ANN optimum conditions, experimental Meullenet‐Owens razor shear (MORS) of meat (1862.6 g and 1869.9 g) was in reasonable agreement with predicted one. Nevertheless, better prediction capability of ANN was proved by higher R² (0.996) and lower absolute average deviation = 4.257) compared to those for RSM (0.852 and 16.534), respectively. These results revealed that ANN was more accurate and much better than RSM model for the optimization of tenderness of meat. The optimum conditions of ultrasound power, ultrasound time, and storage time given by ANN were 812 W, 24.5 min and 25.7 hr, respectively. Under the optimized condition, the cooking loss of meat significantly decreased by ultrasound treatment compared with untreated meat. Lower cooking loss and MORS at the optimal condition were beneficial to meet the satisfaction of consumer and producers for meat factory.     

Effect of animal age,postmortem chilling rate,and aging time on meat quality attributes of water buffalo and humped cattle bulls

The study was aimed to investigate the influence of animal age, post‐slaughter chilling rate, and aging time on meat quality of M. longissimus dorsi (LD) of water buffalo (Bubalus bubalis) and humped cattle (Bos taurus indicus) bulls. After slaughtering, one side of carcasses was subjected to rapid chilling (RC) (0 ± 2°C) and other side was hanged in controlled room temperature (25 ± 2°C) for 3 hr, then allowed to the chiller (0 ± 2°C). The meat quality traits were analyzed at 1, 7, and 14 days of storage. It was noted that rapidly chilled carcasses from the younger animals of both species missed the ideal pH/temperature window, which affects the toughness of the meat. Buffalo meat presented higher shear force, color L* values, and lower b* value as compared to the cattle meat. Moreover, meat shear force values decreased while all color coordinates and cooking loss values increased with lengthening the storage time in both age groups of cattle and buffalo. In conclusion, the tenderness of cattle meat was superior to that of buffalo and RC adversely affect the shear force values of young cattle and both age groups of buffalo bulls.     

Muscle characteristics and meat quality traits are affected by divergent selection on residual feed intake in pigs

Residual feed intake (RFI) is defined as the difference between the observed feed intake and that expected based on requirements for maintenance and production. A divergent selection was conducted during 4 generations in Large White male pigs to produce low and high RFI lines. The present study aims at determining the influence of this selection on biochemical and histological traits of skeletal muscle, and relating these changes to correlated effects on growth, carcass composition, and meat quality traits. At 8 d preslaughter, biopsies from the LM were taken in the fed state on 14 females from each RFI line fed ad libitum. Animals were slaughtered at 107.8 ± 8.0 kg of BW without any previous fasting. Samples of LM, semimembranosus (SM), biceps femoris (BFM), and rhomboideus muscles were taken at both 30 min and 24 h postmortem. Myofiber typing was only assessed in LM. Low RFI pigs ("efficient") had leaner carcasses with greater muscle content (P < 0.001), less backfat thickness (P < 0.001), and less intramuscular fat content in all 4 muscles (P < 0.01 to P = 0.04). Their greater muscle content was associated with hypertrophy of all fast-twitch fibers. Glycogen content in all glycolytic muscles (i.e., LM, SM and BFM), was greater in low than high RFI pigs. The greater accumulation of glycogen in LM of low RFI pigs was specifically located in the fast-twitch glycolytic IIBW fibers, which correspond to fibers containing IIb, IIb + IIx, or IIx myosin heavy chains. The difference in muscle glycogen content between RFI line pigs was more significant in the living animals (P = 0.0003) than at 30 min postmortem (P = 0.08). This was associated with a decreased ultimate pH (P = 0.001), and greater lightness of color (P = 0.002) and drip loss (P = 0.04) in LM of low than high RFI line pigs, suggesting that selection for reduced RFI may impair some meat quality traits, such as water-holding capacity. Pigs from the low RFI line exhibited a greater (P = 0.02) percentage of IIBW fibers in LM and tended (P < 0.10) to have less lipid β-oxidative capacity in LM, SM, and BFM. In contrast, no difference (P > 0.10) between lines was found for citrate synthase and lactate dehydrogenase activities, mitochondrial activity, and expression of genes coding for uncoupling proteins 2 and 3. Differences between RFI pigs in plasma leptin, cortisol, and thyroid hormone concentrations are presented and discussed. In conclusion, selection for low RFI influenced muscle properties in a way favoring muscle mass, but likely impairing meat quality.     

MyoD and Myf6 gene expression patterns in skeletal muscle during embryonic and posthatch development in the domestic duck (Anas platyrhynchos domestica)

The MyoD and Myf6 genes, which are muscle regulatory factors (MRFs), play major roles in muscle growth and development and initiate muscle fibre formation via the regulation of muscle‐specific gene translation. Therefore, MyoD and Myf6 are potential candidate genes for meat production traits in animals and poultry. The objective of this study was to evaluate MyoD and Myf6 gene expression patterns in the skeletal muscle during early developmental stage of ducks. Gene expression levels were detected using the quantitative RT‐PCR method in the breast muscle (BM) and leg muscle (LM) at embryonic days 13, 17, 21, 25, 27, as well as at 1 week posthatching in Gaoyou and Jinding ducks (Anas platyrhynchos domestica). The MyoD and Myf6 gene profiles in the two duck breeds were consistent during early development, and MyoD gene expression showed a ‘wave’ trend in BM and an approximate ‘anti‐√’ trend in LM. Myf6 gene expression in BM showed the highest level at embryonic day 21, which subsequently decreased, although remained relatively high, while levels at embryonic days 13, 17 and 21 were higher in LM. The results of correlation analysis showed that MyoD and Myf6 gene expression levels were more strongly correlated in LM than in BM in both duck breeds. These results indicated that different expression patterns of the MyoD and Myf6 genes in BM and LM may be related to muscle development and differentiation, suggesting that MyoD and Myf6 are integral to skeletal muscle development.     

Electrical stimulation affects metabolic enzyme phosphorylation, protease activation, and meat tenderization in beef

ABSTRACT: The objective of this study was to investigate the response of sarcoplasmic proteins in bovine LM to low-voltage electrical stimulation (ES; 80 V, 35 s) after dressing and its contribution to meat tenderization at an early postmortem time. Proteome analysis showed that ES resulted in decreased (P < 0.05) phosphorylation of creatine kinase M chain, fructose bisphosphate aldolase C-A, β-enolase, and pyruvate kinase at 3 h postmortem. Zymography indicated an earlier (P < 0.05) activation of μ-calpain in ES muscles. Free lysosomal cathepsin B and L activity increased faster (P < 0.05) in ES muscles up to 24 h. Immunohistochemistry and transmission electron microscopy further indicated that lysosomal enzymes were released at an early postmortem time. Electrical stimulation also induced ultrastructural disruption of sarcomeres. In addition, ES accelerated (P < 0.05) the depletion of ATP, creatine phosphate, and glycogen, as well as a pH decline and the more preferred pH/temperature decline mode. Finally, ES accelerated meat tenderization, resulting in lesser (P < 0.05) shear force values than the control over the testing time. A possible relationship was suggested between a change in the phosphorylation of energy metabolic enzymes and the postmortem tenderization of beef. Our results suggested the possible importance of the activation of μ-calpain, phosphorylation of sarcoplasmic proteins, and release of lysosomal enzymes for ES-induced tenderization of beef muscle.     

Modified-atmosphere storage under subatmospheric pressure and beef quality: II. Color, drip, cooking loss, sarcomere length, and tenderness

Beef has a requirement for refrigerated storage up to 14 d to achieve adequate aging and a tender product. To achieve this aging with little spoilage and no surface drying, vacuum packaging is attractive, because it is inherently simple and offers a clear indication to the packer when the process has failed or there is risk of spoilage. However, there is increasing pressure on the meat industry to limit the use of packaging materials in view of their cost and the cost involved in their recovery and recycling. The purpose of this report was to evaluate an alternative storage system in containers using modified atmospheres at reduced pressure (approximately 25 kPa). The quality of the meat for both container- and vacuum-packed treatments was measured during chilled storage for up to 3 wk. Storage time had the most significant effect on quality characteristics, irrespective of the packaging method. Storage in containers under a 70%N2:30%CO2 gas mixture gave characteristics similar to beef stored under vacuum. Storage in containers under 100% CO2 produced less drip loss than under 70%N2:30%CO2, but generally container storage produced 3 times as much drip loss as vacuum packaging. Shear force of the LM was unaffected by the type of packaging, and at d 2 after slaughter (i.e., before the storage trial was begun), sarcomere lengths of muscles intended for container storage were similar to those destined for vacuum storage. During the packaging treatment, the comparison between the storage systems was always done within 1 animal using one carcass-half for container storage and the other half for vacuum packaging; all bulls were shackled from the left hindleg during bleeding. The majority of the muscles from the left sides had lower shear force values than those from the right sides at the earlier storage times (2 and 9 d after slaughter) but had similar values after longer storage (16 and 23 d after slaughter). This is the first report that shackling beef carcasses from the left side can result in more tender meat in the LM from that side. The increased tenderness in the LM from the shackled side probably resulted from an early decrease in pH and an increase in calpain activity after mechanical strain of the muscles on the shackled side. This effect of shackling should be taken into account when designing systematic comparisons of tenderness in beef.