Tenderness Of Bovine Muscle Research Articles

Green tea catechin prevents oxidative stress-regulated autophagy and apoptosis signaling, and inhibits tenderness in postmortem bovine longissimus thoracis et lumborum muscle.

Although green tea catechin has been reported to be an antioxidant and preservative in meat, the extent to which it affects the tenderization of bovine muscle remains largely unknown. This study seeks to evaluate the effect of catechin on the interplay between apoptosis and autophagy, and subsequently, the development of bovine muscle tenderness. The results indicate that catechin significantly alleviated oxidative stress. A concomitant reduction of autophagic markers LC3-II/LC3-I ratio, Beclin-1, and Atg7 levels were caused by catechin. Besides, aforementioned autophagy inhibition was further augmented by PI3K/Akt/mTOR activation. Additionally, catechin protected against mitochondrial dysfunction and inhibited mitochondria-dependent caspase apoptosis pathway. Furthermore, there was a reciprocal inhibition between autophagy and apoptosis. Ultimately, tenderness at 24 and 120h, an increase in the gap between muscle fiber bundles, and disintegration of myofibrillar architectures were all inhibited by catechin. Therefore, despite alleviating oxidative stress, catechin may hamper tenderization pattern of postmortem bovine muscle.

H2O2-induced oxidative stress improves meat tenderness by accelerating glycolysis via hypoxia-inducible factor-1α signaling pathway in postmortem bovine muscle.

Reactive oxygen species (ROS) affect meat quality through multiple biochemical pathways. To investigate the effect of ROS on postmortem glycolysis and tenderness of bovine muscle, ROS content, glycolytic potential, glycolysis rate-limiting enzyme activities, expression of hypoxia-inducible factor-1α (HIF-1α), phosphatidylinositol 3-kinase (PI3K), serine-threonine kinase (AKT), phosphorylated AKT (p-AKT), and tenderness were determined in the H2O2 group and control group. Results showed that the H2O2 group exhibited significantly higher ROS content within 48h, coupled with increased glycolytic potential, pH decline, hexokinase (HK), and phosphofructokinase activities (PFK) early postmortem. These were attributed to ROS-induced PI3K/AKT signaling pathway activation and resultant HIF-1α accumulation. Moreover, shear force in the H2O2 group reached the peak 12h earlier and decreased obviously after 24h, accompanied by a significantly higher myofibril fragmentation index (MFI). These findings suggested that ROS drive HIF-1α accumulation by activating PI3K/AKT signaling pathway, thereby accelerating glycolysis and tenderization of postmortem bovine muscle.

The effect of postmortem pH decline rate on caspase-3 activation and tenderness of bovine skeletal muscle during aging.

This study aimed to investigate the effect of postmortem pH decline rate on caspase-3 activity and bovine muscle tenderness during aging. Protein denaturation, reactive oxygen species (ROS) levels, mitochondrial apoptosis factors, and shear force were assessed in bovine muscles with different pH decline rates. The results showed that, compared with the slow group, the fast pH decline group had a 1.79% and 1.39% higher sarcoplasmic protein denaturation at 6 and 12 h, respectively (p < .05), and a significantly or extremely significantly higher ROS levels at 6-24 (p < .05, p < .01). Moreover, the fast group had a 14.05%, 22.39%,18.34%, and 25.28% of higher mitochondrial dysfunction at 6, 12, 24, and 72 h, respectively (p < .05); a 16.71%, 23.39%, 17.05%, and 26.61% of lower cytochrome c reduction levels at 6, 12, 24, and 120 h, respectively (p < .05); a significantly increased caspase-3 activity and proportion of apoptotic nuclei at 12-168 and 24-168 h, respectively (p < .05); and a 5.70%, 7.24%, 12.16%, 10.10% and 10.49% decreased shear force at 12, 24, 72,120, and 168 h, respectively (p < .05). These results demonstrated that the fast postmortem pH decline enhanced caspase-3 activation and bovine muscle tenderization by mitochondrial dysfunction-induced apoptosis during aging. PRACTICAL APPLICATIONS: Beef tenderness has long been one of the most important concerns for consumers and the meat industry. To date, the postmortem aging process has been an effective way to improve the tenderness of chilled beef. However, changes in many of the elements in a cattle's muscle after slaughter might actually determine the final tenderness of the meat. The present study suggested that the fast postmortem pH decline could promote the activation of caspase-3 and improve the tenderness of beef during aging. This finding can provide a basis for the meat processing industry to produce beef with high tenderness. In the future, beef tenderness could even be improved by adjusting the glycolytic rate and pH of muscle for a short time after slaughter.

Effect of oxidative stress on AIF-mediated apoptosis and bovine muscle tenderness during postmortem aging.

This study aimed to explore the effect exerted by oxidative stress on apoptosis-inducing factors (AIF)-mediated apoptosis and bovine muscle tenderness during postmortem aging. We investigated the reactive oxygen species (ROS) content, mitochondrial membrane permeability, AIF expression level, nucleus apoptosis, shear force, myofibril fragmentation index, pH, and energy level. According to the results, a rise in ROS content was accompanied by the rise in mitochondrial membrane permeability from 6 to 72 hr. In the meantime, the AIF expression in mitochondria was downregulated significantly within 72 hr. However, samples treated with N-acetylcysteine had significantly lower ROS content (6 to 72 hr) and mitochondrial membrane permeability (12 to 72 hr) than the control group. Moreover, during postmortem aging, the variations in AIF levels in mitochondria were closely associated with meat tenderization and nucleus apoptosis. These findings demonstrated that oxidative stress induced by ROS significantly promoted AIF release from mitochondria by enhancing the mitochondrial membrane permeability, and the released AIF mediated nucleus apoptosis that further enhanced bovine muscle tenderness. Besides, results suggest that in the early stage, the environmental factors (ATP content and pH) significantly decreased (0 to 72 hr), whereas ROS-induced oxidative stress had no significant effect on environmental factors. These observations further suggested that during postmortem aging, the decrease of pH and ATP consumption are required by AIF release. We conclude that ROS-induced oxidative stress and internal environment are vital for meat tenderization through the regulation of AIF-mediated apoptosis pathway. PRACTICAL APPLICATION: ROS-induced oxidative stress contributes to bovine muscle tenderization by promoting cell apoptosis. It is likely to lay a theoretical foundation for developing innovative tenderization techniques by altering the internal oxidation environment of postmortem muscles.

Effects of Lysosomal-Mitochondrial Apoptotic Pathway on Tenderness in Post-Mortem Bovine Longissimus Muscle.

The objective of this study was to investigate the mechanism underlying lysosome-mediated apoptosis, the cross-talk between the lysosomes and mitochondria, and the effect of the pathway on bovine longissimus muscle tenderness during 7 d post-mortem aging through the observation and analysis of longissimus dorsi (LD) muscles of six crossbred cattle. Results showed that an elevated reactive oxygen species level ( P < 0.05) can damage lysosomal membrane stability ( P < 0.05) through accumulating redox-active iron of bovine muscle during post-mortem aging. In addition, the activities of cathepsins B and D increased with post-mortem aging ( P < 0.05). Moreover, cathepsin B and D activated Bid and Bax in the mitochondria ( P < 0.05). Activated Bid and Bax triggered mitochondrial membrane permeability ( P < 0.05) and further activated caspase-9 and caspase-3 ( P < 0.05), leading to apoptosis. Ultimately, the tenderness of bovine muscle was improved during post-mortem aging ( P < 0.05). Importantly, cathepsin D plays a crucial role in the lysosomal-mitochondrial apoptotic pathway and tenderness in post-mortem muscle. These findings provide new insights into the apoptotic pathway of bovine muscle during post-mortem aging.

Effects of electrical stimulation, chilling temperature and hot-boning on the tenderness of bovine muscles

The objective of this study was to determine the effects of hot-boning, low voltage electrical stimulation (ES) and chilling temperature on the tenderness of bovine M. longissimus dorsi (LD) and M. semimembranosus (SM) muscles. LD ( n = 32) and SM ( n = 32) muscles were subjected to different post-mortem treatments; hot-boning (before 90 min post-mortem), cold-boning (at 48 h post-mortem), low voltage ES and rapid or slow chilling. Hot-boned muscles which were not electrically stimulated (NES) had higher Warner Bratzler shear force (WBSF) values ( P < 0.001) and shorter sarcomeres ( P < 0.001) than cold-boned muscles. Hot-boned muscles subjected to ES had lower pH values ( P < 0.001) post-stimulation and up to 8 h post-mortem than NES muscles. At both chilling temperatures WBSF values were lower in ES hot-boned LD and SM muscles at days 2, 7 and 14 post-mortem than NES muscles. Hot-boned muscles subjected to slow chilling had longer sarcomeres ( P < 0.001) than those subjected to fast chilling. In hot-boned SM muscles, ES resulted in longer sarcomere lengths ( P < 0.001). However, ES did not have a significant effect on the sarcomere length of LD muscles. As indicated by WBSF values all muscles tenderised during ageing, including muscles which were ‘cold shortened’. Proteolysis was not the main reason for differences in WBSF values between ES and NES muscles as judged by qualitative sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE). A combination of slow chilling and ES had a positive effect on hot-boned muscles with respect to WBSF values.

Literature Abstracts

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Relationship of Fiber Type Composition to Marbling and Tenderness of Bovine Muscle

ABSTRACTBeef carcasses (n = 65) were selected to range widely in marbling (moderately abundan: to practically devoid) and maturity (A, n = 25; B, n = 19; C, n = 6; D, n = 8; E, n = 7). Number, percent, area and mean diameter of β‐red (βR), α‐white (αW) and α‐red (αR) muscle fibers were determined. Warner‐Bratzler shear force values and taste panel tenderness ratings were also obtained. αW muscle fiber parameters were negatively correlated (P &lt; 0.05) to marbling and tenderness ratings while αR and βR parameters were positively correlated (P &lt; 0.05) to these quality attributes. The ratio of αW fiber area to βR and/or αR fiber area was correlated (P &lt; 0.05) with marbling and tenderness. Regression analyses indicate that muscle fiber type composition is more highly related to marbling (marb) than it is to shear force value (SFV) or tenderness rating (TR) although all relationships were significant (P &lt; 0.10). The relationship of these quality indicators to fiber type is greater within A maturity [marb, coefficient of determination (C.D.) = 65.09; SFV, C.D. = 65.09; SFV, C.D. = 28.85; TR, C.D. = 62.94] than for the entire population (murb, C.D. = 49.16; SFV, C.D. = 18.71; TR, C.D. = 30.47). It appears that the oxidative capacity of a muscle is related to marbling and tenderness and that muscle fiber type composition could possibly be used as a predictor of marbling potential.

LITERATURE ABSTRACTS

LITERATURE ABSTRACTS

EFFECTS OF INTRAMUSCULAR COLLAGEN AND ELASTIN ON BOVINE MUSCLE TENDERNESS

Journal of Food ScienceVolume 38, Issue 6 p. 998-1003 EFFECTS OF INTRAMUSCULAR COLLAGEN AND ELASTIN ON BOVINE MUSCLE TENDERNESS H. R. CROSS, H. R. CROSS Texas Agricultural Experiment Station, Meats and Meat Chemistry Section Dept. of Animal Science, Texas A&M University, College Station, TX 77843 USDA Standardization Branch. Livestock Div., AMS. Washington. D.C.Search for more papers by this authorZ. L. CARPENTER, Z. L. CARPENTER Texas Agricultural Experiment Station, Meats and Meat Chemistry Section Dept. of Animal Science, Texas A&M University, College Station, TX 77843Search for more papers by this authorG. C. SMITH, G. C. SMITH Texas Agricultural Experiment Station, Meats and Meat Chemistry Section Dept. of Animal Science, Texas A&M University, College Station, TX 77843Search for more papers by this author H. R. CROSS, H. R. CROSS Texas Agricultural Experiment Station, Meats and Meat Chemistry Section Dept. of Animal Science, Texas A&M University, College Station, TX 77843 USDA Standardization Branch. Livestock Div., AMS. Washington. D.C.Search for more papers by this authorZ. L. CARPENTER, Z. L. CARPENTER Texas Agricultural Experiment Station, Meats and Meat Chemistry Section Dept. of Animal Science, Texas A&M University, College Station, TX 77843Search for more papers by this authorG. C. SMITH, G. C. SMITH Texas Agricultural Experiment Station, Meats and Meat Chemistry Section Dept. of Animal Science, Texas A&M University, College Station, TX 77843Search for more papers by this author First published: September 1973 https://doi.org/10.1111/j.1365-2621.1973.tb02133.xCitations: 243 AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Citing Literature Volume38, Issue6September 1973Pages 998-1003 RelatedInformation

LITERATURE ABSTRACTS

LITERATURE ABSTRACTS

Relationship of Intracellular Proteins and Muscle Pigments to the Tenderness of Bovine Muscles

Relationship of Intracellular Proteins and Muscle Pigments to the Tenderness of Bovine Muscles

Relationship of Water Binding and pH to Tenderness of Bovine Muscles

Relationship of Water Binding and pH to Tenderness of Bovine Muscles

Histological Studies of Post‐Mortem Changes in Sarcomere Length as Related to Bovine Muscle Tenderness

SUMMARYThe effect of post‐mortem muscle contraction on ultimate tenderness was studied in muscles of 12 beef animals of similar weight and grade. State of contraction was determined by measurement of sarcomere lengths. Longissimus dorsi and semimembranosus muscles were observed. Histological samples removed at various intervals post‐mortem were treated with ethylenediaminetetraacetate (EDTA) to prevent further contraction. A phase‐contrast microscope was used to observe muscle fibers, and sareomeres were measured with a filar micrometer. Muscle contraction patterns of each animal were plotted through a 7‐day aging period. State of contraction after 7 days appeared to have a greater influence on subsequent (7 days) tenderness than did state of contraction at time of maximum rigor mortis. Although contraction did not seem to be the factor most responsible for final tenderness, it did appear to have a significant influence. Considerable lengthening of sarcomeres normally occurred during the aging period. Semimembranosus muscles routinely contracted less than longissimus dorsi muscles during rigor mortis, and were more relaxed after 7 days of aging. Semimembranosus muscles were consistently less tender than longissimus dorsi muscles at slaughter, but the reverse was usually true after 7 days.

Further Studies on Bovine Muscle Tenderness as Influenced by Carcass Position, Sarcomere Length, and Fiber Diameter

SUMMARYInterrelationships of fiber diameter, sarcomere length, and tenderness were studied in 12 bovine muscles of horizontally placed and vertically suspended carcass sides. In comparison with the horizontally placed sides, the vertically suspended sides had greater sarcomere lengths in the psoas major, latissimus dorsi, and rectus femoris muscles. Conversely, vertical suspension permitted the longissimus dorsi, gluteus medius, adductor, biceps femoris, and semitendinosus muscles to shorten in sarcomere length. In general the differences in sareomere lengths of muscles (between sides) were associated (r=–.82 P &lt;.01) with differences in fiber diameter. Differences in fiber diameter (between sides) were highly related to differences in shear force (r= .73, P &lt;.01, as were differences in sarcomere length (T = ‐.80, P &lt;.01). When museles shortened, there were corresponding decreases in sarcomere length, increases in fiber diameter, and decreases in tenderness.

Meat Tenderness, Relation between Hydroxyproline of Alkali-Insoluble Protein and Tenderness of Bovine Muscle

Meat Tenderness, Relation between Hydroxyproline of Alkali-Insoluble Protein and Tenderness of Bovine Muscle