Use of plasma induced modification of biomolecules (PLIMB) to evaluate hemin dissociation from fish and bovine methemoglobins.

Hemin dissociation occurs much faster from fish methemoglobin (metHb) compared to mammalian metHb yet the mechanism remains poorly understood. This may involve enhanced solvent access to His(E7) of fish metHbs by a protonation mechanism. Plasma induced modification of biomolecules (PLIMB) produces free radicals that covalently modify solvent accessible residues of proteins, and so can provide insight regarding accessibility of hydronium ions to protonate His(E7). PLIMB-induced modifications to heme crevice sites of trout IV and bovine metHb were determined using tandem mass spectrometry after generating peptides with Trypsin/Lys-C. αHis(CE3) was more modified in trout attributable to the more dynamic nature of bovine αHis(CE3) from available crystal structures. Although His(E7) was not found to be more modified in trout, aspects of trout peptides containing His(E7) hampered modification determinations. An existing computational structure-based approach was also used to estimate protonation tendencies, suggesting His(E7) of metHbs with low hemin affinity are more protonatable.

The color of fresh pork: Consumers expectations, underlying farm-to-fork factors, myoglobin chemistry and contribution of proteomics to decipher the biochemical mechanisms.

The color of fresh pork is a crucial quality attribute that significantly influences consumer perception and purchase decisions. This review first explores consumer expectations and discrimination regarding pork color, as well as an overview of the underlying factors that, from farm-to-fork, contribute to its variation. Understanding the husbandry factors, peri- and post-mortem factors and consumer preferences is essential for the pork industry to meet market demands effectively. This review then delves into current knowledge of pork myoglobin chemistry, its modifications and pork discoloration. Pork myoglobin, which has certain peculiarities comparted to other meat species, plays a weak role in determining pork color, and a thorough understanding of the biochemical changes it undergoes is crucial to understand and improve color stability. Furthermore, the growing role of proteomics as a high-throughput approach and its application as a powerful research tool in meat research, mainly to decipher the biochemical mechanisms involved in pork color determination and identify protein biomarkers, are highlighted. Based on an integrative muscle biology approach, the available proteomics studies on pork color have enabled us to provide the first repertoire of pork color biomarkers, to shortlist and propose a list of proteins for evaluation, and to provide valuable insights into the interconnected biochemical processes implicated in pork color determination. By highlighting the contributions of proteomics in elucidating the biochemical mechanisms underlying pork color determination, the knowledge gained hold significant potential for the pork industry to effectively meet market demands, enhance product quality, and ensure consistent and appealing pork color.

The potential of metabolomics in meat science: Current applications, trends, and challenges.

Metabolites are the final products of metabolism and provide insights into the biochemical balance of tissue systems. A cascade of reactions involving proteins, carbohydrates, and lipids affects meat color, tenderness, and flavor, specifically, metabolites that are key biomolecules in biochemical reactions associated with attainment of acceptable meat quality. Bioinformatics platforms, such as Kyoto Encyclopedia of Genes and Genomes (KEGG) databases and MetaboAnalyst, are utilized to help understanding the role of differentially abundant metabolites and characterizing their roles in cellular function/metabolism. However, the inability to identify all metabolites using a single platform and limited metabolite libraries specifically for meat/food remains a challenge. Therefore, the advances in metabolite separation, easy-to-use data processing, increased resolution of mass-spectrometry, and data analysis will help to make inferences or develop biomarkers related to meat quality. This review discusses how metabolomics can be exploited to characterize meat quality, the challenges, and current trends. SIGNIFICANCE: Metabolites play an important role in attaining consumer-preferred meat quality traits and nutritive value of foods. Visual appearance of fresh foods, such as muscle foods, are utilized by consumers to assess the quality at the retail market before making purchases. Similarly, tenderness and flavor of meats influence eating satisfaction and re-purchase decisions. Inconsistencies in meat quality lead to enormous economic losses to the food industry. For instance, consumers often associate a bright-cherry red color with freshness, and the US beef industry loses $3.74 billion annually due to discoloration during storage. Both pre-and post-harvest factors influence the extent of meat quality changes. Metabolomics offer robust tools to get a snapshot of small molecules such as acids, amino acids, glycolytic- and tricarboxylic acids, fatty acids, and sugars present in post-mortem muscle tissue and their role in meat quality. Further, using bioinformatics platforms enables characterizing the role of differentially present metabolites in meat quality as well as identifying biomarkers for desirable quality traits such as tender meat or color-stable carcasses. Innovative applications of metabolomics can be exploited to elucidate the underpinnings of meat quality and to develop novel strategies to enhance marketability of retail fresh meats.

Proteomic approaches to characterize biochemistry of fresh beef color.

Color of retail fresh beef is the most important quality influencing the consumers' purchase decisions at the point of sale. Discolored fresh beef cuts are either discarded or converted to low-value products, before the microbial quality is compromised, resulting in huge economic loss to meat industry. The interinfluential interactions between myoglobin, small biomolecules, proteome, and cellular components in postmortem skeletal muscles govern the color stability of fresh beef. This review examines the novel applications of high-throughput tools in mass spectrometry and proteomics to elucidate the fundamental basis of these interactions and to explain the underpinning mechanisms of fresh beef color. Advanced proteomic research indicates that a multitude of factors endogenous to skeletal muscles critically influence the biochemistry of myoglobin and color stability in fresh beef. Additionally, this review highlights the potential of muscle proteome components and myoglobin modifications as novel biomarkers for fresh beef color. SIGNIFICANCE: This review highlights the important role of muscle proteome in fresh beef color, which is the major trait impacting consumers' purchase decisions. In recent years, innovative approaches in proteomics have been exploited for an in-depth understanding of the biochemical mechanisms influencing color development and color stability in fresh beef. The review suggests that a wide range of factors, including endogenous skeletal muscle components, can affect myoglobin biochemistry and color stability in beef. Furthermore, the potential use of muscle proteome components and myoglobin post-translational modifications as biomarkers for fresh beef color is discussed. The currently available body of evidence presented in this review can have important implications in meat industry as it provides novel insights into the factors influencing fresh beef color and an up-to-date list of biomarkers that can be used to predict beef color quality.

Color attributes and myoglobin chemistry exhibit relationships with tenderness and calpain-1 abundance in postmortem Longissimus lumborum muscles from Holstein heifers.

The objective of this study was to determine the extent that myoglobin and beef color are associated with calpain-1 relative abundance relative and tenderness. Longissimus lumborum (LL) samples from the left side of Holstein beef carcasses (n = 31) were collected immediately post-evisceration for 0 h analyses. At 48 h postmortem six steaks were removed from the right side of each carcass for analyses at 48 and 336 h postmortem. Myoglobin concentrations resulted in negative correlations (P < 0.05) to Warner-Bratzler shear force (WBSF) values at 336 h postmortem. L*, a*, and b* values at 48 h resulted in positive correlations (P < 0.05) with WBSF values at 48 and 336 h. Values for b* at 336 h had positive correlations with calpain-1 concentration at 0 and 336 h. Data from this study indicate a potential relationship between myoglobin concentration and meat color with tenderness aspects and calpain-1 relative abundance.

Proteome basis for the biological variations in color and tenderness of longissimus thoracis muscle from beef cattle differing in growth rate and feeding regime.

The proteome basis for the biological variations in color and tenderness of longissimus thoracis muscle from ½ Angus (Bos taurus taurus) × ½ Nellore (Bos taurus indicus) crossbred steers was evaluated in a completely randomized experimental design consisting of four treatments (n = 9 per treatment): 1) feedlot finished, high growth rate (FH); 2) feedlot finished, low growth rate (FL); 3) pasture finished, high growth rate (PH); and 4) pasture finished, low growth rate (PL). The following comparisons were made to evaluate the effects of finishing systems and growth rates on muscle proteome: 1) FH × PL; 2) FL × PH; 3) FH × FL; and 4) PH × PL. Sixteen protein spots were differentially abundant among these comparisons (P ≤ 0.05), which were distinguished in two major clusters, energy metabolism- and muscle structure-related proteins that impacted glycolysis, carbon metabolism, amino acid biosynthesis and muscle contraction pathways (FDR ≤ 0.05). For FH × PL comparison, triosephosphate isomerase (TPI), phosphoglucomutase-1 (PGM1) and phosphoglycerate kinase 1 (PGK1) were overabundant in FH beef whereas troponin T (TNNT3), α-actin (ACTA1) and myosin regulatory light chain 2 (MYLPF) were overabundant in PL beef. For the FL × PH comparison, PGM1, phosphoglycerate mutase 2 (PGAM2) and annexin 2 (ANXA2) were overabundant in PH beef. For the FH × FL comparison, AMP deaminase (AMPD1) and serum albumin (ALB) were overabundant in FH beef whereas glycogen phosphorylase (PYGM) was overabundant in FL beef. For the PH × PL comparison, myoglobin (MB) was overabundant in PH beef whereas PYGM and MYLPF were overabundant in PL beef. In non-aged beef, L* was positively correlated with PGM1 (r = 0.54) while tenderness was negatively correlated with PGAM2 (r = -0.74) and ANXA2 (r = -0.60). In 7-d aged beef, color attributes (L*, a* and b*) were positively correlated with PGM1 (r = 0.67, 0.64 and 0.64, respectively) while tenderness was negatively correlated with TNNT3 (r = -0.57), PGK1 (r = -0.52) and MYLPF (r = -0.66). Therefore, finishing systems and growth rate affected the muscle proteome profile, which was related to beef color and tenderness. Additionally, these results suggest potential biomarkers for beef color (PGM1 and PGAM2) and tenderness (ANXA2, MYLPF, PGK1 and TNNT3).

Application of Vis-NIR and SWIR spectroscopy for the segregation of bison muscles based on their color stability.

The study objective was to investigate the potential for using visible near-infrared (Vis-NIR) and short wave infrared (SWIR) spectroscopy to segregate bison portions based on muscle types and storage periods. In the Vis-NIR range, the principal component analysis showed clear segregation of the muscles based on storage at retail display d 4 whereas the discrimination based on muscle type was better portrayed in the SWIR region. Furthermore, partial least squares discriminant analysis (PLS-DA) models classified muscles based on muscle type and storage in the Vis-NIR range with the classification accuracy of 97% for calibration and 86% for cross-validation. Finally, the PLS-regression models were developed for the successful prediction of a* value with an R2 of 0.88 (RMSEC: 1.57), 0.84 (RMSECV: 1.88), and 0.90 (RMSEP: 1.41), color score with an R2 of 0.96 (0.25), 0.95 (0.27), and 0.92 (0.32), and discoloration score with an R2 of 0.96 (0.47), 0.93 (0.63), and 0.93 (0.56) for calibration, cross-validation, and prediction, respectively.

Broiler genetics influences proteome profiles of normal and woody breast muscle.

Wooden or woody breast (WB) is a myopathy of the pectoralis major in fast-growing broilers that influences the quality of breast meat and causes an economic loss in the poultry industry. The objective of this study was to evaluate growth and proteome differences between 5 genetic strains of broilers that yield WB and normal breast (NB) meat. Eight-week-old broilers were evaluated for the WB myopathy and divided into NB and WB groups. Differential expression of proteins was analyzed using 2-dimensional gel electrophoresis and LC-MS/MS to elucidate the mechanism behind the breast myopathy because of the genetic backgrounds of the birds. The percentages of birds with WB were 61.3, 68.8, 46.9, 45.2, and 87.5% for strains 1-5, respectively, indicating variability in WB myopathy among broiler strains. Birds from strains 1, 3, and 5 in the WB group were heavier than those in the NB group (P < 0.05). Woody breast meat from all strains were heavier than NB meat (P < 0.05). Within WB, strain 5 had a greater breast yield than strains 1, 3, and 4 (P < 0.0001). Woody breast from strains 2, 3, 4, and 5 had a greater breast yield than NB (P < 0.05). Six proteins were more abundant in NB of strain 5 than those of strains 2, 3, and 4, and these proteins were related to muscle growth, regeneration, contraction, apoptosis, and oxidative stress. Within WB, 14 proteins were differentially expressed between strain 5 and other strains, suggesting high protein synthesis, weak structural integrity, intense contraction, and oxidative stress in strain 5 birds. The differences between WB from strain 3 and strains 1, 2, and 4 were mainly glycolytic. In conclusion, protein profiles of broiler breast differed because of both broiler genetics and the presence of WB myopathy.

Early Postmortem Proteome Changes in Normal and Woody Broiler Breast Muscles.

Early postmortem changes in the whole muscle proteome from normal broiler (NB) and woody broiler (WB) breasts at 0 min, 15 min, 4 h, and 24 h after slaughter were analyzed using two-dimensional gel electrophoresis (2DE) and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Elongation factor 2, EH domain-containing protein 2, phosphoglycerate mutase 1 (PGAM1), and T-complex protein 1 subunit gamma were differentially abundant in both NB and WB muscles during the early postmortem storage. Twenty additional proteins were differentially abundant among four postmortem time points in either NB or WB muscles. In the postmortem WB, changes in protein degradation were observed, including the degradation of desmin fragments, ovotransferrin chain A, and troponin I chain I. Additionally, a few glycolytic proteins in the WB might have undergone post-translational modification, including enolase, phosphoglucomutase-1, PGAM1, and pyruvate kinase. These changes in protein biomarkers highlight the impact of WB myopathy on postmortem proteome changes and increase our understanding of the relationship between WB conditions, postmortem biochemistry, and meat quality.

Biomolecular Interactions Governing Fresh Meat Color in Post-mortem Skeletal Muscle: A Review.

Appearance is an important sensory property that significantly influences consumers' perceptions of fresh meat quality. Failure to meet consumer expectations can lead to rejection of meat products, concomitant loss in value, and potential production of organic waste. Immediately after animal harvest, skeletal muscle metabolism changes from aerobic to anaerobic. However, anoxic post-mortem muscle is biochemically active, and biomolecular interaction between myoglobin, mitochondria, metabolites, and lipid oxidation determines meat color. This review examines how metabolites and mitochondrial activity can influence myoglobin oxygenation and metmyoglobin reducing activity. Further, the review highlights recent research that has examined myoglobin redox dynamics, sarcoplasmic metabolite changes, and/or post-mortem biochemistry.

Skeletal muscle proteome analysis provides insights on high altitude adaptation of yaks.

The differences in proteome profile of longissimus thoracis (LT) muscles of yak (Bos grunniens) and cattle (Bos taurus) were investigated employing isobaric tag for relative and absolute quantification (iTRAQ) approach to identify differentially expressed proteins and to understand the cellular level adaptations of yaks to high altitudes. Fifty-two proteins were differentially expressed in the two species, among which 20 were up-regulated and 32 were down-regulated in yaks. Gene ontology (GO) annotation revealed that most of the differentially expressed proteins were involved in the molecular function of protein binding, catalytic activity, and structural activity. Protein-protein interaction analysis recognized 24 proteins (involved in structural integrity, calcium ion regulation, and energy metabolism), as key nodes in biological interaction networks. These findings indicated that mammals living at high altitudes could possibly generate energy by pronounced protein catabolism and glycolysis compared with those living in the plains. The key differentially expressed proteins included calsequestrin 1, prostaglandin reductase 1 and ATP synthase subunit O, which were possibly associated with the cellular and biochemical adaptation of yaks to high altitude. These key proteins may be exploited as candidate proteins for mammalian adaptation to high altitudes.

Muscle-specific color stability in fresh beef from grain-finished Bos indicus cattle.

OBJECTIVE: To investigate the color and oxidative stabilities of longissimus lumborum (LL) and psoas major (PM) muscles from grain-finished Bos indicus cattle in Brazil. METHODS: The LL and PM muscles were obtained 24 h post-mortem from eight (n = 8) Nellore bull carcasses, fabricated into 1.5-cm steaks, aerobically packaged, and stored at 4°C for nine days. Steaks were analyzed for myoglobin concentration, pH, instrumental color, metmyoglobin reducing activity (MRA) and lipid oxidation. RESULTS: The LL steaks exhibited greater (p<0.05) redness, color stability, and MRA than their PM counterparts on days 5 and 9. The LL and PM steaks demonstrated similar (p>0.05) lightness and yellowness on days 0, 5, and 9. On the other hand, PM steaks exhibited greater (p<0.05) myoglobin concentration, pH, and lipid oxidation than their LL counterparts. CONCLUSION: These results indicated that muscle source influenced the color and oxidative stabilities of beef from grain-finished Bos indicus animals. These results highlighted the necessity of muscle-specific strategies to improve the color stability of beef from grain-fed Bos indicus cattle.

Muscle-Specific Mitochondrial Functionality and Its Influence on Fresh Beef Color Stability.

Fresh beef color stability is a muscle-specific trait. Mitochondria remain biochemically active in postmortem beef muscles and influence meat color. Although several intrinsic factors governing muscle-specific beef color have been studied extensively, the role of mitochondrial functionality in muscle-dependent color stability is yet to be examined. Therefore, the objective of this study was to examine mitochondrial oxygen consumption rate (OCR), mitochondrial metmyoglobin reducing activity (MMRA), and instrumental color attributes in beef Longissimus lumborum (LL) and Psoas major (PM) during retail display. Using a split-plot design, six (n = 6) beef LL and PM muscles were fabricated into 2.54-cm-thick steaks, packaged in polyvinylchloride overwrap, and randomly assigned to instrumental color measurement for six days and mitochondrial isolation for days 0, 1, 3, or 5 of display at 4 °C. Mitochondria isolated from steaks were used to assess the effects of muscle and display time on OCR and MMRA. The PM steaks were less color-stable (p < 0.05) during display compared with the LL counterparts. For both muscles, OCR decreased during display, albeit the decrease was more rapid in PM than in the LL. Similarly, MMRA decreased during display for the LL and PM. However, this decrease was less (p < 0.05) for mitochondria from LL steaks, which were more resistant to display-mediated effects on OCR and MMRA. These results indicated that the muscle-specific differences in mitochondrial activity may contribute partially to the variations in color stability of beef LL and PM muscles. PRACTICAL APPLICATION: During retail display tenderloin steaks packaged in PVC overwrap discolor quicker than strip loin steaks. This research determines the basis for muscle-specific differences in color stability. The results indicate that mitochondria present in tenderloin lose its functionality faster than strip loin mitochondria. Developing strategies to minimize muscle-specific differences in mitochondrial changes can increase color stability and value of fresh beef.

Differential abundance of muscle proteome in cultured channel catfish (Ictalurus punctatus) subjected to ante-mortem stressors and its impact on fillet quality.

The effects of environmental and handling stress during catfish (Ictalurus punctatus) aquaculture were evaluated to identify the biochemical alterations they induce in the muscle proteome and their impacts on fillet quality. Temperature (25°C and 33°C) and oxygen (~2.5mg/L [L] and >5mg/L [H]) were manipulated followed by sequential socking (S) and transport (T) stress to evaluate changes in quality when fish were subjected to handling (25-H-ST; temperature-oxygen-handling), oxygen stress (25-L-ST), temperature stress (33-H-ST) and severe stress (33-L-ST). Instrumental color and texture of fillets were evaluated, and muscle proteome profile was analyzed. Fillet redness, yellowness and chroma decreased, and hue angle increased in all treatments except temperature stress (33-H-ST). Alterations in texture compared to controls were observed when oxygen levels were held high. In general, changes in the abundance of structural proteins and those involved in protein regulation and energy metabolism were identified. Rearing under hypoxic conditions demonstrated a shift in metabolism to ketogenic pathways and a suppression of the stress-induced changes as the severity of the stress increased. Increased proteolytic activity observed through the down-regulation of various structural proteins could be responsible for the alterations in color and texture.

Proteome basis of pale, soft, and exudative-like (PSE-like) broiler breast (Pectoralis major) meat.

Pale, Soft, and Exudative (PSE) broiler breast meat has poor protein functionality, which leads to quality problems and economic loss in the poultry industry. Proteomics has been applied to characterize the biochemical mechanisms governing tenderness, color, and water-holding capacity in meat. However, the proteome basis of PSE has not yet been characterized for broiler breast meat. Therefore, this study was conducted to determine the differences in meat quality (cooking loss and shear force), descriptive sensory characteristics, consumer acceptance, and whole muscle proteome between normal and PSE-like broiler breast meat. Male Hubbard × Cobb 500 birds (n = 1,050) were raised in commercial houses. Prior to harvest, a sample of the broilers (n = 900) were subjected to short-term stress (38°C for 2 h), and the remaining broilers (n = 150) were maintained at control conditions (21°C for 2 h). Broiler breast (Pectoralis major) meat was collected and characterized by pH24 and L*24 as normal (pH24 5.8 to 6.2, L*24 45 to 55) or PSE-like (pH24 5.4 to 5.7, L*24 55 to 65) samples. Normal broiler breast meat had lower shear force values than PSE-like meat (P < 0.05). Based on sensory descriptive analysis, normal cooked chicken breast meat was more tender and juicier than PSE-like breast meat (P < 0.05). Consumer sensory analysis results indicated that 81% of consumer panelists liked normal breast meat whereas 62% of the panelists liked PSE-like breast meat. Whole muscle proteome profiling identified fifteen differentially abundant proteins in normal and PSE-like broiler breast samples. Actin alpha, myosin heavy chain, phosphoglycerate kinase, creatine kinase M type, beta-enolase, carbonic anhydrase 2, proteasome subunit alpha, pyruvate kinase, and malate dehydrogenase were over-abundant (P < 0.05) in PSE-like broiler breast whereas phosphoglycerate mutase-1, alpha-enolase, ATP-dependent 6-phosphofructokinase, and fructose 1,6-bisphosphatase were over-abundant (P < 0.05) in normal meat. Thus, results indicated that differences in proteome abundance could be related to the meat quality differences between normal and PSE-like broiler breast meat.

Muscle-specific colour stability of blesbok (Damaliscus pygargus phillipsi) meat.

The increasing demand for meat from alternative species, such as blesbok (Damaliscus pygargus phillipsi), gives rise to the need for characterizing the quality attributes of fresh meat from these species. While muscle-specific colour stability has been extensively studied in conventional livestock, limited information is available on this phenomenon in game meat. Therefore, the objective of this study was to examine the colour stability of three major blesbok muscles, infraspinatus (IS), longissimus thoracis et lumborum (LTL) and biceps femoris (BF). Instrumental colour, surface myoglobin redox forms, and biochemical attributes influencing colour stability were measured on 2.5-cm steaks from blesbok IS, LTL, and BF during refrigerated storage under aerobic conditions for eight days. IS steaks consistently demonstrated higher (P≤0.05) redness, colour stability, and chroma than the LTL and BF steaks. These findings suggested that blesbok IS muscle is more colour-stable than its LTL and BF counterparts. The game industry may employ muscle-specific strategies to improve marketability of fresh blesbok meat.

Factors influencing internal color of cooked meats.

This manuscript overviews the pertinent research on internal color of uncured cooked meats, biochemical processes involved in meat cookery, and fundamental mechanisms governing myoglobin thermal stability. Heat-induced denaturation of myoglobin, responsible for the characteristic dull-brown color of cooked meats, is influenced by a multitude of endogenous (i.e., pH, muscle source, species, redox state) and exogenous (i.e., packaging, ingredients, storage) factors. The interactions between these factors critically influence the internal cooked color and can confuse the consumers, who often perceive cooked color to be a reliable indicator for doneness and safety. While certain phenomena in cooked meat color are cosmetic in nature, others can mislead consumers and result in foodborne illnesses. Research in meat color suggests that processing technologies and cooking practices in industry as well as households influence the internal cooked color. Additionally, the guidelines of many international public health and regulatory authorities recommend using meat thermometers to determine safe cooking endpoint temperature and to ensure product safety.

Color attributes and oxidative stability of longissimus lumborum and psoas major muscles from Nellore bulls.

The influence of muscle source on color stability of fresh beef from purebred Bos indicus cattle was investigated. Longissimus lumborum (LL) and psoas major (PM) muscles obtained from twelve (n=12) Nellore bull carcasses (24h post-mortem) were fabricated into 2.54-cm steaks, aerobically packaged, and stored at 4°C for nine days. Steaks were analyzed on day 0 for proximate composition and myoglobin concentration, whereas pH, instrumental color, metmyoglobin reducing activity (MRA), lipid oxidation, and protein oxidation were evaluated on days 0, 3, 6, and 9. LL steaks exhibited greater (P<0.05) redness, color stability, and MRA than PM counterparts. On the other hand, PM steaks demonstrated greater (P<0.05) myoglobin content, lipid oxidation, and protein oxidation than LL steaks. These results indicated the critical influence of muscle source on discoloration of fresh beef from Bos indicus animals and suggested the necessity to engineer muscle-specific strategies to improve color stability and marketability of beef from Bos indicus cattle.

Proteome basis for intramuscular variation in color stability of beef semimembranosus.

The objective of the present study was to characterize the proteome basis for intramuscular color stability variations in beef semimembranosus. Semimembranosus muscles from eight carcasses (n=8) were fabricated into 2.54-cm thick color-labile inside (ISM) and color-stable outside (OSM) steaks. One steak for sarcoplasmic proteome analysis was immediately frozen, whereas other steaks were allotted to retail display under aerobic packaging. Color attributes were evaluated instrumentally and biochemically on 0, 2, and 4days. Sarcoplasmic proteome was analyzed using two-dimensional electrophoresis and tandem mass spectrometry. ISM steaks demonstrated greater (P<0.01) abundance of glycolytic enzymes (fructose-bisphosphate aldolase A, phosphoglycerate mutase 2, and beta-enolase) and phosphatidylethanolamine-binding protein 1 than their OSM counterparts. Possible rapid post-mortem glycolysis in ISM, insinuated by over-abundance of glycolytic enzymes, could lead to rapid pH decline during early post-mortem, which in turn could potentially compromise its color stability. These results indicated that differential abundance of sarcoplasmic proteome contributes to intramuscular variations in beef color stability.

Post-mortem oxidative stability of three yak (Bos grunniens) muscles as influenced by animal age.

The influence of animal age and muscle source on the oxidative stability of yak steaks was examined. Longissimus thoracis (LT) muscles from yaks of different age groups (0.5, 1.5, 2.5, and 3.5 years), and three muscle sources of LT, Psoas major (PM), and Biceps femoris (BF) from yaks of 0.5, 1.5, and 2.5 years, were evaluated for metmyoglobin content, activity of antioxidant enzymes, and antioxidant capacity. Oxidative stability was influenced (P<0.05) by muscle source and animal age. LT steaks from 0.5, 1.5, and 2.5 year old yaks exhibited lower (P<0.05) metmyoglobin content than their PM and BF counterparts. Furthermore, LT steaks from 3.5 year old yaks demonstrated lower (P<0.05) metmyoglobin content and greater (P<0.05) activities of antioxidant enzymes than LT steaks from other age groups. These results indicated the necessity to develop muscle- and age-specific processing strategies to improve color and oxidative stability of yak meat.