Towards muscle-specific meat color stability of Chinese Luxi yellow cattle: A proteomic insight into post-mortem storage

Wu, Wei; Yu, Qunli; Fu, Yu; Tian, Xiaojing; Jia, Fei; Li, Xingmin; Dai, Ruitong

doi:10.1016/j.jprot.2015.10.027

Cited by 70 publications

(82 citation statements)

References 54 publications

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“…Joseph et al (2012) compared the sarcoplasmic proteome profile of beef LL and PM, and attributed the greater color stability of LL to the greater abundance of metabolic enzymes, antioxidant proteins, and chaperones compared to color-labile PM. Similarly, Wu et al (2016) reported several glycolytic and antioxidant proteins to be differentially abundant in LL and PM during postmortem storage (15 d) in Chinese Luxi yellow cattle. Clerens et al (2016) performed proteomic and peptidomic analysis of 4 muscles (LL, PM, ST, and infraspinatus) from New Zealand-raised Angus steers and reported significant intensity differences between many proteins, including hemoglobin subunit β, carbonic anhydrase 3, triosephosphate isomerase, phosphoglycerate mutase 2, serum albumin and β enolase.…”

Section: Sarcoplasmic Proteome Analysesmentioning

confidence: 86%

“…Protein deglycase DJ-1 protects cells against oxidative stress and cell death by acting as an oxidative stress sensor, redox-sensitive chaperone, and protease. The protein was more abundant in ST7 compared to ST0 (Table 12), and has been previously identified to be differentially abundant in sarcoplasmic proteome in relation to meat color (Joseph et al, 2012;Wu et al, 2016), tenderness (Jia et al, 2009), and water holding capacity (Hwang et al, 2005). In general, chaperone proteins can prevent protein aggregation and protein denaturation occurring during the muscle-to-meat conversion (Sayd et al, 2006).…”

Section: Chaperonesmentioning

confidence: 93%

“…Joseph et al (2012) compared the sarcoplasmic proteome of color-stable longissimus lumborum (LL) and color-labile psoas major (PM), and reported differential abundance of several proteins, including metabolic enzymes, antioxidant proteins, and chaperones. Further, Wu et al (2015Wu et al ( , 2016 reported differentially abundant sarcoplasmic proteins in LL, PM, and semitendinosus (ST) muscle from Luxi yellow cattle during postmortem storage for 0, 5, 10, and 15 d. Postmortem aging also influences the sarcoplasmic proteome, and aging alters meat quality traits (color, pH, and water holding capacity) in beef LL by affecting the sarcoplasmic protein patterns (Marino et al, 2014). Together these studies indicated that muscle source and aging can affect sarcoplasmic proteome profile, which in turn can influence meat color.…”

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confidence: 99%

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Changes in the Sarcoplasmic Proteome of Beef Muscles with Differential Color Stability during Postmortem Aging

Nair

Beach

et al. 2018

Meat and Muscle Biology

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Beef color is a muscle-specific trait, and sarcoplasmic proteome influences muscle-specific variations in beef color stability. Postmortem aging influences the color and sarcoplasmic proteome of beef muscles. Nonetheless, muscle-specific changes in sarcoplasmic proteome of beef muscles with differential color stability during aging have not been characterized yet. Therefore, our objective was to examine the changes in the sarcoplasmic proteome of 3 differentially color stable muscles from beef hindquarters during postmortem aging. Longissimus lumborum (LL), psoas major (PM), and semitendinosus (ST) separated from 8 (n = 8) beef carcasses (24 h postmortem) were subjected to aging in vacuum packaging (2°C) for 0, 7, 14, and 21 d. On each aging day, steaks were fabricated, and allotted to refrigerated storage (2°C) under aerobic packaging. Samples for proteome analysis obtained during fabrication were frozen at –80°C. Instrumental color and metmyoglobin reducing activity were evaluated on d 0, 3, and 6 of storage. Sarcoplasmic proteome was analyzed, and differentially abundant proteins were identified using mass spectrometry. Color attributes and biochemical parameters were influenced by muscle source and aging (P < 0.05); LL and ST had greater (P < 0.05) surface redness than PM. Aging also influenced surface redness, with 7-d aged steaks demonstrating greatest values (P < 0.05). Proteome analysis identified 135 protein spots differentially abundant (P < 0.05) between the muscles and aging time points indicating muscle-specific changes during aging. The identified proteins included glycolytic enzymes, proteins associated with energy metabolism, antioxidant proteins, chaperones, and transport proteins. Overall, the glycolytic enzymes were more abundant (P < 0.05) in color-stable muscles and at aging times with greater color stability, indicating that these proteins could be used as potential biomarkers for beef color.

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Section: Sarcoplasmic Proteome Analysesmentioning

confidence: 86%

Section: Chaperonesmentioning

confidence: 93%

mentioning

confidence: 99%

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Changes in the Sarcoplasmic Proteome of Beef Muscles with Differential Color Stability during Postmortem Aging

Nair

Beach

et al. 2018

Meat and Muscle Biology

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“…Beef color stability is a muscle-specific trait, and various muscles in a beef carcass discolor at different rates (Hunt and Hedrick, 1977a;O'Keeffe and Hood, 1982;McKenna et al, 2005). From this standpoint, the biochemical bases of intermuscular variations in beef color have been studied extensively (McKenna et al, 2005;Seyfert et al, 2006;Joseph et al, 2012;Wu et al, 2016;Nair et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

“…Proteomic approaches have characterized the fundamental basis of color stability variations in fresh beef, such as muscle-specificity (Joseph et al, 2012;Wu et al, 2016;Nair et al, 2018) and animal effect (Canto et al, 2015). Previous investigations (Nair et al, 2016) on beef ISM and OSM steaks (48 h postmortem) reported an increased abundance of glycolytic enzymes in sarcoplasmic proteome of ISM, which could possibly lead to a faster pH drop in ISM during the postmortem period while the carcass temperature is still high.…”

Section: Introductionmentioning

confidence: 99%

Intramuscular Variations in Color and Sarcoplasmic Proteome of Beef Semimembranosus during Postmortem Aging

Nair

Beach

et al. 2018

Meat and Muscle Biology

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Abstract:Beef semimembranosus exhibits intramuscular difference in color stability, and the inside region (ISM) of the muscle is color-labile, whereas the outside region (OSM) is color-stable. Variations in sarcoplasmic proteins are known to contribute to this intramuscular color difference. Sarcoplasmic proteome and beef color are affected by postmortem aging. The objective of the present study was to examine the effect of aging on intramuscular color variations and the sarcoplasmic proteome of beef semimembranosus. Semimembranosus muscles obtained from 8 beef carcasses (n = 8) were subjected to aging at 2°C for 0, 7, 14, and 21 d. On each aging day, the muscles were fabricated into ISM and OSM steaks and allotted to refrigerated storage (2°C) under aerobic packaging. Instrumental color and metmyoglobin reducing activity were evaluated on d 0, 3, and 6 of storage. Samples frozen on d 0 and d 21 of aging were utilized for sarcoplasmic proteome analysis. Color attributes of both ISM and OSM steaks were influenced by aging, with steaks aged for 21 d having the lowest (P < 0.05) color stability. The ISM steaks had greater (P < 0.05) lightness than OSM counterparts, and the difference in lightness was not negated by aging. The ISM and OSM had similar (P > 0.05) redness on d 0 of storage, whereas ISM had lower (P < 0.05) redness compared to OSM on d 3 and d 6 of storage. Several proteins associated with glycolysis and energy metabolism were of greater abundance (P < 0.05) in OSM than in ISM after 21-d aging. Furthermore, the influence of 21-d aging on sarcoplasmic proteome was observed at a greater extent in OSM than in ISM, indicating that the effect of aging on sarcoplasmic proteome of beef semimembranosus was influenced by the location within the muscle.

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Estimation of the proteome affecting changes in tenderness of yak meat during storage by label‐free mass spectrometry

Liu

2022

Veterinary Medicine & Sci

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Background Tenderness is the main quality of meat products. However, the meat tenderness formation is a complex biological process, and pathways and proteins that affect the tenderness of yak meat are unknown. Methods Label‐free proteomics method was used to explore the effects of differentially expressed proteins on the tenderness of yak skeletal muscle (tenderloin) during post‐mortem storage (0, 3, and 7 days) at 3 ± 1°C. Results The tenderness of yak skeletal muscle improved significantly during storage. A total of 91 differentially expressed proteins of yak skeletal muscle during post‐mortem storage were identified by the following comparisons: day 3 versus 0, day 7 versus 0, and day 7 versus 3. NDUFS6, CYCS, COX6A2, LDB3, HSPB7, TPM4, TAGLN, COL1A1, LUM, MYH11, ACTC1, and MYOZ1 proteins showed a significant difference during yak skeletal muscle post‐mortem storage. Furthermore, bioinformatics analyses revealed that the identified proteins were related to carbon metabolism, citrate cycle, glycolysis, oxidative phosphorylation, and RNA degradation. Conclusion The results of the present study could provide proteomic insights into changes in yak skeletal muscle tenderness during storage and may be a valuable resource for future investigations.

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Towards muscle-specific meat color stability of Chinese Luxi yellow cattle: A proteomic insight into post-mortem storage

Cited by 70 publications

References 54 publications

Changes in the Sarcoplasmic Proteome of Beef Muscles with Differential Color Stability during Postmortem Aging

Changes in the Sarcoplasmic Proteome of Beef Muscles with Differential Color Stability during Postmortem Aging

Intramuscular Variations in Color and Sarcoplasmic Proteome of Beef Semimembranosus during Postmortem Aging

Estimation of the proteome affecting changes in tenderness of yak meat during storage by label‐free mass spectrometry

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