Differential abundance of sarcoplasmic proteome explains animal effect on beef Longissimus lumborum color stability

Canto, Anna C.V.C.S.; Suman, Surendranath P.; Nair, Mahesh N.; Li, Shuting; Rentfrow, G.; Beach, Carol M.; Silva, Teofilo J.P.; Wheeler, T. L.; Shackelford, S. D.; Grayson, A.L.; McKeith, Russell O.; King, D. A.

doi:10.1016/j.meatsci.2014.11.011

Cited by 105 publications

(106 citation statements)

References 76 publications

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“…In agreement, the Mb concentration was not found to be indicative of color stability in blesbok muscles as well (Neethling et al, 2016). Similarly, other studies have also reported that the relationship between Mb concentration and color stability in beef muscles is inconclusive (Sammel et al, 2002;McKenna et al, 2005;Canto et al, 2015).…”

Section: Biochemical Attributes Influencing Surface Color Stabilitymentioning

confidence: 63%

Color Stability of Fallow Deer (Dama dama) Infraspinatus, Longissimus Thoracis et Lumborum, and Biceps Femoris Muscles During Refrigerated Storage

Neethling

Sigge

Hoffman

et al. 2018

Meat and Muscle Biology

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Fallow deer (Dama dama) meat comprises a relatively small proportion of the game meat market in South Africa, despite having huge potential. To exploit its market potential, the quality attributes of fresh meat from fallow deer need to be characterized. Limited studies have been undertaken on the color stability of economically important muscles in game species. Therefore, the objective of the present study was to examine the color stability of 3 major muscles, i.e., infraspinatus (IS), longissimus thoracis et lumborum (LTL), and biceps femoris (BF), from fallow deer. The IS, LTL, and BF muscles were removed from both sides of 12 (6 male and 6 female) fallow deer carcasses. The muscles were fabricated into 2.5-cm steaks. The steaks were aerobically over-wrapped and stored at 2°C for 8 d. Meat pH, instrumental color, surface myoglobin redox forms, and metmyoglobin reducing activity were evaluated at specific intervals. Data were analyzed using mixed model repeated measures ANOVA, with gender, muscle, and time as fixed effects. The IS muscle exhibited greater (P < 0.05) pH, surface redness, color stability, oxymyoglobin content, and metmyoglobin reducing activity than the LTL and BF counterparts. In addition, surface metmyoglobin and total iron contents were lower in IS than in LTL and BF. While the IS demonstrated stable redness throughout the storage, the LTL and BF remained color stable only for 1 to 2 d. These findings suggested that fallow deer IS muscle is more color stable than the LTL and BF during refrigerated storage.

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Section: Biochemical Attributes Influencing Surface Color Stabilitymentioning

confidence: 63%

Color Stability of Fallow Deer (Dama dama) Infraspinatus, Longissimus Thoracis et Lumborum, and Biceps Femoris Muscles During Refrigerated Storage

Neethling

Sigge

Hoffman

et al. 2018

Meat and Muscle Biology

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“…Overall, a differential abundance of proteins related to energy metabolism has been previously reported (Joseph et al, 2012;Canto et al, 2015) to be associated with differences in beef color stability, with color-stable steaks demonstrating greater abundance of these proteins than their colorlabile counterparts. However, in the present study, both OSM0 and OSM21 steaks had similar redness after 21-d aging (P = 0.3837).…”

Section: Effect Of 21-d Aging On Sarcoplasmic Proteome Of Osmmentioning

confidence: 76%

“…1. Multiple protein spots with similar molecular weight, but different isoelectric point (pI), were identified as the same protein, which could be attributed to the occurrence of protein isoforms or post-translational modifications such as phosphorylation (Canto et al, 2015;Anderson et al, 2014). However, protein phosphorylation was not analyzed in the present study to confirm this possibility.…”

Section: Sarcoplasmic Proteome Variations Between Ism and Osm Aged Fomentioning

confidence: 78%

“…The myoglobin spots of interest in the gels had similar molecular mass, but with different isoelectric point (pI), which is indicative of post-translational modifications such as phosphorylation (Anderson et al, 2014). Previous research also reported differential abundance of myo- globin isoforms between color-stable and color-labile beef longissimus lumborum (Canto et al, 2015). These authors reported a greater abundance of a myoglobin isoform in color-labile steaks compared to color-stable steaks, suggesting that myoglobin post-translational modifications may influence meat color.…”

Section: Effect Of 21-d Aging On Sarcoplasmic Proteome Of Osmmentioning

confidence: 94%

“…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%

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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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Proteomics in food: Quality, safety, microbes, and allergens

et al. 2016

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Food safety and quality and their associated risks pose a major concern worldwide regarding not only the relative economical losses but also the potential danger to consumer's health. Customer's confidence in the integrity of the food supply could be hampered by inappropriate food safety measures. A lack of measures and reliable assays to evaluate and maintain a good control of food characteristics may affect the food industry economy and shatter consumer confidence. It is imperative to create and to establish fast and reliable analytical methods that allow a good and rapid analysis of food products during the whole food chain. Proteomics can represent a powerful tool to address this issue, due to its proven excellent quantitative and qualitative drawbacks in protein analysis. This review illustrates the applications of proteomics in the past few years in food science focusing on food of animal origin with some brief hints on other types. Aim of this review is to highlight the importance of this science as a valuable tool to assess food quality and safety. Emphasis is also posed in food processing, allergies, and possible contaminants like bacteria, fungi, and other pathogens.

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Differential abundance of sarcoplasmic proteome explains animal effect on beef Longissimus lumborum color stability

Cited by 105 publications

References 76 publications

Color Stability of Fallow Deer (Dama dama) Infraspinatus, Longissimus Thoracis et Lumborum, and Biceps Femoris Muscles During Refrigerated Storage

Color Stability of Fallow Deer (Dama dama) Infraspinatus, Longissimus Thoracis et Lumborum, and Biceps Femoris Muscles During Refrigerated Storage

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

Proteomics in food: Quality, safety, microbes, and allergens

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