Effects of malate, lactate, and pyruvate on myoglobin redox stability in homogenates of three bovine muscles

Mohan, Anand; Hunt, Melvin C.; Barstow, Thomas J.; Houser, T. A.; Muthukrishnan, S.

doi:10.1016/j.meatsci.2010.04.030

Cited by 37 publications

(27 citation statements)

References 16 publications

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“…In addition, PM had greater decrease in mitochondrial content than LL. Mohan, Hunt, Barstow, Houser, and Muthukrishnan () reported approximately 1.21‐fold greater mitochondrial concentration in beef PM compared with LL muscle in 10‐day aged samples and a more reduction in PM mitochondrial content with aging time than LL. The lower mitochondrial content may be responsible for decrease in OCR of PM mitochondria than LL mitochondria.…”

Section: Discussionmentioning

confidence: 99%

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

Mancini

Belskie

Suman

et al. 2018

Journal of Food Science

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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.

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Section: Discussionmentioning

confidence: 99%

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

Mancini

Belskie

Suman

et al. 2018

Journal of Food Science

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“…Cytoplasmic malate dehydrogenase is responsible for shuttling NADH across the mitochondrial membrane via the malate-aspartate shuttle, whereas mitochondrial malate dehydrogenase is a principal enzyme of the citric acid cycle (operated within mitochondria) which catalyzes the conversion of oxaloacetate and malate utilizing the NAD/NADH coenzyme system (Minarik et al, 2002). Mohan et al (2010aMohan et al ( , 2010b reported that malate decreases metmyoglobin formation in beef muscle homogenates by generating NADH utilizing the malate dehydrogenase enzyme system, which is subsequently used for metmyoglobin reduction. The differential abundance of these enzymes indicates that different muscles could differ in their response to malate enhancement.…”

Section: Proteins Related To Energy Metabolismmentioning

confidence: 99%

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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“…The shelf life of fresh meat is closely associated with color stability. With discoloration, meat loses retail value and may even be discarded (Mohan et al 2010). The amount and the state of myoglobin determine meat color; the oxidation of myoglobin to metmyoglobin during storage is responsible for the deterioration of meat color (Bekhit et al 2001;McKenna et al 2005).…”

mentioning

confidence: 99%

Color stability and antioxidant capacity of yak meat as affected by feeding with pasture or grain

et al. 2015

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-R. 2015. Color stability and antioxidant capacity of yak meat as affected by feeding with pasture or grain. Can. J. Anim. Sci. 95: 189Á195. The objective of the present study was to analyze the effect of pasture or grain on color stability and antioxidant capacity of M. longissimus lumborum (LL) from pasture-fed (PF) or grain-fed (GF) yaks. The color stability and metmyoglobin percentage (MetMb%) were determined during 9 d of aerobic refrigerated storage. The antioxidant capacity was estimated by the total phenolics content, Trolox equivalent antioxidant capacity (TEAC), and ferric reducing antioxidant power (FRAP). Compared with the GF group, the LL from the PF group showed significantly (PB0.05) higher redness (a* values), with lower decline rate in a* values (PB0.05) over 1 to 7 d of refrigerated storage. The LL from the PF group had a significantly (PB0.05) lower metmyoglobin accumulation rate. At the end of storage, the muscle's MetMb% of the PF and GF group were 46.33 and 56.66%, respectively. The PF group showed significantly higher total phenolics content ('23.94%; PB0.05) in muscles, resulting in greater TEAC and FRAP, which were 24.81 and 3.99% higher than the GF group (PB0.05), respectively. In conclusion, the pasture enhanced antioxidant capacity of yak meat and contributed to improve the meat color stability.Key words: Yak meat, color stability, Antioxidant capacity, phenolics, pasture, grain Chen, C., Han, L., Yu, Q.-L. et Li, R.-R. 2015. La stabilite´de couleur et la capacite´antioxydante de la viande de yak selon une alimentation au paˆturage ou aux grains. Can. J. Anim. Sci. 95: 189Á195. L'objectif de la pre´sente e´tude e´tait d'analyser les effets de l'alimentation au paˆturage ou aux grains sur la stabilite´de couleur et la capacite´antioxydante du muscle M. longissimus lumborum (LL) chez les yaks nourris au paˆturage (PF Á « pasture-fed ») ou aux grains (GF Á « grain-fed »). La stabilite´de couleur et le pourcentage de metmyoglobine (MetMb%) ont e´te´de´termine´s durant 9 jours d'entreposage re´frige´re´en conditions ae´robiques. La capacite´antioxydante a e´te´estime´e par de´termination des contenus totaux en compose´s phe´noliques, capacite´antioxydante e´quivalente Trolox (TEAC Á « Trolox equivalent antioxidant capacity »), et la puissance antioxydante de re´duction ferrique (FRAP Á « ferric reducing antioxidant power »). Par rapport au groupe GF, le LL du groupe PF de´montrait une rougeur (a* values) significativement plus e´leve´e (PB0,05), avec plus faible taux de de´clin de a* values (PB0,05) au cours des jours 1 a`7 d'entreposage re´frige´re´. Le LL du groupe PF avait un taux d'accumulation de metmyoglobine significativement plus bas (PB0,05) a`la fin de la pe´riode d'entreposage, le MetMb% des muscles des groupes PF et GF e´taient de 46,33 % et 56,66 %, respectivement. Le groupe PF avait une plus forte teneur en compose´s phe´noliques ('23,94 %; PB0,05) dans les muscles, ce qui se soldait par de plus grandes valeurs de TEAC et de FRAP, qui e´taient de 24,81 % et 3,99 % plus e´leve...

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Effects of malate, lactate, and pyruvate on myoglobin redox stability in homogenates of three bovine muscles

Cited by 37 publications

References 16 publications

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

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

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

Color stability and antioxidant capacity of yak meat as affected by feeding with pasture or grain

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