Myoglobin Redox Form Stabilization by Compartmentalized Lactate and Malate Dehydrogenases

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

doi:10.1021/jf100714g

Cited by 28 publications

(17 citation statements)

References 39 publications

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“…Nevertheless, metabolism of carbohydrates can be attributed to the generation of reducing equivalents such as NADH and FADH (flavin adenine dinucleotide reduced). Mitochondrial content is greater in PM than LL (Mohan et al, 2010;Ramanathan et al, 2015) which can significantly influence the utilization of metabolites postmortem. One hundred and forty-one metabolites were identified in LL and PM.…”

Section: Resultsmentioning

confidence: 99%

Metabolite Profile Differences between Beef Longissimus and Psoas Muscles during Display

Abraham

Dillwith

Mafi

et al. 2017

Meat and Muscle Biology

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Abstract:The objective of this research was to compare metabolite profiles between beef longissimus and psoas muscles during display. Beef short loins were collected 3 d postmortem (n = 10). Steaks were cut from each longissimus lumborum (LL) and psoas major (PM) muscle and displayed under retail conditions for 7 d. Surface color, biochemical properties, and metabolites were analyzed during storage. PM decreased in redness (P < 0.05) by d 3 of display compared with LL. There were differences in metabolite concentrations (P < 0.05) between each muscle type at each time point. Sugars, amino acids, tricarboxylic acid cycle intermediates, and glycolytic substrates were detected in both muscles. Glycolytic metabolites such as pyruvic acid, glucose-6-phosphate, and fructose were greater (P < 0.05) in LL than PM at all display times. On d 0, the intensity of pyruvic acid in LL and PM were 142 and 42, respectively. Citric acid and succinic acid were lower on d 0, but were greater (P < 0.05) in LL compared with PM by d 7 of display. Carnitine was lower (P < 0.05) in LL than PM at all display times. On d 7, carnitine level in LL was 4.1 while in PM was 13,500. The results suggest that in addition to muscle-specific differences in mitochondrial and enzyme activities, inherent metabolite differences also may contribute to muscle color stability.

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Section: Resultsmentioning

confidence: 99%

Metabolite Profile Differences between Beef Longissimus and Psoas Muscles during Display

Abraham

Dillwith

Mafi

et al. 2017

Meat and Muscle Biology

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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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“…Wittenberg & Wittenberg (2007) reported that oxygen can be delivered to cytochrome c oxidase in the inner membrane via facilitated diffusion, which results from increasing oxygen availability that occurs when oxymyoglobin is close to mitochondria. Mohan et al (2010) reported that the differences in cytochrome c oxidase activity among the three muscles (LL > psoas major > semitendinosus) corresponded well with metmyoglobin reducing activity and colour stability differences exhibited by these muscles. Ke et al (2017) reported approximately 1.8-fold difference in mitochondrial content between beef psoas major and LL muscles and suggested that greater oxygen consumption rate may possibly be detrimental to colour stability.…”

Section: Figurementioning

confidence: 77%

Supranutritional supplementation of vitamin E influences mitochondrial proteome profile of post-mortem <i>longissimus lumborum</i> from feedlot heifers

Zhai¹,

Suman²,

Nair³

et al. 2019

SA J. An. Sci.

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Supplementation of vitamin E improves beef colour stability by minimizing lipid oxidation-induced myoglobin oxidation. Mitochondria affect myoglobin redox stability, and dietary vitamin E influences mitochondrial functionality in skeletal muscles. Nonetheless, the influence of vitamin E on the mitochondrial proteome of beef skeletal muscles has yet to be investigated. Therefore, the objective of this study was to examine the effect of dietary vitamin E on mitochondrial proteome of post-mortem beef longissimus lumborum (LL) muscle. Beef LL muscle samples (24 hours post-mortem) were obtained from the carcasses of nine (n = 9) vitamin E-fed (VITE) (1000 IU vitamin E for 89 days) and nine (n = 9) control (CONT) (diet without supplemental vitamin E) heifers. The mitochondrial proteome was analysed using two-dimensional gel electrophoresis and mass spectrometry, and nine differentially abundant spots were identified. All the differentially abundant spots were over-abundant in CONT, and the proteins were electron transport chain enzymes (NADH dehydrogenase iron-sulphur protein 8, NADH dehydrogenase flavoprotein 2, and cytochrome c oxidase subunit 5B), metabolic enzymes (succinate-CoA ligase (ADP-forming) subunit beta; dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; pyruvate dehydrogenase protein X component), and enzymes involved in ATP regeneration (creatine kinase S-type). The low abundance of these proteins in VITE may decrease mitochondrial activity, resulting in low oxidative activity. These findings suggest that the strong antioxidant activity of vitamin E leads to less expression of mitochondrial oxidative enzymes in beef skeletal muscles.

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Myoglobin Redox Form Stabilization by Compartmentalized Lactate and Malate Dehydrogenases

Cited by 28 publications

References 39 publications

Metabolite Profile Differences between Beef Longissimus and Psoas Muscles during Display

Metabolite Profile Differences between Beef Longissimus and Psoas Muscles during Display

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

Supranutritional supplementation of vitamin E influences mitochondrial proteome profile of post-mortem <i>longissimus lumborum</i> from feedlot heifers

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