Reverse electron transport effects on NADH formation and metmyoglobin reduction

Belskie, Kaylin; Buiten, Charlene B. Van; Ramanathan, Ranjith; Mancini, R.A.

doi:10.1016/j.meatsci.2015.02.012

Cited by 40 publications

(25 citation statements)

References 13 publications

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“…NADH in LL and SM muscle was higher than that in PM muscle. NADH plays a critical role in maintaining the color stability of meat due to its ability to reduce metmyoglobin (Belskie et al., ; Ramanathan et al., , ). The higher NADH content in LL and SM muscles accounts for the better color stability determined in this study, which is in agreement with literature (Bjelanovic et al., ; Kim et al., ).…”

Section: Resultsmentioning

confidence: 99%

“…Metmyoglobin reducing activity (MRA) is probably the most important intrinsic factor to maintain the color stability of beef (Ledward, 1985;Bekhit & Faustman, 2005). NADH is necessary for the reduction of metmyoglobin, either enzymatic or non-enzymatic reduction (Belskie, Van Buiten, Ramanathan, & Mancini, 2015;Kim et al, 2006;Kim, Keeton, Smith, Berghman, & Savell 2009b). Lactate Dehydrogenase (LDH) and Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are the only two dehydrogenases which catalyze the production of NADH in glycolysis.…”

Section: Introductionmentioning

confidence: 99%

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Meat Color Stability of Ovine Muscles Is Related to Glycolytic Dehydrogenase Activities

Xin

et al. 2018

Journal of Food Science

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The relationship between glycolytic dehydrogenase, including glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH), lactic dehydrogenase (LDH), and meat color stability was studied in this study using ovine muscle. Three different ovine muscles, including M. longissimus lumborum (LL), M. semimembranosus (SM), and M. psoas major (PM), were obtained (n = 10, respectively), and then displayed for 7 days at 4 °C. The LL and SM muscle had higher surface redness, higher (P < 0.05) GAPDH activity, nicotinamide adenine dinucleotide (NADH) content, and lower (P < 0.05) LDH‐B activity than PM muscles during display. The PM muscle had the worst color stability and lowest NADH content. These results suggest that variation in color stability of physiologically different muscles may be affected by glycolysis dehydrogenases. Comparatively, our data showed that GAPDH may play a more important role than LDH‐B to maintain meat color stability.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Meat Color Stability of Ovine Muscles Is Related to Glycolytic Dehydrogenase Activities

Xin

et al. 2018

Journal of Food Science

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“…After slaughter, enzymatic systems involved in metmyoglobin reduction are continuously depleted as time progresses, thus the meat color is affected. Belskie and others () reported that succinate and NAD can generate NADH in bovine tissue postmortem by reverse electron flow, which can be used to reduce metmyoglobin by 2 pathways: electron transport‐mediated and metmyoglobin reductase NADH‐dependent. The discoloration of red meat is the result of oxymyoglobin (cherry red color) from fresh red meat oxidation to metmyoglobin (brown color).…”

Section: Heme Protein Oxidationmentioning

confidence: 99%

Mechanisms of Oxidative Processes in Meat and Toxicity Induced by Postprandial Degradation Products: A Review

Papuc¹,

Goran²,

Predescu³

et al. 2016

Comp Rev Food Sci Food Safe

232

142

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Antioxidant system loss after slaughtering, reactive species production, cell disruption, contact with oxygen and light, heme and nonheme iron, and irradiation starts up mainly by 2 related oxidative processes: lipid peroxidation and protein oxidation. Products generated in these processes are responsible for meat quality loss, and some of them are suspected to be toxic to humans. This review article is focused on reactive species implicated in oxidative processes in meat, on lipid peroxidation mechanisms, heme protein, and nonheme protein oxidation, and on some toxic oxidation and digestion products. Nonenzymatic fatty acid peroxidation is exemplified by an arachidonic acyl group, and the initiation of chain reaction can be described by 3 pathways: singlet oxygen, hydroxyl radical from the Fenton reaction, and perferrylmyoglobin. Enzymatic oxidation of fatty acids is exemplified using linoleic acid, and the main characteristics of lipoxygenase are also presented. Heme protein oxidation is described in an interrelation with lipid peroxidation and the significance for food quality is shown. For protein oxidation, 3 different mechanism types are described: oxidation of amino acid residues, oxidation of protein backbone, and reactions of proteins with carbonyl compounds from lipid peroxidation. The effects of oxidative damage on protein properties and bioavailability are also shown. At the end of each oxidative process, the postprandial toxicity induced by oxidation products and the dietary degradation products are presented. Also discussed are reports by some researchers who suggest that dietary lipid and protein oxidation products and heme iron from red meat are in part cytotoxic and/or genotoxic.

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“…Competition for oxygen between myoglobin and mitochondria affects initial bloomed color intensity and oxymyoglobin formation (Faustman & Cassens, 1990). Mitochondria also promote color stability by providing reducing equivalents for metmyoglobin reduction (Belskie, Van Buiten, Ramanathan, & Mancini, 2015).…”

Section: Introductionmentioning

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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Reverse electron transport effects on NADH formation and metmyoglobin reduction

Cited by 40 publications

References 13 publications

Meat Color Stability of Ovine Muscles Is Related to Glycolytic Dehydrogenase Activities

Meat Color Stability of Ovine Muscles Is Related to Glycolytic Dehydrogenase Activities

Mechanisms of Oxidative Processes in Meat and Toxicity Induced by Postprandial Degradation Products: A Review

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

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