Postmortem oxygen consumption by mitochondria and its effects on myoglobin form and stability.
ABSTRACT The objective of this study was to assess the morphological integrity and functional potential of mitochondria from postmortem bovine cardiac muscle and evaluate mitochondrial interactions with myoglobin (Mb) in vitro. Electron microscopy revealed that mitochondria maintained structural integrity at 2 h postmortem; prolonged storage resulted in swelling and breakage. At 2 h, 96 h, and 60 days postmortem, the mitochondrial state III oxygen consumption rate (OCR) and respiratory control ratio decreased with time at pH 7.2 and 5.6 (p < 0.05). Mitochondria isolated at 60 days did not exhibit ADP-induced transitions from state IV to state III oxygen consumption. Tissue oxygen consumption also decreased with time postmortem (p < 0.05). Mitochondrial oxygen consumption was inhibited by decreased pH in vitro (p < 0.05). In a closed system, mitochondrial respiration resulted in decreased oxygen partial pressure (pO(2)) and enhanced conversion of oxymyoglobin (OxyMb) to deoxymyoglobin (DeoMb) or metmyoglobin (MetMb). Greater mitochondrial densities caused rapid decreases in pO(2) and favored DeoMb formation at pH 7.2 in closed systems (p < 0.05); there was no effect on MetMb formation (p > 0.05). MetMb formation was inversely proportional to mitochondrial density at pH 5.6 in closed systems. Mitochondrial respiration in open systems resulted in greater MetMb and DeoMb formation at pH 5.6 and pH 7.2, respectively, vs controls (p < 0.05). The greatest MetMb formation was observed with a mitochondrial density of 0.5 mg/mL at both pH values in open systems. Mitochondrial respiration facilitated a shift in Mb form from OxyMb to DeoMb or MetMb, and this was dependent on pH, oxygen availability, and mitochondrial density.
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ABSTRACT: Spectrophotometric measures were used to determine the redness:browness (R630/R580) of 4238 lamb longissimus muscle after 3days under simulated display. The results were analysed using linear mixed effects models. Environmental factors represented by effects such as kill group and site of production produced the greatest variation of up to 2.76 units in R630/R580. Isocitrate dehydrogenase activity, reflecting muscle oxidative capacity, reduced R630/R580 by 0.5 units. Selection for high muscling sires increased R630/R580 by 0.27 units, likely due to changes in muscle oxidative capacity. Lamb carcass weight also increased R630/R580 by 0.5 units. Analysis of genotypic factors influencing lamb size and growth rate such as sire type and dam breed further supported that increased growth rate improves meat R630/R580. Our findings suggest that breeding for increased growth rate and increased muscle weight could result in Australian lamb meat retaining its red colour for extended periods whilst on display.Meat Science 09/2013; · 2.75 Impact Factor
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ABSTRACT: Our objective was to evaluate the influence of lactate on in vitro redox stability and thermostability of beef, horse, pork, and sheep myoglobins. Lactate (200mM) had no effect (P>0.05) on redox stability at physiological (pH7.4, 37°C) and meat (pH5.6, 4°C) conditions. However, lactate increased (P<0.05) metmyoglobin formation at a condition simulating stressed live skeletal muscle (pH6.5, 37°C). The redox stability of myoglobins at stressed live skeletal muscle and meat conditions was species-specific (P<0.05). Myoglobin thermostability at 71°C was lower (P<0.05) in the presence of lactate compared with controls and was influenced (P<0.05) by species. The results of the present study indicate that the effects of lactate on myoglobin are temperature and pH dependent. The observed lack of influence of lactate on myoglobin redox stability at meat condition suggests that the color stability of lactate-enhanced fresh meat is not due to direct interactions between the ingredient and the heme protein.Meat Science 08/2013; 96(1):408-412. · 2.75 Impact Factor
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ABSTRACT: Research suggests that NADH formed from lactate addition can increase mitochondrial oxygen consumption. However, limited research has assessed the subsequent effects of lactate-mediated mitochondrial oxygen consumption on oxymyoglobin. Therefore, our objective was to assess the effects of bovine mitochondrial oxygen consumption on oxymyoglobin in the presence of lactate, LDH, and NAD. Isolated beef cardiac and skeletal muscle mitochondria (n=5) were reacted with lactate (40mM), LDH (100units), and NAD (0.02mM) to initiate oxygen consumption. Myoglobin redox state was measured to assess the effects of oxygen consumption on oxymyoglobin. The addition of lactate-LDH-NAD to mitochondria increased (p<0.05) both oxygen consumption and conversion of oxymyoglobin to deoxymyoglobin compared with control mitochondria without substrates. The addition of antimycin A to mitochondria decreased oxygen consumption and deoxymyoglobin formation (p<0.05). The results suggest that increased oxygen consumption can influence myoglobin redox state and this effect might be partially responsible for the darkening effect in lactate enhanced beef.Meat Science 12/2012; 93(4):893-897. · 2.75 Impact Factor