The effects of lipid peroxidation products 4-HNE and 4-ONE on lactate dehydrogenase activity, myoglobin redox stability, and mitochondrial structural integrity
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Meat quality is affected by many components, such as sarcoplasmic enzymes, mitochondria, and myoglobin. Rancidity of lipids and hemoprotein oxidation are interlinked. Both of these constituents’ reactions are important in muscle as well as meat. In a living system, pathways exist to prevent harmful oxidation, detoxify the compounds resulting from lipid peroxidation, and reduce myoglobin to its functional redox state. In post mortem skeletal muscle, however, these systems rapidly deplete cofactors and substrates that are necessary to carry out enzymatic functions. As a result, membrane lipids begin to oxidize, leading to rancidity. Myoglobin, the primary pigment in meat, begins to oxidize to metmyoglobin, leading to meat quality loss. This research study seeks to determine how two lipid peroxidation products, 4-hydroxy-2-nonenal, and 4-oxo-2-nonenal, accelerate quality loss. Results suggest that 4-ONE inhibits lactate dehydrogenase activity, myoglobin stability, and mitochondrial integrity.