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The effects and specificity of dietary supplementation of EconomasETM (EcoE), mainly consisting of organic selenium (0.15 or 0.30 mg/kg feed; Se) or of vitamin E (100 or 200 mg/kg feed; VE), on lipid oxidation were evaluated in rabbit hamburgers during refrigerated storage. Oxidation data obtained by thiobarbituric acid-reactive substances (TBARS) spectrophotometric analysis and solid-phase microextraction (SPME) coupled with gas chromatography (GC) to determine hexanal content were compared. The relationships between oxidation levels, colour and pH and the discriminability of EcoE- or VE-treatment compared with control were also examined. TBARS content decreased in both VE and EcoE groups, while hexanal showed lower values only in the VE100 dietary group. The colour parameters were compatible with acceptable product quality and seemed to parallel the TBARS values up to the second day storage. Both VE and EcoE improved oxidative stability without affecting the sensory properties, but the VE effect appeared to more specifically hamper lipid oxidation, as evidenced by the determination and quantification of hexanal, a specific product of fatty acid peroxidation.

Under aerobic conditions, mitochondrial oxidative phosphorylation (OXPHOS) converts the energy released by nutrient oxidation into ATP, the currency of living organisms. The whole biochemical machinery is hosted by the inner mitochondrial membrane (mtIM) where the protonmotive force built by respiratory complexes, dynamically assembled as super-complexes, allows the F1FO-ATP synthase to make ATP from ADP + Pi. Recently mitochondria emerged not only as cell powerhouses, but also as signaling hubs by way of reactive oxygen species (ROS) production. However, when ROS removal systems and/or OXPHOS constituents are defective, the physiological ROS generation can cause ROS imbalance and oxidative stress, which in turn damages cell components. Moreover, the morphology of mitochondria rules cell fate and the formation of the mitochondrial permeability transition pore in the mtIM, which, most likely with the F1FO-ATP synthase contribution, permeabilizes mitochondria and leads to cell death. As the multiple mitochondrial functions are mutually interconnected, changes in protein composition by mutations or in supercomplex assembly and/or in membrane structures often generate a dysfunctional cascade and lead to life-incompatible diseases or severe syndromes. The known structural/functional changes in mitochondrial proteins and structures, which impact mitochondrial bioenergetics because of an impaired or defective energy transduction system, here reviewed, constitute the main biochemical damage in a variety of genetic and age-related diseases.