Collapse of the endogenous antioxidant enzymes in post-mortem broiler thigh muscles triggers oxidative stress and impairs water-holding capacity
This study was conducted to investigate the effect of the collapse of the endogenous antioxidant enzymes, namely, catalase (CAT), glutathione peroxidase (GSH-Px) and superoxide dismutase (SOD) in post-mortem (PM) chicken thigh muscles on the extent of lipid and protein oxidation and the functionality of the muscle in terms of water-holding. To fulfil this objective, the samples were divided into two treatments: one group of muscles (n = 8) was subjected to delay cooling (DC) (at ~ 37 °C for 200 min PM) and then stored at 4 °C for 24 h. The second group (n = 8) was subjected to a normal cooling (NC): samples were immediately chilled at 4 °C for 24 h. DC samples presented a decrease in 16% of CAT, 25% GSH-Px and 20% SOD activity in relation to NC. Consistently, an increase of 36% of total carbonyl, 15% of Schiff bases and 27% of TBA-RS and 14% of tryptophan depletion was observed in DC samples, as compared to NC. The results suggested that DC challenged muscles to struggle against oxidative reactions, consuming endogenous antioxidant defenses and causing protein and lipid oxidation which in turn affect the quality and safety of chicken meat. These results emphasize the role of PM oxidative stress on chicken quality and safety. Antioxidant strategies like fast cooling may be combined with others (dietary antioxidants) to preserve chicken quality against oxidative stress.
KeywordsM. peroneus longus Antioxidant enzymes Protein oxidation Carcass cooling Lipid oxidation Chicken quality
Funding was provided by Secretaría de Estado de Investigación, Desarrollo e Innovación (Grant No. AGL2017-84586-R).
- Aebi H (1974) Catalase. In: Methods of enzymatic analysis, pp 673–684. https://doi.org/10.1016/B978-0-12-091302-2.50032-3
- Carvalho RH, Soares AL, Honorato DCB, Guarnieri PD, Pedrão MR, Paião FG, Oba A, Ida EI, Shimokomaki M (2014) The incidence of pale, soft, and exudative (PSE) turkey meat at a Brazilian commercial plant and the functional properties in its meat product. LWT Food Sci Technol 59(2):883–888. https://doi.org/10.1016/j.lwt.2014.07.019 CrossRefGoogle Scholar
- Carvalho RH, Ida EI, Madruga MS, Martínez SL, Shimokomaki M, Estévez M (2017) Underlying connections between the redox system imbalance, protein oxidation and impaired quality traits in pale, soft and exudative (PSE) poultry meat. Food Chem 215:129–137. https://doi.org/10.1016/j.foodchem.2016.07.182 CrossRefGoogle Scholar
- Honikel KO (1987) How to measure the water-holding capacity of meat? Recommendation of standardized methods. In: Tarrant PV, Eikelenboom G, Monin G (eds) Evaluation and control of meat quality in pigs. Current topics in veterinary medicine and animal science, vol 38. Springer, Dordrecht, pp 129–142. https://doi.org/10.1007/978-94-009-3301-9_11 Google Scholar
- Mahecha L, Nuernberg K, Nuernberg G, Martin J, Hubbermann EM, Knoeller S, Claeyse E, De Smet S, Dannenberger D (2011) Antioxidant enzyme activities and antioxidant capacity in longissimus muscle from bulls fed diets rich in polyunsaturated fatty acids. Food Chem 127(2):379–386. https://doi.org/10.1016/j.foodchem.2010.12.117 CrossRefGoogle Scholar
- Marklund S, Marklund G (1974) Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem FEBS 47(3):469–474. https://doi.org/10.1111/j.1432-1033.1974.tb03714.x CrossRefGoogle Scholar
- Rysman T, Utrera M, Morcuende D, Van Royen G, Van Weyenberg S, De Smet S, Estévez M (2016) Apple phenolics as inhibitors of the carbonylation pathway during in vitro metal-catalyzed oxidation of myofibrillar proteins. Food Chem 211:784–790. https://doi.org/10.1016/j.foodchem.2016.05.126 CrossRefGoogle Scholar