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. 2019 Mar;56(3):1371-1379.
doi: 10.1007/s13197-019-03611-1. Epub 2019 Feb 13.

Collapse of the endogenous antioxidant enzymes in post- mortem broiler thigh muscles triggers oxidative stress and impairs water-holding capacity

Rafael H Carvalho  1   2 , Elza I Ida  2 , Marta S Madruga  3 , Massami Shimokomaki #  1 , Mario Estévez #  4
Affiliations

Collapse of the endogenous antioxidant enzymes in post- mortem broiler thigh muscles triggers oxidative stress and impairs water-holding capacity

Rafael H Carvalho et al. J Food Sci Technol. 2019 Mar.

Abstract

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.

Keywords: Antioxidant enzymes; Carcass cooling; Chicken quality; Lipid oxidation; M. peroneus longus; Protein oxidation.

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Figures

Fig. 1
Fig. 1
Formation of oxidation products under normal cooling (NC) and delayed cooling (DC) in chicken thigh meat. a TBA-RS (mg MDA/kg muscle) and b protein carbonyls (nmol carbonyls/mg protein). Significant differences between means in Student’s T test are denoted on top of bars
Fig. 2
Fig. 2
Measurements of tryptophan (a) and Schiff bases (b) under normal cooling (NC) and delayed cooling (DC) chicken thigh meat. a tryptophan in mg NATA/g protein and b Schiff bases in fluorescence intensity. Significant differences between means in Student’s T test are denoted on top of bars
Fig. 3
Fig. 3
Overlay of similarity map of thigh meat samples and computed variables in principal component analysis (PCA). DC = delay cooling, NC = normal cooling, WHC_p = press method. WHC_c = centrifugation method. WHC_s = centrifugation method with salt addition, CAT = catalase (CAT), GSH-Px = glutathione peroxidase SOD = superoxide dismutase activity, DNPH = protein carbonyls TBA-RS = thiobarbituric acid-reactive substances, SB = Schiff base and Tryp = tryptophan
Fig. 4
Fig. 4
Proposed mechanisms for the observed effects of cooling on the meat quality and oxidative systems in chicken thigh meat. WHC = water holding capacity, CAT = catalase, GSH-Px = glutathione peroxidase SOD = superoxide dismutase activity, TBA-RS = thiobarbituric acid-reactive substances, SB = Schiff base and tryp = tryptophan
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