Abstract

The excessive release of calcium from the sarcoplasmic reticulum during the installation of PSE (Pale, Soft, Exudative) meat, leads to increase of phospholipase A2 (PLA2) activity and consequently causes a higher lipid oxidation. In contrast, glutathione peroxidase (GSH-Px) is a selenium-dependent antioxidant enzyme that prevents the oxidative damage. The aim of this work was to investigate the secreted PLA2 (sPLA2) and GSH-PX activities in PSE poultry meat. Breast meat samples (Pectoralis major m.) (n=24) were obtained from commercial slaughterhouse. Samples were classified as PSE and Control Meat based on pH and L* values, fillets with pH1h30? 6.0 and L24h* ?53.0 as PSE and fillets with pH1h30> 6.0 and L24h*<53.0 with Control. sPLA2 was analyzed using enzymatic assay kit and GSH-Px was measured a coupled assay procedure recording the NADPH (nicotinamide adenine dinucleotide phosphate reduced) oxidation. The sPLA2 average was 0.295 Umg-1 of protein for PSE meat and 0.380 Umg-1 of protein for Control meat, did not differ significantly (p >0,05). The GSH-Px activity was approximately 24,4% higher (p?0,05) for Control meat when compared to PSE meat. The sPLA2 activity of PSE fillets did not changed, however PSE fillets present the enzymatic system of antioxidant defense compromised with lower GSH-PX activity.

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