The objective of this study was to evaluate the association between oxidative damage to proteins (represented by protein carbonylation) and beef tenderness. Three experimental groups were selected by shear force (SF): tender (38.2 ± 2.9 N), intermediate (51.9 ± 6.8 N), and tough meat (74.5 ± 7.8 N). Two-dimensional electrophoresis with hydrazide fluorophore derivatization was used. The structural proteins actin (ACTA1), myosin (MYL1 and MYL3), desmin (DES) and troponin T (TNNT1 and TNNT3), antioxidant proteins (PRDX1, PRDX2 and PARK7) and heat shock proteins (HSPB1, CRYAB and HSPB6) showed an increase in the oxidative damage in tender meat when compared to the intermediate and tough meat (P < .05). Decrease in oxidative damage of the metabolic enzymes (TPI1, GAPDH and ENO3) were observed in tender meat group (P < .05). The present results suggest that oxidation act on the proteins of different metabolic pathways and consequently affect meat tenderness in Angus crossbred cattle.

这项研究的目的是评估蛋白质的氧化损伤（以蛋白质羰基化表示）与牛肉嫩度之间的关系。通过剪切力（SF）选择了三个实验组：嫩肉（38.2±2.9 N），中间肉（51.9±6.8 N）和硬肉（74.5±7.8 N）。使用具有酰肼荧光团衍生作用的二维电泳。结构蛋白肌动蛋白（ACTA1），肌球蛋白（MYL1和MYL3），结蛋白（DES）和肌钙蛋白T（TNNT1和TNNT3），抗氧化剂蛋白（PRDX1，PRDX2和PARK7）和热激蛋白（HSPB1，CRYAB和HSPB6）显示出与中间肉和强韧肉相比，嫩肉的氧化损伤增加（P  < .05）。嫩肉组中代谢酶（TPI1，GAPDH和ENO3）的氧化损伤减少（P  <  .05）。目前的结果表明，氧化作用于不同代谢途径的蛋白质，从而影响安格斯杂交牛的肉嫩度。