The aim of this study was to investigate the effects of oxidation on the structure of pork myofibrillar proteins (MPs) and the water retention mechanism of MPs gel. In a Fenton reaction system, protein oxidation increases (P < 0.05) with hydrogen peroxide (H2O2) concentration (0, 0.5, 1, 3, 5, 10, and 20 mmol/L). The Brunauer-Emmett-Teller surface area of the proteins gel gradually increased (P < 0.05) from 6.17 m2/g to 14.73 m2/g. Low field nuclear magnetic resonance results showed that immobilized water in the gel gradually decreased but free water content gradually increased (P < 0.05). Gel strength and water holding capacity (WHC) increased and then decreased. The results reveal that moderate oxidation contributes to the compact and uniform pore structure, higher WHC of proteins gel as well. However, excessive oxidation leads to increase pores and changes in water states of gel, leading to lower WHC.

中文翻译：

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体外氧化对猪肌肉肌原纤维蛋白凝胶保水机理的影响。

这项研究的目的是研究氧化对猪肉肌原纤维蛋白（MPs）的结构以及MPs凝胶的保水机理的影响。在Fenton反应系统中，蛋白质氧化随着过氧化氢（H2O2）浓度（0、0.5、1、3、5、10和20 mmol / L）的增加（P <0.05）。蛋白质凝胶的Brunauer-Emmett-Teller表面积从6.17 m2 / g逐渐增加（P <0.05）至14.73 m2 / g。低场核磁共振结果表明，凝胶中固定化的水逐渐减少，但游离水含量逐渐增加（P <0.05）。凝胶强度和持水量（WHC）先升高后降低。结果表明，适度的氧化有助于形成紧密而均匀的孔结构，蛋白质凝胶的WHC也较高。然而，