College of Food Science, Southwest University, Chongqing 400715, China.
College of Food Science, Southwest University, Chongqing 400715, China; Chongqing Engineering Research Center of Regional Food, Chongqing 400715, China.
Food Chem. 2020 Jun 15;315:126226. doi: 10.1016/j.foodchem.2020.126226. Epub 2020 Jan 19.
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 (HO) 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 m/g to 14.73 m/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.
本研究旨在探讨氧化对猪肉肌原纤维蛋白（MPs）结构和 MPs 凝胶保水机制的影响。在芬顿反应体系中，随着过氧化氢（HO）浓度（0、0.5、1、3、5、10 和 20mmol/L）的增加，蛋白质氧化程度增加（P<0.05）。蛋白质凝胶的 Brunauer-Emmett-Teller 表面积逐渐从 6.17m/g 增加到 14.73m/g（P<0.05）。低场核磁共振结果表明，凝胶中固定水逐渐减少，而自由水含量逐渐增加（P<0.05）。凝胶强度和持水能力（WHC）先增加后降低。结果表明，适度氧化有助于形成更紧密、均匀的孔结构和更高的 MPs 凝胶 WHC。然而，过度氧化会导致孔增加和凝胶水状态的变化，从而降低 WHC。
