化学
肌原纤维
丁香酚
氧化磷酸化
氧化应激
蛋白质聚集
化学工程
生物物理学
有机化学
生物化学
生物
工程类
作者
Deyin Pan,Jinming Ma,Jingjing Diao,Jiaqi Li,Hongsheng Chen
标识
DOI:10.1016/j.fochx.2023.100946
摘要
The effects of eugenol (EG; 0, 5, 20, and 50 mg/g protein) on the structure and gel properties of pork myofibrillar protein (MPs) under a hydroxyl radical-generating system were explored in this study. The results revealed that the addition of a high concentration of EG (50 mg/g protein) markedly reduced the carbonyl content and enhanced the fluorescence intensity, surface hydrophobicity, and protected the secondary structure of MPs, compared to oxidized MPs. In addition, the high concentration group noticeably increased the storage modulus (G'), gel strength, and water-holding capacity (WHC), and significantly hindered the oxidation-induced transformation of immobilized water of the MPs gel to free water and basically favored the formation of a finer and more homogeneous three-dimensional network structure, This work verified that the adding of EG could effectively improve the gel quality of oxidized MPs and more successfully delay oxidation-induced damage to muscle protein structure.
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