Excessive free radical grafting interferes with the macromolecular association and crystallization of brined porcine myofibrils during heat-set gelatinization

文献类型： 外文期刊

第一作者： Zhang, Min

作者： Zhang, Min;He, Lichao;Wang, Yanbo;Li, Chengliang;Jin, Guofeng;Zhang, Min;Zhang, Min;Li, Chengliang;Jin, Yongguo;Tang, Xiaoyan;Jin, Guofeng;Tang, Xiaoyan

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关键词： Myofibril; Salt diffusion; Free radical grafting; Heat-set gelatinization; Crystallization; Thermodynamics

期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：8.1； 五年影响因子：7.7 ）

ISSN： 0963-9969

年卷期： 2024 年 175 卷

页码：

收录情况： SCI

摘要： Free radical grafting and oxidative modification show superiority in myofibrillar protein (MP) aggregation patterns during salting process, but their consequent formation mechanisms of protein hydration network require further evaluation. Herein, we explored the effect of salt-curing (0, 1, 3 and 5 %) on MP protein polymer substrate, water-protein interaction, crystallization events and thermal stability under H2O2/ascorbate-based hydroxyl radical (center dot OH)-generating system (HRGS) (1, 10, 20 mM H2O2). Results showed that moderate salting (<= 3%) favored the water binding of MP gels during the oxidation course. Accordingly, the maximum thermal stability (Tm) of MP gels was obtained at 3 % salting could be greatly attributed to the protein chain solubilization and refolding process. However, 5 % salt synergized with center dot OH oxidation intensified diffraction peak 2 (the most striking diffraction feature). Microstructural analysis validated a maximum compactness of MP gel following brining with 5 % salt at potent oxidation strength (20 mM H2O2). This study maybe promises efficient strategy to the myogenetic fibril products and biomaterials.

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