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The mechanism of improved myosin gel properties by low dose rosmarinic acid addition during gel formation
Food Hydrocolloids ( IF 10.7 ) Pub Date : 2020-09-01 , DOI: 10.1016/j.foodhyd.2020.105869
Hongjie Dai , Xueke Chen , Lin Peng , Liang Ma , Yi Sun , Lin Li , Qiang Wang , Yuhao Zhang

Abstract In this study, the interaction mechanism between rosmarinic acid (RA) and myosin and its effect on gel formation during the heating process at different NaCl concentrations were investigated. The results showed that the RA addition improved the strength, water retention and elastic modulus of myosin gel. During the gel formation, the head aggregation of myosin was weakened due to the enhanced hydrophobic interaction and hydrogen bonds between RA and myosin. As temperature increased, the partially oxidized RA could form covalent crosslinking with the sulfhydryl groups of myosin. The interaction between RA and myosin promoted the unfolding of myosin structure, resulting in the reduction of the α-helix content and the exposure of hydrophobic groups of myosin, which accelerated the gel formation of myosin during the heating process. Moreover, the medium-high NaCl concentration facilitated these non-covalent and covalent interactions, thereby improving the gel properties of myosin.

中文翻译:

在凝胶形成过程中通过添加低剂量迷迭香酸改善肌球蛋白凝胶特性的机制

摘要 本研究研究了迷迭香酸(RA)与肌球蛋白的相互作用机制及其对不同NaCl浓度加热过程中凝胶形成的影响。结果表明,RA的加入提高了肌球蛋白凝胶的强度、保水性和弹性模量。在凝胶形成过程中,由于 RA 和肌球蛋白之间的疏水相互作用和氢键增强,肌球蛋白的头部聚集减弱。随着温度升高,部分氧化的 RA 可以与肌球蛋白的巯基形成共价交联。RA与肌球蛋白的相互作用促进了肌球蛋白结构的解折叠,导致α-螺旋含量降低,肌球蛋白疏水基团暴露,加速了肌球蛋白在加热过程中的凝胶形成。而且,
更新日期:2020-09-01
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