School of Food Engineering, Yantai Key Laboratory of Nanoscience and Technology for Prepared Food, Yantai Engineering Research Center of Green Food Processing and Quality Control, Bionanotechnology Institute, Ludong University, Yantai 264025, China.
School of Food Engineering, Yantai Key Laboratory of Nanoscience and Technology for Prepared Food, Yantai Engineering Research Center of Green Food Processing and Quality Control, Bionanotechnology Institute, Ludong University, Yantai 264025, China.
Food Res Int. 2023 Nov;173(Pt 1):113275. doi: 10.1016/j.foodres.2023.113275. Epub 2023 Jul 13.
Myosin is an ideal binding receptor for aroma compounds and its functional properties are easily affected by glucose. The study comprehensively clarified the effects of glucose glycation-induced structural modifications of myosin on its binding ability with furan derivatives, including 2-methylfuran, 2-furfural, and 2-furfurylthiol. The results demonstrated that the binding levels of furan derivatives were obviously affected by the glycation levels of myosin due to the changes of myosin structure and surface. The increased glycation levels caused the unfolding of myosin structure and accelerated the aggregation, as were exhibited by the data of zeta potential, particle size, microstructure, and secondary structure. The glycated myosin with wrinkled surfaces favored the significant increase of hydrophobic interactions (31.59-69.50 μg), the more exposure of amino acid residues (3459-6048), the formation of free sulfhydryl groups (16.37-20.58 mmol/10g) and hydrogen bonds. These key (non)covalent linkages accounted for the generation of glycated myosin-odorants complex, including 2-furfurylthiol (29.17-47.87 %), thus enhancing the resultant binding ability as evidenced by the free furan derivatives concentrations, fluorescence quenching and molecular docking simulation analysis. The glycated myosin for 8 h bound highest concentrations of furan derivatives. The results will provide comprehensive data on the retention of aroma compounds in meat products.
肌球蛋白是一种理想的芳香化合物结合受体，其功能特性很容易受到葡萄糖的影响。本研究全面阐明了葡萄糖糖基化诱导的肌球蛋白结构修饰对其与呋喃衍生物（包括 2-甲基呋喃、2-糠醛和 2-糠硫醇）结合能力的影响。结果表明，由于肌球蛋白结构和表面的变化，呋喃衍生物的结合水平明显受到肌球蛋白糖基化水平的影响。糖基化程度的增加导致肌球蛋白结构展开并加速聚集，这一点可以从zeta 电位、粒径、微观结构和二级结构的数据中得到证实。表面起皱的糖化肌球蛋白有利于疏水性相互作用（31.59-69.50μg）的显著增加、更多的氨基酸残基暴露（3459-6048）、游离巯基基团的形成（16.37-20.58mmol/10g）和氢键的形成。这些关键的（非）共价键合解释了糖化肌球蛋白-气味剂复合物的形成，包括 2-糠硫醇（29.17-47.87%），从而增强了结合能力，这可以从游离呋喃衍生物浓度、荧光猝灭和分子对接模拟分析得到证明。糖化肌球蛋白在 8 小时内结合了最高浓度的呋喃衍生物。研究结果将为肉类产品中香气化合物的保留提供全面的数据。
