Abstract：
In this study, the interaction mechanism between theaflavin and myosin was explored to confirm the potential application of theaflavin in the meat protein system. A series of theaflavin and myosin solutions were prepared for spectroscopic studies. Spectroscopy results showed that theaflavins formed complexes with myosin and affected the microenvironment of myosin. And that addition of theaflavin cause static quenching of the myosin solution. Theaflavin and bovine myosin combined through hydrophobic interaction to form a complex, and gradually increasing the temperature was conducive to the binding of theaflavin and bovine myosin. This interaction results in a decrease in the α -helix content of myosin. Molecular dynamics simulation results confirmed that hydrophobic interactions and hydrogen bonds made the protein structure more compact and stable. And the in vitro digestion process was simulated. The results showed that the addition of theaflavin could significantly reduce the digestibility of myosin.
摘要：
在这项研究中,探讨了茶黄素与肌球蛋白的相互作用机制，以证实茶黄素在肉类蛋白质系统中的潜在应用。制备了一系列茶黄素和肌球蛋白溶液用于光谱研究。光谱学结果表明，茶黄素与肌球蛋白形成复合物，并影响肌球蛋白的微环境。添加茶黄素会导致肌球蛋白溶液的静态猝灭。茶黄素和牛肌球蛋白通过疏水相互作用结合形成复合物,逐渐升高温度有利于茶黄素与牛肌球蛋白的结合。这种相互作用导致肌球蛋白的α-螺旋含量降低。分子动力学模拟结果证实，疏水相互作用和氢键使蛋白质结构更加紧凑和稳定。并对体外消化过程进行了模拟。结果表明,添加茶黄素能显著降低肌球蛋白的消化率。
