Abstract：
(-)-Epigallocatechin-3-gallate (EGCG) is remarkably efficacious in inhibiting the browning of red meat. We therefore propose a hypothesis that EGCG forms complexes with myoglobin, thereby stabilizing its structure and thus preventing browning. This study investigated the interaction mechanism between EGCG and myoglobin. EGCG induced static quenching of myoglobin. Noncovalent forces, including hydrogen bonds and van der Waals, primarily governing the interactions between myoglobin and EGCG. The interactions primarily disrupted myoglobin\'s secondary structure, thus significantly reducing surface hydrophobicity by 53% (P < 0.05). The modification augmented the solubility and thermal stability of myoglobin. The radius of gyration (Rg) value fluctuated between 1.47 and 1.54 nm, and the hydroxyl groups in EGCG formed an average of 2.93 hydrogen bonds with myoglobin. Our findings elucidated the formation of stable myoglobin-EGCG complexes and the myoglobin-EGCG interaction, thus confirming our initial hypothesis.
摘要：
（-）-表没食子儿茶素-3-没食子酸酯（EGCG）在抑制红肉褐变方面非常有效。因此，我们提出了一个假设，即EGCG与肌红蛋白形成复合物，从而稳定其结构，从而防止褐变。本研究探讨了EGCG与肌红蛋白之间的相互作用机制。EGCG诱导肌红蛋白的静态猝灭。非共价力，包括氢键和范德华,主要控制肌红蛋白和EGCG之间的相互作用。这些相互作用主要破坏了肌红蛋白的二级结构，从而使表面疏水性显著降低53%(P<0.05)。该修饰增强了肌红蛋白的溶解度和热稳定性。回转半径（Rg）值在1.47和1.54nm之间波动，EGCG中的羟基与肌红蛋白平均形成2.93个氢键。我们的发现阐明了稳定的肌红蛋白-EGCG复合物的形成和肌红蛋白-EGCG相互作用，从而证实了我们最初的假设。
