Zhu Hongxing, Zhang Muhan, Wang Peng, Sun Chong, Xu Weimin, Ma Jingjing, Zhu Yongzhi, Wang Daoying
Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing Agricultural University, Nanjing 210095, China.
Food Chem. 2022 Jul 15;382:132354. doi: 10.1016/j.foodchem.2022.132354. Epub 2022 Feb 7.
The properties, structure and water holding capacity of myosin were analyzed after incubated with myoglobin (Mb) hemin prosthetic group. The results revealed moderate oxidation of hemin prosthetic group could improve the solubility of myosin. Besides, it could stretch the protein structure and cross-link the molecules to form the soluble polymer. Hence, moderate oxidation could improve the gel properties and the gel network structure. However, excessive oxidation would greatly reduce the physical and chemical properties of myosin, which was not conducive to the gel formation and would lead to a decrease in water retention. Moreover, fluorescence spectroscopy and cyclic voltammetry (CV) proved hemin prosthetic group had a high affinity for myosin. The interaction mechanism was further studied by molecular docking and molecular dynamics (MD) simulations. This study provides some fundamental prospects to be applied in the functional regulation of meat protein.
在与肌红蛋白（Mb）血红素辅基孵育后，对肌球蛋白的性质、结构和持水能力进行了分析。结果表明，血红素辅基的适度氧化可提高肌球蛋白的溶解度。此外，它可以伸展蛋白质结构并使分子交联形成可溶性聚合物。因此，适度氧化可以改善凝胶特性和凝胶网络结构。然而，过度氧化会大大降低肌球蛋白的物理和化学性质，这不利于凝胶形成并会导致保水性下降。此外，荧光光谱和循环伏安法（CV）证明血红素辅基对肌球蛋白具有高亲和力。通过分子对接和分子动力学（MD）模拟进一步研究了相互作用机制。本研究为肉类蛋白质的功能调控应用提供了一些基础前景。
