Wang Haitang, Xia Xiufang, Yin Xiaoyu, Liu Haotian, Chen Qian, Kong Baohua
College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
Int J Biol Macromol. 2021 Dec 15;193(Pt A):672-680. doi: 10.1016/j.ijbiomac.2021.10.105. Epub 2021 Oct 25.
In this study, we investigated the interaction between myofibrillar proteins (MPs) and selected alcohols (1-pentanol, 1-hexanol, and 1-heptanol). Only 1-heptanol exhibited the binding ability to MPs, and the binding ability significantly increased with increasing protein concentration (p < 0.05). In addition, both static and dynamic quenching occurred during the interaction, with a red shift of the maximum absorption peak in the synchronous fluorescence spectra indicating a change in the microenvironment of the MPs. The results of circular dichroism measurements suggested that the interaction between MPs and 1-heptanol altered the secondary structure of the MPs. Furthermore, thermodynamic analysis showed that hydrogen bonding and van der Waals forces dominated the interaction between MPs and 1-heptanol, which was confirmed by the results of molecular docking/dynamics simulations. This study provides an in-depth understanding of the interaction between MPs and alcohols, which can help to improve the flavor control in meat.
在本研究中，我们研究了肌原纤维蛋白（MPs）与选定的醇类（1-戊醇、1-己醇和1-庚醇）之间的相互作用。只有1-庚醇表现出与MPs的结合能力，且结合能力随蛋白质浓度的增加而显著增强（p < 0.05）。此外，相互作用过程中发生了静态和动态猝灭，同步荧光光谱中最大吸收峰的红移表明MPs的微环境发生了变化。圆二色性测量结果表明，MPs与1-庚醇之间的相互作用改变了MPs的二级结构。此外，热力学分析表明，氢键和范德华力主导了MPs与1-庚醇之间的相互作用，分子对接/动力学模拟结果证实了这一点。本研究深入了解了MPs与醇类之间的相互作用，有助于改善肉类的风味控制。
