Key Laboratory of Agro-Products Processing, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Ministry of Agriculture and Rural Affairs, Beijing 100193, China; Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, China.
Department of Food Science and Technology, Faculty of Agriculture, Assiut University, Assiut 71526, Egypt.
Int J Biol Macromol. 2023 Dec 31;253(Pt 2):126844. doi: 10.1016/j.ijbiomac.2023.126844. Epub 2023 Sep 11.
Flavor is one of the most important factors that affect consumers' preference for processed meat products. This study aimed to investigate effects of heating on interaction between myofibrillar proteins (MPs) and pyrazine compounds and understand the underlying mechanisms. A combination of multispectral, molecular docking, and molecular dynamics technologies was used to achieve study's aim. Results demonstrated that MPs underwent structural reconstruction and expansion during heating, which significantly altered surface hydrophobicity and SH content. MPs' zeta potential reduced from -7.29 to -10.47 when a short heating time. Additionally, a positive correlation was found between β-sheet content and ability of MPs to adsorb pyrazine compounds. Molecular docking analysis revealed 13 binding sites for pyrazines and MPs. Furthermore, amino acid residues and pyrazine compounds were found to interact by four different forms of forces, primarily van der Waals forces, carbon‑hydrogen bonds, alkyl groups, and π-alkyl groups. Obtained results demonstrated that adequate or optimized heat treatment could expose more binding sites, hence enhancing the binding of MPs to pyrazine compounds. This study may be used to better understand how structural changes in MPs during processing affect MPs' capacity to bind flavor substances, which can help improve flavor of processed meats to encourage their consumption.
风味是影响消费者对加工肉类产品偏好的最重要因素之一。本研究旨在探讨加热对肌原纤维蛋白（MPs）与吡嗪类化合物相互作用的影响，并了解其潜在机制。本研究采用多光谱、分子对接和分子动力学技术相结合的方法来实现研究目的。结果表明，MPs 在加热过程中发生了结构重构和膨胀，这显著改变了表面疏水性和 SH 含量。当加热时间较短时，MPs 的 ζ 电位从-7.29 降低到-10.47。此外，β-折叠含量与 MPs 吸附吡嗪类化合物的能力之间存在正相关关系。分子对接分析显示，吡嗪和 MPs 有 13 个结合位点。此外，发现氨基酸残基和吡嗪类化合物通过四种不同形式的力相互作用，主要是范德华力、碳氢键、烷基和π-烷基。研究结果表明，适当或优化的热处理可以暴露出更多的结合位点，从而增强 MPs 与吡嗪类化合物的结合。本研究可以帮助更好地理解加工过程中 MPs 结构变化如何影响 MPs 结合风味物质的能力，从而有助于改善加工肉类的风味，鼓励其消费。
