Understanding protein-lipid interactions in pyrazine binding under heat treatment: A case study of collagen and triglycerides

文献类型： 外文期刊

第一作者： Nie, Ruotong

作者： Nie, Ruotong;Wang, Zhenyu;Wei, Xiangru;Zhang, Dequan;Liu, Huan;Zhang, Chunjiang;Nie, Ruotong;Wang, Zhenyu;Wei, Xiangru;Zhang, Dequan;Liu, Huan;Zhang, Chunjiang;Zhang, Dequan;Zhang, Chunjiang

作者机构：

关键词： Collagen; Triglycerides; Pyrazine; Heat treatment; Molecular docking

期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）

ISSN： 0308-8146

年卷期： 2025 年 482 卷

页码：

收录情况： SCI

摘要： Background: Collagen-triglyceride complexes in animal skin govern flavor retention during thermal processing, yet their molecular interactions with pyrazines remain unresolved. Objectives: This study aims to elucidate heat-induced collagen-triglyceride complex formation (25 degrees C, 47 degrees C, 64 degrees C, 75 degrees C, and 79 degrees C), identify pyrazine-binding residues, and assess implications for flavor retention strategies. Methods: An in vitro collagen-triglyceride-pyrazine model was developed. Complex formation was validated via confocal laser scanning microscopy (CLSM), while heating-induced structural changes were analyzed through rheology, fluorescence spectroscopy, and XRD. Molecular docking quantified binding energies and dynamics. Results: Heating stabilized the collagen-triglyceride complexes via hydrogen bonds, van der Waals forces, and covalent bonds (zeta potential:-12.75 to-5.53 mV), showing high affinity for 2-ethyl-5-methyl and 3-ethyl-2,5dimethyl pyrazines. Molecular docking revealed GLU-A-12, HYP-B-7, and PHE-C-9 as key residues, destabilizing hydrogen networks but enhancing thermal stability. Conclusion: The integration of multi-scale analyses clarifies collagen-lipid-flavor interactions in flavor retention, providing valuable theoretical support for optimizing roasting technologies.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序