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Understanding protein-lipid interactions in pyrazine binding under heat treatment: A case study of collagen and
Ruotong Nie1, Zhenyu Wang1, Xiangru Wei1
1Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs; Laboratory of Processing Technology Integration for Chinese-style Meat and Vegetable Dishes, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
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 °C, 47 °C, 64 °C, 75 °C, and 79 °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-2,5-dimethyl 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.
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