数字农科院2.0

Interactions between lycopene and myofibrillar proteins under different pH conditions: Implications for structural properties and in vitro digestibility

文献类型： 外文期刊

作者： Jia Huang;Min You;Yanyan Chen;Chunhui Zhang;Feng Huang

作者机构：

关键词： Digestibility;Lycopene;Molecular docking;Myofibrillar proteins;Peptidomics;Structure characteristics

期刊名称： Food Hydrocolloids

ISSN： 0268-005X

年卷期： 2026 年 175 卷

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

摘要： This study investigated the mechanism behind pH-dependent interactions between lycopene (LYC) and myofibrillar proteins (MPs) and their effects on protein structure, colloidal stability and digestibility. Results revealed that LYC binding is driven by hydrogen bonding and van der Waals forces at neutral pH, whereas hydrophobic interactions dominate under acidic/alkaline conditions. Structural analyses showed that LYC reduced α-helix/β-sheet content, increased random coil structures, and induced localized unfolding at the myosin head-tail junction, particularly at pH 7, without altering surface hydrophobicity or zeta potential. Crucially, LYC embedding favored colloidal stability while preventing excessive aggregation. Molecular dynamics simulations confirmed structural destabilization accompanied by compaction. Digestion studies demonstrated significantly enhanced hydrolysis and bioactive peptide release at pH 7 due to improved enzyme accessibility, while extreme pH values led to aggregation and reduced digestibility. These findings highlight LYC as a pH-sensitive structural modulator for MPs to optimize colloidal stability and digestibility, providing a framework for designing nutrient-dense meat products with tailored functionality.

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