Unraveling the covalent binding mechanisms of aroma compounds with porcine proteins: A mass spectrometry, proteomics, and conformational analysis approach

文献类型： 外文期刊

第一作者： Wang, Tianze

作者： Wang, Tianze;Yang, Ping;Wang, Jingfan;Huang, Feng;Han, Dong;Zhang, Chunhui

作者机构：

关键词： Covalent interaction; Aroma compounds; Porcine proteins; Mass spectrometry; Proteomics

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 493 卷

页码：

收录情况： SCI

摘要： This work investigated the covalent interaction mechanisms between eight aroma compounds from heatprocessed pork and porcine proteins. The effects of aroma compounds on protein conformation and covalent reactive groups were evaluated before and after heating, demonstrating that covalent binding potential for hexanal, (E)-2-octenal (OCT), (E,E)-2,4-decadienal (DEC), dimethyl trisulfide (DMTS), and 2-methyl-3-furanthiol (MFT). Covalent binding of OCT, DEC, DMTS, and MFT, along with hydrophobic interactions of OCT and DEC, disrupted protein secondary structure and inhibited peptide chain cross-linking, with heating enhancing interactions. Mass spectrometry identified covalent adducts between two protein peptides and aroma compounds, showing adduct formation rates by analyzing adduct concentration changes: DEC > OCT for amino groups and DMTS > DEC > OCT > MFT for sulfhydryl groups. Proteomics identified specific sites and types of modifications induced by aroma compounds. These findings provide a theoretical basis for controlling flavor loss in meat products due to covalent interaction.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序