Scholarlink

<p>In this study, we systematically investigated the effects of β-conglycinin (7&#xa0;S) / lecithin molar ratios (ranging from 5:1 to 40:1) on the structural modification and immunoreactivity attenuation of 7&#xa0;S. Lecithin addition resulted in a dose-dependent increase in particle size and turbidity, indicating structural rearrangements of 7&#xa0;S. Multispectroscopic and molecular docking techniques confirmed that lecithin molecules were primarily interacted with hydrophobic domains of 7&#xa0;S. This molecular insertion triggered significant structural changes, characterized by the exposure of buried hydrophobic domains, as evidenced by the enhancement in ANS fluorescence intensity. When the ratio of 7&#xa0;S to lecithin was 30:1, the obtained complexes exhibited the highest fluorescence intensity (240.8 a.u.) and the lowest free sulfhydryl content (4.93 µmol/g). Furthermore, microstructural analysis revealed that lecithin-modified 7&#xa0;S displayed a more disordered and less compact surface structure. Importantly, these structural alterations not only decreased the IgG and IgE binding ability of 7&#xa0;S (assessed by ELISA), but also reduced the hypersensitivity responses (the release of histamine) in RBL-2H3 cells. These findings provide critical insights into the molecular mechanisms underlying lecithin’s immunomodulatory effects within allergenic food matrices.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Soy lecithin-mediated structural modulation of β-conglycinin and its implications for allergenicity in soy-based matrices

  • 期刊论文

  • 发表日期：

    2026年3月2日

查看全文
  • Hui Yang,
  • Yinuo Xiao,
  • Endian Guo,
  • Chenxi Fan,
  • Xuan Shang

摘要

In this study, we systematically investigated the effects of β-conglycinin (7 S) / lecithin molar ratios (ranging from 5:1 to 40:1) on the structural modification and immunoreactivity attenuation of 7 S. Lecithin addition resulted in a dose-dependent increase in particle size and turbidity, indicating structural rearrangements of 7 S. Multispectroscopic and molecular docking techniques confirmed that lecithin molecules were primarily interacted with hydrophobic domains of 7 S. This molecular insertion triggered significant structural changes, characterized by the exposure of buried hydrophobic domains, as evidenced by the enhancement in ANS fluorescence intensity. When the ratio of 7 S to lecithin was 30:1, the obtained complexes exhibited the highest fluorescence intensity (240.8 a.u.) and the lowest free sulfhydryl content (4.93 µmol/g). Furthermore, microstructural analysis revealed that lecithin-modified 7 S displayed a more disordered and less compact surface structure. Importantly, these structural alterations not only decreased the IgG and IgE binding ability of 7 S (assessed by ELISA), but also reduced the hypersensitivity responses (the release of histamine) in RBL-2H3 cells. These findings provide critical insights into the molecular mechanisms underlying lecithin’s immunomodulatory effects within allergenic food matrices.