Scholarlink

<p>The low water solubility and stability of hesperidin (HP) as a bioactive substance greatly limit its application. In this paper, the anti-solvent precipitation and pH-shifting methods were used to prepare soybean isolate protein (SPI) and HP complexes. The complex prepared by the pH-shifting method (PSPI-HP) showed a higher loading efficiency of HP than the complex obtained by the anti-solvent precipitation method (ASPI-HP) (90.88 ± 1.27% versus 71.22 ± 0.68%). The stability of PSPI-HP was better than that in ASPI-HP when exposed to environmental factors. Multi-spectral evaluations and molecular docking results indicated that HP formed stable complexes with SPI through hydrogen bonding and hydrophobic interactions. Circular dichroism results demonstrated a decrease in α-helix and an increase in β- sheet and β-turn content upon SPI binding to HP. Compared with SPI and ASPI-HP, PSPI-HP exhibited better antioxidant activity and emulsifying activity. The results offer novel perspectives on the interaction between SPI and HP and broaden the potential applications of HP in the food and pharmaceutical industries.</p> Graphical abstract <p></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

Fabrication and characterization of hesperidin and soybean protein isolate complexes with enhancing solubility and functional properties

  • 期刊论文

  • 发表日期：

    2025年3月25日

查看全文
  • Weiben Ge,
  • Jinghui Chen,
  • Yiheng Li,
  • Hongxin Wang

摘要

The low water solubility and stability of hesperidin (HP) as a bioactive substance greatly limit its application. In this paper, the anti-solvent precipitation and pH-shifting methods were used to prepare soybean isolate protein (SPI) and HP complexes. The complex prepared by the pH-shifting method (PSPI-HP) showed a higher loading efficiency of HP than the complex obtained by the anti-solvent precipitation method (ASPI-HP) (90.88 ± 1.27% versus 71.22 ± 0.68%). The stability of PSPI-HP was better than that in ASPI-HP when exposed to environmental factors. Multi-spectral evaluations and molecular docking results indicated that HP formed stable complexes with SPI through hydrogen bonding and hydrophobic interactions. Circular dichroism results demonstrated a decrease in α-helix and an increase in β- sheet and β-turn content upon SPI binding to HP. Compared with SPI and ASPI-HP, PSPI-HP exhibited better antioxidant activity and emulsifying activity. The results offer novel perspectives on the interaction between SPI and HP and broaden the potential applications of HP in the food and pharmaceutical industries.

Graphical abstract