Scholarlink

<p>This study investigates the impact of sorbitol and Mg<sup>2</sup>⁺ on the conformation and aggregation of myofibrillar proteins after thawing under low temperature and high humidity conditions. The mechanisms are explored by analyzing the microstructure, gel properties, and conformational changes of proteins. The results show that the synergistic effect of sorbitol and Mg<sup>2</sup>⁺ results in a smoother and denser microstructure in myofibrillar protein gels, significantly improving water-holding capacity (WHC) and gel strength. Under heat-induced conditions, a stronger protein network is formed, thereby increasing in both <i>G</i>′ and <i>G</i>″. Secondary structure analysis reveals that the addition of salt ions increases the proportion of β-sheets, promoting tighter protein aggregation. Sorbitol stabilizes the proportion of α-helices by forming hydrogen bonds with proteins and water molecules, allowing the protein to remain moderately unfolded and promoting a more stable protein structure. Fluorescence intensity results show that the addition of sorbitol effectively mitigates the aggregation effect induced by high salt concentrations, allowing the proteins to maintain moderate unfolding. Moreover, ionic bonds dominate in the protein suspension, while sorbitol also increases the content of hydrogen bonds and disulfide bonds. This indicates a synergistic effect between sorbitol and Mg<sup>2</sup>⁺ to alleviate the negative impact of freezing–thawing on protein conformation.</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

Improvement of Myofibrillar Protein Gel Properties After Freezing–Thawing by Magnesium Ions and Sorbitol: Synergistic Effects of Ionic Bridges and Hydrogen Bonds

  • 期刊论文

  • 发表日期：

    2025年4月23日

查看全文
  • Jun Xiang,
  • Na Luo,
  • Chaofan Guo,
  • Yuxiang Zhang,
  • Xin Chen,
  • Xingwei Wang,
  • Xiaoyu Yin,
  • Xuejiao Wang,
  • Jianxin Cao

摘要

This study investigates the impact of sorbitol and Mg2⁺ on the conformation and aggregation of myofibrillar proteins after thawing under low temperature and high humidity conditions. The mechanisms are explored by analyzing the microstructure, gel properties, and conformational changes of proteins. The results show that the synergistic effect of sorbitol and Mg2⁺ results in a smoother and denser microstructure in myofibrillar protein gels, significantly improving water-holding capacity (WHC) and gel strength. Under heat-induced conditions, a stronger protein network is formed, thereby increasing in both G′ and G″. Secondary structure analysis reveals that the addition of salt ions increases the proportion of β-sheets, promoting tighter protein aggregation. Sorbitol stabilizes the proportion of α-helices by forming hydrogen bonds with proteins and water molecules, allowing the protein to remain moderately unfolded and promoting a more stable protein structure. Fluorescence intensity results show that the addition of sorbitol effectively mitigates the aggregation effect induced by high salt concentrations, allowing the proteins to maintain moderate unfolding. Moreover, ionic bonds dominate in the protein suspension, while sorbitol also increases the content of hydrogen bonds and disulfide bonds. This indicates a synergistic effect between sorbitol and Mg2⁺ to alleviate the negative impact of freezing–thawing on protein conformation.