结构依赖的多的交互调节:在芬顿氧化过程中增强肌纤维素-大豆蛋白质复合物的凝和氧化稳定性
Zhifeng Tan1, Xiaoqing Yang1, Yidan Wang1
1SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.
Food chemistry
|December 24, 2025
概括
像taxifolin和EGCG这样的多醇有效地抑制了食品系统中的蛋白质氧化. 它们稳定蛋白质结构,改善凝性质和颜色,提供对食品保存机制的见解.
科学领域:
- 食品科学 食品科学 食品科学
- 蛋白质化学 蛋白质化学
- 生物化学 生化学
背景情况:
- 蛋白质氧化是食品系统的一个主要问题,影响质量和营养价值.
- 多因其抗氧化特性而闻名,但它们在蛋白质系统中的特定作用需要进一步阐明.
研究的目的:
- 在调节氧化肌纤维蛋白 (MP) 和大豆蛋白分离物 (SPI) 复合系统中研究酸 (GA),塔克西福林 (TF) 和表甲基酸 (EGCG) 的结构功能关系.
- 了解蛋白质氧化受多介导抑制的分子机制及其对凝性质的影响.
主要方法:
- MP和SPI复合系统的芬顿氧化.
- 分析蛋白质构造变化和氧化标志物 (例如碳基含量).
- 对凝性质的评估 (例如,纹理,颜色稳定性).
- 分子动力学模拟以阐明相互作用机制.
主要成果:
- TF和EGCG在抑制蛋白质氧化方面比GA更有效,降低碳酸含量分别为3.4倍和3.0倍.
- 聚醇诱导蛋白质构造变化和增强凝特性,包括颜色稳定性,特别是通过TF.
- 分子动力学表明,TF通过非共价相互作用形成稳定的界面桥梁,稳定MP-SPI复合体.
结论:
- 聚,特别是TF和EGCG,在抑制蛋白质氧化和改善基于蛋白质的食品系统的功能性质方面发挥着至关重要的作用.
- TF独特的二黄结构有助于其在保持凝颜色稳定性方面的卓越有效性.
- 这项研究强调了多在竞争性结合和界面桥接中的双重作用,提供了对它们对氧化驱动蛋白质聚合的保护作用的分子理解.
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