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豆蛋白分离物-酸双网乳液凝:形成机制和改善冷融化稳定性
Shijiao Wang1, Zenan Wu1, Lingyue Jia1
1College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
International journal of biological macromolecules
|June 24, 2024
概括
将酸添加到大豆蛋白分离乳液凝中,可以在冷解过程中提高其稳定性. 这创造了一个双重的网络结构,增强了水的保留和防止聚合,使冷食品应用受益.
科学领域:
- 食品科学与技术 食品科学与技术
- 生物材料科学 生物材料科学
- 蛋白质化学 蛋白质化学
背景情况:
- 豆蛋白分离物 (SPI) 是一种常见的食品成分,但基于SPI的乳液凝缺乏冷解稳定性,导致聚合和脱油.
- 提高SPI乳液凝的稳定性对于其在冷食品中的应用至关重要.
研究的目的:
- 调查大豆蛋白分离物-藻酸盐 (SPI-SA) 双网络结构对乳液凝冷稳定性的影响.
- 阐明酸增强SPI乳液凝稳定性的机制.
主要方法:
- 使用SPI和藻酸盐 (SA) 用热处理和离子交联制备了乳液凝.
- 包括富里埃变换红外光谱和低场核磁共振在内的技术被用来分析结构和特性.
主要成果:
- 酸与SPI形成了多样化的网络结构,受相分离和Ca2+交联的影响,形成稳定的SPI-SA复合体.
- 在FTIR分析中,SPI-SA复合体因特征性峰值消失而得到证实.
- 低场核磁共振显示,SA限制了水的迁移,增加了结合的水和改善了保持水的能力.
结论:
- SPI-SA双网络结构显著提高了乳液凝的冷解稳定性.
- 酸的加入改善了水的保留,并防止了SPI乳液凝中的聚合.
- 这项研究为在冷食品中使用SPI提供了科学依据.
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