提高高蛋白饮料的热稳定性,通过热处理对乳清蛋白进行修改
1Midwest Dairy Foods Research Center, Department of Food Science and Nutrition, University of Minnesota, Saint Paul, MN 55108.
Journal of dairy science
|February 22, 2026
概括
通过热和剪切加工修改乳清蛋白可以提高高蛋白饮料的热稳定性. 这种方法产生了小小的乳清蛋白聚合物,在热处理和储存过程中增强了体稳定性.
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
- 体科学 体科学 体科学
背景情况:
- 高蛋白饮料的结合体稳定性至关重要,特别是在热处理过程中.
- 乳清蛋白在加热下变质和聚合,限制了它们在此类系统中的使用.
- 了解乳清蛋白和素的相互作用是改善饮料稳定性的关键.
研究的目的:
- 研究热修饰乳清蛋白对高蛋白饮料热稳定性的影响.
- 为了确定修改的乳清蛋白如何影响合体稳定性和热凝固时间.
- 探索乳清蛋白修饰,聚合物形成和饮料稳定性之间的关系.
主要方法:
- 通过在90°C和10,000rpm加热酸化乳清蛋白分离物 (AWPI) 来制备改性乳清蛋白.
- 特性包括表面电荷,粒子大小,疏水性和硫基.
- 修改的乳清蛋白被纳入高蛋白系统 (8-10%的蛋白质) 中,可变的素与乳清比率 (80:20至50:50).
- 测量包括粘度,颗粒大小和热凝固时间.
主要成果:
- 热修饰增加了乳清蛋白的疏水性和硫基,形成小聚合物 (~61 nm).
- 这些改良的乳清蛋白在高蛋白系统中增强了热稳定性,延长了凝固时间.
- 即使在10%的蛋白质和50:50的素与乳清比率下,修改的乳清蛋白质也提高了稳定性 (0.8分钟到2分钟).
结论:
- 在修改过程中形成的小乳清蛋白聚合物增强了高蛋白饮料的热稳定性.
- 低pH诱导的乳清蛋白聚合可以减少素-乳清蛋白相互作用.
- 这种方法提供了一种策略,以提高乳清蛋白在热加工,高蛋白食品系统中的应用性.
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