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选择性酶化水解对大豆蛋白分离物的结构性质和凝性质的影响
Zhijun Fan1,2, Yue San1, Saike Tang1
1College of Food Science, Northeast Agricultural University, Harbin 150030, China.
Foods (Basel, Switzerland)
|November 27, 2025
概括
豆蛋白分离物 (SPI) 的酶性修改,使用帕帕因改善了凝质地和稳定性,比性蛋白酶更好. 用Papain处理的SPI凝表现出增强的水能力和优越的结构和质性质.
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:
- 大豆蛋白分离物 (SPI) 凝通常具有不良的稳定性和质地.
- 酶性水解可以改善蛋白质功能和凝性质.
研究的目的:
- 使用性蛋白酶和帕帕因修改SPI.
- 评估酶化水解对SPI结构和凝质量的影响.
主要方法:
- 分析水解度 (DH),粒子大小和蛋白质纯度.
- 检查了二次结构变化 (FT-IR),纹理,水容量 (WHC),质和微观结构.
- 使用SDS-PAGE来评估蛋白质水解.
主要成果:
- 与性蛋白酶相比,帕帕因水解产生了较大的分子量.
- 酶修饰增加了α螺旋和β片的含量.
- 用帕帕因修饰的SPI凝显示出优异的WHC,纹理,质 (G') 和微观结构.
结论:
- 帕帕因在增强SPI凝特性方面比性蛋白酶更有效.
- 酶修饰为改善食品应用中的SPI功能提供了一个可行的策略.
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