洞察乳清蛋白分离物和半氨酸之间的联合挤出机制
Sinan Mu1, Heyang Xu1, Liying Han2
1Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, PR China.
Journal of agricultural and food chemistry
|October 17, 2024
概括
乳清蛋白分离物 (WPI) 与氨酸 (Cys) 联合挤出显示出增加的二硫化物交叉链接,特别是在α-乳蛋白位点. 这增强了蛋白质聚合和保持水分的能力,创造了一个新的食品成分.
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 生物化学
背景情况:
- 乳清蛋白分离物 (WPI) 是一种有价值的食品成分.
- 了解蛋白质交叉链接对于开发新的食品功能至关重要.
- 氨酸 (Cys) 可以促进蛋白质中二硫化键的形成.
研究的目的:
- 为了研究与不同度的Cys.共挤出WPI的二硫化物交叉链接点.
- 分析WPI在低温共挤出过程中的结构变化和水分布.
- 为了阐明WPI-Cys交叉链接的分子机制.
主要方法:
- 液体染色学电喷离离子双重质谱学 (LC/MS/MS) 使用pLink软件进行二硫化物位点分析.
- 二甲基硫酸盐-聚烯胺凝电泳 (SDS-PAGE) 和大小排除色谱用于蛋白质聚合.
- 对WPI结构和水结合性质的分析.
主要成果:
- 确定了α-La (6) 和α-La (120) 作为α-乳蛋白 (α-La) 中关键的分子间二硫化物交叉链接点.
- 蛋白质聚合物的分子量随着Cys度的增加而增加,达到100mMCys的峰值.
- 高Cys度改变了WPI的二次结构,从有序到无序,并增加了水结合能力.
结论:
- 与Cys的低温共挤出有效地诱导了WPI中的二硫化物交叉链接.
- α-乳蛋白是WPI聚合中的主要反应物.
- 交叉链接的WPI表现出增强的水容量,使其成为一个有前途的新食品原料.
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