在UHT牛奶加工过程中,探索β-乳糖球蛋白和素小粒之间的动态相互作用
Tai Zhang1, Yisuo Liu1, Jiayuan Cao2
1State Key Laboratory of Marine Food Processing & Safety Control, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, Shandong Province, China; Food Laboratory of Zhongyuan, Luohe 462300, Henan, China.
International journal of biological macromolecules
|August 1, 2024
概括
超高温 (UHT) 处理导致牛奶中的蛋白质聚合. 这项研究揭示了β-乳糖球蛋白 (β-Lg) 如何与素小粒相互作用,导致聚合和缩短保质期.
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
- 乳制品技术 乳制品技术
背景情况:
- 牛奶的超高温 (UHT) 处理导致蛋白质聚合,减少保质期.
- 在UHT治疗过程中,β-乳糖球蛋白 (β-Lg) 诱导素小细胞聚合的确切机制尚未完全理解.
研究的目的:
- 在UHT加工过程中研究β-Lg和素粒之间的动态相互作用.
- 阐明在牛奶中UHT诱导的蛋白质聚合背后的分子机制.
主要方法:
- 实验技术包括拉曼光谱,FTIR,冷TEM,SAXS和MST.
- 分子动力学模拟和分子对接.
主要成果:
- β-Lg 破坏了素小粒的稳定,增加了它们的尺寸和zeta潜力.
- 和二硫化物键被确定为β-Lg和素微粒相互作用的关键促进者.
- 发现β-Lg在细胞表面与kd为3.84±1.14μm的 κ-素结合.
- 非共价相互作用 (静电,范德瓦尔斯) 启动聚合,随后形成二硫化键.
结论:
- 在β-Lg和素小粒之间发生的非共价相互作用和随后的二硫化结合促使UHT牛奶中的蛋白质聚合.
- 了解这些相互作用为改善UHT加工乳制品的稳定性和保质期提供了关键的见解.
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