转质氨酶交联是否会降低β-乳糖球蛋白的抗体识别能力:从规范角度分析
Lei Fang1, Xun Han1, Yue Zhang1
1School of Biology and Food Engineering, Changshu Institute of Technology, Changshu 215500, China.
Molecules (Basel, Switzerland)
|February 13, 2025
概括
转谷氨酸酶 (TGase) 治疗可以降低牛奶中的β-乳糖球蛋白 (β-LG) 的过敏性. 这种酶修饰改变了蛋白质结构,降低了抗体识别和IgE结合,为低过敏性乳制品铺平了道路.
科学领域:
- 食品科学 食品科学 食品科学
- 过敏性研究 研究过敏性研究
- 蛋白质化学 蛋白质化学
背景情况:
- β-乳糖球蛋白 (β-LG) 是牛奶中的主要过敏原,在全球引起食物过敏.
- 开发低过敏性乳制品对于公众健康和消费者安全至关重要.
- 酶修饰提供了一种减少蛋白质过敏性的潜在策略.
研究的目的:
- 研究转谷氨酸酶 (TGase) 对抗体识别能力 (ARC) 和β-LG的结构性质的影响.
- 评估TGase介导交叉链接在制造低过敏性乳制品方面的潜力.
- 确定最佳的TGas处理条件,以减少β-LG过敏性.
主要方法:
- 用不同的TGas度和持续时间处理β-LG溶液.
- 使用ELISA测量IgE结合的抗体识别能力的分析.
- 通过电泳,UV-Vis吸收,光谱学和疏水性测量评估结构变化.
主要成果:
- TGase治疗显著降低了β-LG的ARC和IgE结合能力,最佳降低在20U/g和6小时.
- 结构分析表明,随着长时间的TGase处理,紫外线吸收,光强度和水性增加.
- 电泳检测显示没有显著的交叉连接,但结构性修改可能掩盖了过敏原表位.
结论:
- 通过改变其结构和降低抗体识别,TGase有效地降低了β-LG的潜在过敏性.
- 早期的结构变化掩盖了表位,而后期的结构变化可能会导致再暴露.
- 对于开发低过敏性乳制品来管理牛奶过敏,TGase提出了一种有前途的方法.
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