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在pH值和热处理期间,以光和X射线散射研究豆衍生的白蛋白的结构演变

Ruifen Li¹, Jacob J K Kirkensgaard², Milena Corredig¹

¹Department of Food Science & CiFood Center for Innovative Food Research, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark.

Food research international (Ottawa, Ont.)

|May 10, 2024

概括

豆蛋白表现出明显的结构变化和聚合行为,受pH和热量的影响. 它们在酸性pH3时保持稳定,但在更高的pH水平时聚合,特别是在加热后.

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
生物物理分析分析

背景情况:

豆蛋白是豆蛋白加工侧流中发现的可溶性蛋白质.
它们的功能性质不同于豆球蛋白,具有作为食品成分的潜力.

研究的目的:

在不同的pH值和热量条件下,研究豆蛋白的聚合和结构变化.
了解 pea 专素的稳定性和行为,以应用于潜在的食品应用.

主要方法:

通过在酸性pH下沉球蛋白来提取豆类白蛋白.
使用尺寸排除色谱加上多角度激光光散射 (SEC-MALS) 的分析.
使用小角度X射线散射 (SAXS) 在不同的pH值和热处理下进行结构研究.

主要成果:

豆蛋白显示了四种不同的种群,包括单体 (PA1),二元体 (PA2) 和大聚合物 (~250 kDa).
专在pH3时最稳定,在热处理过程中没有观察到聚合.
在加热后在pH 7.5和8发生聚合,而在pH 4,4.5和7.7加热之前,聚合物也存在.

结论:

豆蛋白的稳定性高度依赖于pH值和温度.
了解这些结构动态对于优化 pea 专素作为功能性食品成分的使用至关重要.

关键词:

专辑蛋白,结构,结构热引起的聚合是由于热引起的.豆蛋白质是一种豆蛋白质.美国证券交易所 (SEC-MALS)小角X射线散射的小角度X射线散射.

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