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豆类和蛋白蛋白混合物的热行为

Jian Kuang^1,2, Pascaline Hamon², Valérie Lechevalier²

¹PAM UMR A 02.102, L'Institut Agro Dijon, Université Bourgogne Franche-Comté, F-21000 Dijon, France.

Foods (Basel, Switzerland)

|July 14, 2023

概括

用植物蛋白替代动物蛋白提供了可持续的食物选择. 这项研究检查了蛋白和豆蛋白分离混合物,揭示了蛋白质相互作用和pH依赖的凝形成,这对食品加工至关重要.

科学领域:

食品科学与技术食品科学与技术
蛋白质化学蛋白质化学
可持续的粮食生产可持续的粮食生产

背景情况:

用植物蛋白部分替代动物蛋白质是可持续粮食发展的关键.
了解复合蛋白成分的热行为对于控制食品加工至关重要.
蛋白 (EW) 和豆蛋白分离物 (PPI) 是具有明显热性质的常见蛋白质来源.

研究的目的:

为了研究EW和PPI混合物的热行为.
在不同的pH条件下分析蛋白质相互作用和凝特性.
为控制复合蛋白成分的热处理提供见解.

主要方法:

在pH值7.5和9.0下制备具有不同PPI/EW比率 (100/0到0/100) 的蛋白质悬浮液.
差分扫描热量计 (DSC) 用于分析热变性.
动态风湿学 (温度扫描模式) 来评估凝形成和过渡.

主要成果:

DSC数据显示了EW和PPI蛋白之间的相互作用,改变了变性化温度.
变化度 (∆H) 取决于pH值,与豆蛋白展开和溶解性变化有关.
凝形成主要由EW蛋白控制,混合物显示弹性模量 (G') 增加,EW含量更高.
在含有EW的系统中观察到两种热sol-gel转换;第一个转换在pH9.0时是由于豆球蛋白相互作用引起的.

结论:

在EW和PPI之间发生蛋白相互作用,影响热变性和凝.
pH显著影响蛋白质的展开,溶解度和整体凝过程.
在这些复合系统中,EW蛋白主导着凝网络的形成,豆蛋白调节过渡.

关键词:

凝血是凝固的过程.不同扫描热量计差异扫描热量计.蛋白蛋白是一种蛋白质.凝结点是凝结点的时间.豆蛋白分离物豆蛋白分离物溶解度溶解度溶解度溶解度

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