高度 kazein micelles 和豆蛋白混合系统的酸凝
Luis Gustavo Lima Nascimento1, Raiane Rodrigues da Silva2, Davide Odelli2
1Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa (UFV), 36570-900 Viçosa, Minas Gerais, Brazil; Lille, CNRS, INRAE, Centrale Lille, UMR 8207 - UMET - Unité Matériaux et Transformations, équipe Processus aux Interfaces et Hygiène des Matériaux (PIHM), F-59000 Lille, France.
Food research international (Ottawa, Ont.)
|November 30, 2024
概括
这项研究探讨了混合豆和牛奶蛋白来改善植物性食品质感. 结果表明,特定的比例和预处理可以定制凝特性,增强弹性,并可能克服任何风味问题.
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
- 材料科学 材料科学 材料科学
背景情况:
- 对植物性蛋白质 (大豆,豆,豆) 的需求不断增长,面临着质地差和豆香味等挑战.
- 牛奶蛋白被广泛接受,使其与植物蛋白结合成为改善食品的有希望的战略.
- 混合植物和牛奶蛋白可以显著改变凝形成和最终产品结构.
研究的目的:
- 在高度下通过酸化制造混合素小粒 (CMs) 和豆蛋白凝,使用四种不同的蛋白质比例 (80:20,60:40,40:60,20:80).
- 研究热预处理对凝过程和最终凝特性的影响.
- 了解不同蛋白质比例如何影响凝形成动力学和机械性能.
主要方法:
- 使用高度的素微粒 (CMs) 和豆蛋白制备混合凝.
- 酸性化过程以诱导四种不同的蛋白质比例的凝.
- 在酸性化之前热处理对凝性质的影响的评估.
- 风湿学测量 (G*),以评估凝弹性和形成动态.
主要成果:
- 用豆蛋白替换CMs延迟了初始凝的形成,并增加了G*上升所需的时间,特别是在较高度的豆蛋白中.
- 在80:20和60:40的比例下,在豆蛋白的存在下,最终的凝弹性得到了增强,这表明豆蛋白网络的形成.
- CMs似乎限制了豆蛋白的聚合,这表明影响网络结构的复杂相互作用.
结论:
- 可以成功地开发混合素微粒和豆蛋白凝,通过调整蛋白质比率来调整性能.
- 热预处理和特定蛋白质比率可以控制凝特性,为开发新型食品铺平了道路.
- 这些发现突出了利用豆蛋白与乳制品蛋白结合使用的潜力,以创建改进的植物性食品成分.
相关概念视频
03:22Colloids
17.3K
Children at play often make suspensions such as mixtures of mud and water, flour and water, or a suspension of solid pigments in water known as tempera paint. These suspensions are heterogeneous mixtures composed of relatively large particles that are visible to the naked eye or can be seen with a magnifying glass. They are cloudy, and the suspended particles settle out after mixing. On the other hand, a solution is a homogeneous mixture in which no settling occurs and in which the dissolved...
17.3K
01:27SDS-PAGE
27.4K
Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
27.4K