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热诱导大豆乳清蛋白相互作用:可溶性和不溶性蛋白质复合物的形成。

Heat-induced soy-whey proteins interactions: formation of soluble and insoluble protein complexes.

作者信息

Roesch Rodrigo R, Corredig Milena

机构信息

Department of Food Science, University of Guelph, Guelph, Ontario N1G 2W1, Canada.

出版信息

J Agric Food Chem. 2005 May 4;53(9):3476-82. doi: 10.1021/jf048870d.

Abstract

The aggregation behavior during heating of a solution containing soy protein and whey protein isolate (WPI) was studied using rheology, confocal microscopy, gel filtration, and electrophoresis. Soy/WPI mixtures formed gels at 6% total protein concentration with a high elastic modulus (G') and no apparent phase separation. The ratio of soy to WPI was fundamental in determining the type of network formed. Systems containing a high soy to WPI ratio (>70% soy protein) showed a different evolution of the elastic modulus during heat treatment, with two apparent stages of network development. Whey proteins formed disulfide bridges with soy proteins during heating, and at low ratios of soy/WPI, the aggregates seemed to be predominantly formed by 7S, the basic subunits of 11S and beta-lactoglobulin. Size exclusion chromatography indicated the presence of high molecular weight soluble complexes in mixtures containing high soy/WPI ratios. Results presented are the first evidence of interactions between soy proteins and whey proteins and show the potential for the creation of a new group of functional ingredients.

摘要

使用流变学、共聚焦显微镜、凝胶过滤和电泳研究了含有大豆蛋白和乳清分离蛋白(WPI)的溶液在加热过程中的聚集行为。大豆/WPI混合物在总蛋白浓度为6%时形成凝胶,具有高弹性模量(G')且无明显相分离。大豆与WPI的比例是决定形成的网络类型的关键因素。大豆与WPI比例高(大豆蛋白>70%)的体系在热处理过程中弹性模量呈现不同的变化,有两个明显的网络发展阶段。加热过程中乳清蛋白与大豆蛋白形成二硫键,在低大豆/WPI比例下,聚集体似乎主要由7S、11S的基本亚基和β-乳球蛋白形成。尺寸排阻色谱表明在大豆/WPI比例高的混合物中存在高分子量可溶性复合物。所呈现的结果是大豆蛋白和乳清蛋白之间相互作用的首个证据,并显示了创造一组新的功能成分的潜力。

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