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茶儿茶素与酪蛋白胶束的相互作用及其对凝乳酶功能的影响。

Interactions between tea catechins and casein micelles and their impact on renneting functionality.

机构信息

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

出版信息

Food Chem. 2014 Jan 15;143:27-32. doi: 10.1016/j.foodchem.2013.07.092. Epub 2013 Jul 27.

Abstract

Many studies have shown that tea catechins bind to milk proteins. This research focused on the association of tea polyphenols with casein micelles, and the consequences of the interactions on the renneting behaviour of skim milk. It was hypothesized that epigallocatechin-gallate (EGCG), the main catechin present in green tea, forms complexes with the casein micelles and that the association modifies the processing functionality of casein micelles. The binding of EGCG to casein micelles was quantified using HPLC. The formation of catechin-casein micelles complexes affected the rennet induced gelation of milk, and the effect was concentration dependent. Both the primary as well as the secondary stage of gelation were affected. These experiments clearly identify the need for a better understanding of the effect of tea polyphenols on the processing functionality of casein micelles, before milk products can be used as an appropriate platform for delivery of bioactive compounds.

摘要

许多研究表明,茶儿茶素与牛奶蛋白结合。本研究集中于研究多酚与酪蛋白胶束的相互作用,以及相互作用对脱脂牛奶凝乳行为的影响。研究假设,绿茶中主要的儿茶素表没食子儿茶素没食子酸酯(EGCG)与酪蛋白胶束形成复合物,并且这种结合改变了酪蛋白胶束的加工功能。使用 HPLC 定量测定 EGCG 与酪蛋白胶束的结合。儿茶素-酪蛋白胶束复合物的形成影响了牛奶的凝乳诱导凝胶化,并且这种影响是浓度依赖性的。凝胶化的初级和次级阶段都受到影响。这些实验清楚地表明,在将乳制品用作生物活性化合物传递的合适平台之前,需要更好地了解茶多酚对酪蛋白胶束加工功能的影响。

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