大豆分离蛋白和乳清分离蛋白复合纳米颗粒的制备及其在高内相皮克林乳剂中的性能研究

IF 9.8 1区 农林科学 Q1 CHEMISTRY, APPLIED Food Chemistry Pub Date : 2025-06-15 Epub Date: 2025-02-19 DOI:10.1016/j.foodchem.2025.143476
Yaxin Yin , Jue Xu , Zihang Shi , Daodong Pan , Zhen Wu , Xiaoqun Zeng , Maolin Tu
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引用次数: 0

摘要

本研究探讨了热驱动在大豆分离蛋白和乳清分离蛋白(SPI-WPI)配合物形成中的作用,以及SPI-WPI配合物在高内相皮克林乳剂(hips)中的稳定性作用。红外光谱峰的移动和荧光强度的变化表明了这两种蛋白之间的相互作用,这表明SPI-WPI不是两个分散的粒子群。当SPI与WPI质量比为7:3时,最大乳化活性为10.65 m2/g,电势绝对值为37.87 mV。随着SPI-WPI复合物浓度和pH的增加,液滴变得均匀致密。预测高浓度条件更有利于凝胶网络结构的形成。本研究为利用复合蛋白稳定hipes提供了有效的策略。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Research on the preparation of soy protein isolate and whey protein isolate composite nanoparticles and their characteristics in high internal phase Pickering emulsions
This study investigated the role of thermal drive in the formation of soy protein isolate and whey protein isolate (SPI–WPI) complexes, as well as the stability effect of SPI–WPI complexes on high internal phase Pickering emulsions (HIPPEs). The shift in the peaks in the infrared spectrum and the change in fluorescence intensity indicated the interaction between these two proteins, which implies that SPI–WPI is not two dispersed groups of particles. Maximum emulsification activity (10.65 m2/g) and the absolute value of potential (37.87 mV) were achieved at an SPI to WPI mass ratio of 7:3. As the concentration and pH of the SPI–WPI complex increased, the droplets become evenly uniform and compact. It is predicted that the high concentration conditions are more favorable for the formation of a gel network structure. This research provides an effective strategy for HIPPEs stabilization using complex proteins.
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来源期刊
Food Chemistry
Food Chemistry 工程技术-食品科技
CiteScore
16.30
自引率
10.20%
发文量
3130
审稿时长
122 days
期刊介绍: Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.
期刊最新文献
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