Non-covalent interaction of the plant protein composites-proanthocyanidins and the utilization in oil in water emulsions
文献类型： 外文期刊
作者： Wang, Xiaoxiao 1 ; Chen, Jun 1 ; Geng, Qin 1 ; He, Xuemei 3 ; Tang, Yayuan 3 ; Deng, Lizhen 1 ; Li, Ti 1 ; Liu, Chengmei 1 ; Dai, Taotao 1 ;
作者机构： 1.Nanchang Univ, State Key Lab Food Sci & Resources, Nanchang 330047, Peoples R China
2.Nanchang Univ, Int Inst Food Innovat Co Ltd, Nanchang, Jiangxi, Peoples R China
3.Guangxi Acad Agr Sci, Nanning 530007, Guangxi, Peoples R China
4.Nanchang Univ, 235 Nanjing East Rd, Nanchang, Peoples R China
关键词： Plant proteins; Proanthocyanidins; Interaction; Emulsion
期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：6.0； 五年影响因子：6.0 ）
ISSN： 0023-6438
年卷期： 2024 年 198 卷
页码：
收录情况： SCI
摘要： The polyphenols and plant proteins are increasingly being utilized as functional food ingredients, it is critical to understand their interaction mechanism with each other. In this study, protein composites (RP-PP and RP-SPI) were fabricated using pH-driven technology by rice protein (RP) with pea protein (PP) and soy protein isolates (SPI), respectively. The interaction mechanism between the protein composites and proanthocyanidins (PA) was also explored using a combined approach of spectroscopy and thermodynamics. The analysis of fluorescence spectroscopy and turbidity confirmed the formation of the protein composites-PA colloidal complexes. The thermodynamic results calculated from fluorescence data and ITC analysis indicated the hydrogen bond was the main interaction force between the protein composites and PA. The secondary structures of the protein composites were changed with the decreased alpha-helix and beta-turn due to the increasing PA. In addition, the existence of PA reduced the surface hydrophobicity, particle size, and the interfacial tension of proteins. Furthermore, the thermal stability and zeta potential of proteins increased after the binding of the PA. Ultimately, the PA showed a potential in reducing the dimension of droplet and enhancing storage stability of proteins-PA emulsion. This study provides useful information for the industrial application of the proteins-polyphenols complexes.
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