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花生蛋白与大米蛋白共组装的研究:对蛋白质构象和免疫球蛋白E结合能力的影响

Investigation of Co-Assembly of Peanut Protein and Rice Protein: Effects on Protein Conformation and Immunoglobulin E Binding Capacity.

作者信息

Geng Qin, McClements David Julian, Dai Taotao, Li Changhong, Wu Zhihua, Chen Hongbing

机构信息

State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, China.

Sino-German Joint Research Institute, Nanchang University, Nanchang 330047, China.

出版信息

Foods. 2025 May 11;14(10):1699. doi: 10.3390/foods14101699.

DOI:10.3390/foods14101699
PMID:40428478
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12111746/
Abstract

Reducing the allergenicity of food components through processing is attracting great attention in the food industry. This study investigated the structure and allergenicity of complexes formed from peanut protein (PP) and rice protein (RP) using the pH-driven method. The properties of the PP-RP complexes were investigated using morphological analysis, multi-spectroscopic characterization, IgE binding capacity analysis, and in vitro digestibility studies. Morphological analysis showed that the complexes lost their particulate structures after pH-driven treatment. Spectroscopic analysis showed that the pH-driven treatment promoted protein structural changes, making them more susceptible to degradation. There were also changes in the tertiary structures of the proteins in the complexes following the pH-driven treatment. The IgE binding capacity and digestibility studies suggested that the pH-driven treatment reduced the potential allergenicity of PP by altering its structure under gastrointestinal conditions. This study provides a promising approach for producing hypoallergenic peanut protein ingredients for use in the food industry.

摘要

通过加工降低食品成分的致敏性在食品工业中备受关注。本研究采用pH驱动法研究了花生蛋白(PP)和大米蛋白(RP)形成的复合物的结构和致敏性。通过形态分析、多光谱表征、IgE结合能力分析和体外消化率研究对PP-RP复合物的性质进行了研究。形态分析表明,pH驱动处理后复合物失去了颗粒结构。光谱分析表明,pH驱动处理促进了蛋白质结构的变化,使其更容易降解。pH驱动处理后,复合物中蛋白质的三级结构也发生了变化。IgE结合能力和消化率研究表明,pH驱动处理通过在胃肠道条件下改变PP的结构降低了其潜在致敏性。本研究为生产用于食品工业的低致敏性花生蛋白成分提供了一种有前景的方法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/bd6bbf93828b/foods-14-01699-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/e25480977ecd/foods-14-01699-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/78f3d8dfc82d/foods-14-01699-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/13d1f96f4cc9/foods-14-01699-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/9cfcf4f65d4b/foods-14-01699-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/7e96d9b8846d/foods-14-01699-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/04488242f62f/foods-14-01699-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/bd6bbf93828b/foods-14-01699-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/e25480977ecd/foods-14-01699-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/78f3d8dfc82d/foods-14-01699-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/13d1f96f4cc9/foods-14-01699-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/9cfcf4f65d4b/foods-14-01699-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/7e96d9b8846d/foods-14-01699-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/04488242f62f/foods-14-01699-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea5a/12111746/bd6bbf93828b/foods-14-01699-g007.jpg

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本文引用的文献

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Int J Biol Macromol. 2024 Feb;258(Pt 1):128340. doi: 10.1016/j.ijbiomac.2023.128340. Epub 2023 Nov 23.
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IgE Recognition and Structural Analysis of Disulfide Bond Rearrangement and Chemical Modifications in Allergen Aggregations in Roasted Peanuts.IgE 识别与结构分析:烘烤花生中过敏原聚集物中二硫键重排和化学修饰
J Agric Food Chem. 2023 Jun 14;71(23):9110-9119. doi: 10.1021/acs.jafc.3c01482. Epub 2023 May 31.
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Structural and functional properties of self-assembled peanut protein nanoparticles prepared by ultrasonic treatment: Effects of ultrasound intensity and protein concentration.
超声处理制备的自组装花生蛋白纳米颗粒的结构和功能特性:超声强度和蛋白质浓度的影响。
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