基于酶解调节α-乳白蛋白的抗原性:洞察结构和线性表位

IF 2.5 2区 农林科学 Q3 FOOD SCIENCE & TECHNOLOGY
Peng Sun, Guangqing Mu, Ziqi Gao, Anqi Zhao, Qing Zhao, Qi Sun, Xiaomeng Wu, Fanhua Kong
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引用次数: 0

摘要

本研究调查了酶处理对α-乳清蛋白(ALA)过敏性的影响。利用 BIOPEP 数据库,我们确定了五种能最佳清除过敏原表位的蛋白酶,同时考虑了成本效益。值得注意的是,碱性蛋白酶的抗原还原率最高,达到 46.46%,水解度为 30.01%,87.80% 的肽段小于 1 kDa。肽组学分析表明,AA32-38 和 AA42-48 是 ALA 的关键线性表位。此外,碱性蛋白酶处理可显著降低亲水性氨基酸的比例,从而通过降低 IgE/IgG 结合亲和力来降低 ALA 的过敏原潜力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Regulating antigenicity of α‐lactalbumin based on enzymolysis: Insights into structure and linear epitopes
This study investigated the effect of enzymatic treatment on the allergenicity of α‐lactalbumin (ALA). Utilising the BIOPEP database, we identified five proteases that optimally clear allergen epitopes, while considering cost‐efficiency. Notably, alkaline protease demonstrated the highest antigen reduction rate of 46.46%, with a hydrolysis degree of 30.01%, and 87.80% of the resulting peptides were found to be smaller than 1 kDa. Peptidomics analysis revealed AA32–38 and AA42–48 as key linear epitopes of ALA. Furthermore, alkaline protease treatment significantly reduced the proportion of hydrophilic amino acids, thereby decreasing the allergen potential of ALA by lowering its IgE/IgG binding affinity.
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来源期刊
International Journal of Dairy Technology
International Journal of Dairy Technology 工程技术-食品科技
CiteScore
7.00
自引率
4.50%
发文量
76
审稿时长
12 months
期刊介绍: The International Journal of Dairy Technology ranks highly among the leading dairy journals published worldwide, and is the flagship of the Society. As indicated in its title, the journal is international in scope. Published quarterly, International Journal of Dairy Technology contains original papers and review articles covering topics that are at the interface between fundamental dairy research and the practical technological challenges facing the modern dairy industry worldwide. Topics addressed span the full range of dairy technologies, the production of diverse dairy products across the world and the development of dairy ingredients for food applications.
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