{"title":"Regulating antigenicity of α‐lactalbumin based on enzymolysis: Insights into structure and linear epitopes","authors":"Peng Sun, Guangqing Mu, Ziqi Gao, Anqi Zhao, Qing Zhao, Qi Sun, Xiaomeng Wu, Fanhua Kong","doi":"10.1111/1471-0307.13128","DOIUrl":null,"url":null,"abstract":"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.","PeriodicalId":13822,"journal":{"name":"International Journal of Dairy Technology","volume":null,"pages":null},"PeriodicalIF":2.5000,"publicationDate":"2024-08-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Dairy Technology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1111/1471-0307.13128","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
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.
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.