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 re...

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Bibliographic Details
Published inInternational journal of dairy technology Vol. 77; no. 4; pp. 1170 - 1182
Main Authors Sun, Peng, Mu, Guangqing, Gao, Ziqi, Zhao, Anqi, Zhao, Qing, Sun, Qi, Wu, Xiaomeng, Kong, Fanhua
Format Journal Article
LanguageEnglish
Published Oxford Blackwell Publishing Ltd 01.11.2024
Subjects
Alkaline protease
Allergenicity
Allergens
Amino acids
Antigenicity
Enzymolysis
Epitopes
Immunoglobulin G
Lactalbumin
Linear epitopes
Peptides
Peptidomics
Protease
α‐Lactalbumin
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Summary: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. This article reveals the differential effects of different proteases on the antigenicity of α‐lactalbumin, in order to reveal their mechanisms of action on structure and linear epitopes.
Bibliography:These two authors contributed equally to this work.
ISSN:1364-727X
1471-0307
DOI:10.1111/1471-0307.13128