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Optimizing β-Lactoglobulin antigenicity through single enzyme hydrolysis: Exploring structural changes and effects on

Peng Sun¹, Xiaomeng Wu¹, Qi Sun¹

¹School of Food Science and Technology, Dalian Polytechnic University, Dalian 116000, Liaoning, China.

|October 30, 2024

Summary

Enzymatic hydrolysis using pepsin, chymotrypsin A, papain, and stem bromelain effectively reduced beta-lactoglobulin (β-LG) allergenicity by degrading its structure and cleaving allergenic epitopes.

Keywords:

Antigenic epitopes Enzymatic hydrolysis Peptidomics Structure change β-Lactoglobulin

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Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens

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Published on: February 24, 2021

Area of Science:

Food Science
Allergy Research
Biochemistry

Background:

Beta-lactoglobulin (β-LG) is a primary dairy allergen.
Limited research exists on optimal enzymatic conditions for reducing β-LG antigenicity.
Bioinformatics can identify proteases for allergen epitope elimination.

Purpose of the Study:

Investigate antigenicity, structure, and peptide profiles of β-LG hydrolysates.
Identify proteases that effectively eliminate allergenic epitopes.
Provide a basis for low-allergenicity dairy material development.

Main Methods:

Bioinformatic selection of advantageous proteases.
Enzymatic hydrolysis of β-LG using pepsin, chymotrypsin A, papain, and stem bromelain.
Analysis of antigen reduction, structural changes, and peptide distribution.

Main Results:

Optimal hydrolysis reduced β-LG antigenicity by 33.54%–47.37%.
Proteases degraded β-LG, reducing α-helix content, fluorescence, and surface hydrophobicity.
Cleavage of linear epitopes resulted in varying antigen reduction rates.

Conclusions:

Enzymatic hydrolysis effectively reduces β-LG allergenicity.
Specific proteases offer targeted approaches for creating low-allergenicity dairy products.
Findings support developing enzymatic hydrolysis for hypoallergenic dairy materials.