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Updated: Jan 16, 2026
Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
Published on: February 24, 2021
A study on structural, functional properties and allergenicity of β-lactoglobulin by malondialdehyde during milk
Xin Qu1, Ni Yang2, Ying Zhang3
1Qingdao Municipal Center For Disease Control & Prevention, Qingdao, China.
Background:
β-;actoglobulin (βLG) is the main component of milk. Milk βLG is highly susceptible to lipid peroxidation during processing and preservation. Notably, malondialdehyde (MDA) is one of the main lipid peroxidation products, which could influence the structure, functional properties and allergenicity of βLG. In the present study, the structure of different samples was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, fluorescence spectroscopy, circular dichroism, and liquid chromatography-tanndem mass spectrometry. Functional properties were determined by foaming and emulsifying properties. Allergenicity was assayed by cell and animal models.
Results:
The results revealed that MDA induced changes in the structural profile of βLG. The special amino acids, lysine, histidine, arginine, glycine and phenylalanine were modified. These structural changes of βLG influence foaming and emulsifying properties. Furthermore, KU812 cell results showed that the release of histamine and β-hexosaminidase decreased by 55.6% and 43.3% with 20 mm MDA treatment, respectively. The BALB/c mouse model showed that the MDA-βLG group had decreased levels of antibodies, histamine and mMCP-1 in sera. Notably, the allergenicity was substantially reduced by promoting Th1-related cytokines and suppressing Th2-related cytokines.
Conclusion:
The present study has revealed that MDA treatment induced changes in the functional and allergic properties during milk processing. © 2025 Society of Chemical Industry.
Insights
Malondialdehyde (MDA) modifies milk β-lactoglobulin (βLG) structure, altering its functional and allergenic properties. MDA treatment reduced allergenicity by modulating immune responses, offering insights for milk processing.
Area of Science:
- Food Science
- Biochemistry
- Immunology
Background:
- β-lactoglobulin (βLG) is a primary milk protein susceptible to lipid peroxidation.
- Malondialdehyde (MDA), a lipid peroxidation product, can alter βLG structure, function, and allergenicity.
Purpose of the Study:
- To investigate the impact of MDA on βLG structure, functional properties, and allergenicity.
- To assess the potential of MDA treatment to modify milk protein allergenicity.
Main Methods:
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)
- Fluorescence spectroscopy
- Circular dichroism (CD)
- Liquid chromatography-tandem mass spectrometry (LC-MS/MS)
- Foaming and emulsifying property assays
- Cell-based assays (KU812 cells)
- Animal models (BALB/c mice)
Main Results:
- MDA treatment induced structural modifications in βLG, affecting specific amino acids.
- Structural changes impacted βLG's foaming and emulsifying capabilities.
- MDA-βLG treatment significantly reduced histamine and β-hexosaminidase release in KU812 cells.
- In mice, MDA-βLG decreased specific antibodies, histamine, and mMCP-1, promoting Th1 and suppressing Th2 immune responses.
Conclusions:
- MDA treatment alters the functional and allergenic properties of βLG.
- This study demonstrates MDA's potential to reduce milk protein allergenicity during processing.
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