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Article Abstract
Cow milk allergy is one of the common food allergy, and goat milk is a potential alternatives. However, research on its sensitization is limited, and its practicle application remains controversial. This study combined molecular docking and molecular dynamics simulation to investigate hotspot residues and epitopes of goat α-lactalbumin (α-LA) and β-lactoglobulin (β-LG). Energy calculations showed that Phe31 and Gln35 played key roles in binding of α-LA and β-LG to IgG. A comprehensive analysis of hotspot amino acids and antigenic epitopes revealed that the binding regions of α-LA to IgG-Fab were Phe31-Leu42 and Tyr103-Leu110, while those in β-LG are Ala34-Ser36, Trp61-Gly64, and Ile147-Phe151. Hydrolysis of goat whey protein by alcalase reduced the antigenicity of α-LA and β-LG by 59.27 % and 33.21 %, respectively. LC-MS/MS analysis further confirmed that alcalase enzyme significantly disrupted the antigenic epitopes of goat whey protein. This study provided a theoretical foundation for developing hypoallergenic goat whey protein products.
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| http://dx.doi.org/10.1016/j.foodchem.2025.145835 | DOI Listing |
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