Antigenicity of α-casein reduced by hydrolysis function using Clavispora lusitaniae DPU-MWFCl-D2 isolated from infant feces combining with alkaline protease

Bovine casein, particularly α-casein, is a common source of allergenic epitopes that trigger adverse immune responses in susceptible individuals. In this study, we developed a method to significantly reduce the antigenicity of α-casein by combining hydrolysis with yeast and alkaline proteases. enzyme-linked immunosorbent assay, liquid chromatography coupled with tandem mass spectrometry, Tricine-SDS-PAGE, and electronic tongue were employed to assess the products of two-step hydrolysis. Infant and child allergy serum was used to evaluate IgE binding capacity. The serum IgE inhibition rate of the hydrolysate was 23.55% and the antigenicity of α-casein decreased by 81.40%. The bitterness and astringency produced during hydrolysis are also reduced. These results indicate that the combined hydrolysis of Clavispora lusitaniae DPU-MWFCl-D2 with an alkaline protease enhances the breakdown of allergenic epitopes, striking a balance between diminished antigenicity and good taste. This study provides a potential solution for developing hypoallergenic dairy products.