Actinidin-induced hydrolysis of milk proteins: Effect on antigenicity

Actinidin was used to hydrolyse proteins in whey protein isolate (WPI) and milk concentrate (MPC) reduce immunoreactivity of β-lactoglobulin (β-LG) αs1-casein (αs1-CN). Samples were incubated at an enzyme substrate ratio 1:100 (5.21 units actinidin activity g−1 protein) 10 or 60 °C for up 31 5 h, respectively. Protein hydrolysis determined by the degree SDS-PAGE. Antigenicity hydrolysates β-LG αs1-CN antibody-binding capacity using enzyme-linked immunosorbent assay (ELISA) quantification kits. ELISA showed significant reduction antigenicity with higher (DH) actinidin. At °C, h resulted ∼43% ∼48% MPC ∼54% WPI. Hydrolysis also decrease ∼39 42% respectively, but only 14% Treatment can modification conformation cleavage masking epitopes αs1-CN.