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• W2900258564 abstract "Denaturation of β-lactoglobulin (BLG) was studied in relation to its antigenicity at two heat treatments in several native protein mixtures; allergenicity was determined by enzyme-linked immunosorbent assay based on BLG capacity to bind with immunoglobulin G (IgG) antibodies. The influence of other proteins on BLG denaturation correlated with altered antigenicity. Treatment at 72 °C/15 s enhanced antigenicity in a BLG+α-lactalbumin (ALA) mixture, possibly due to exposed epitopes in the unfolded structure. Treatment at 100 °C/30 s mostly resulted in BLG-led protein aggregation through thiol/disulphide interactions and decreased antigenicity by fragmentation and masking of epitopes, the extent of which was mixture-dependent. The presence of IgG resulted in diminished antigenicity in BLG + ALA + IgG at 100 °C/30 s in comparison with BLG + ALA. ALA governed whey protein denaturation over BLG in BLG + ALA + IgG + bovine serum albumin (BSA), possibly catalysed by BSA at 100 °C/30 s, resulting in a higher retention of antigenicity than in other mixtures." @default.
• W2900258564 created "2018-11-16" @default.
• W2900258564 creator A5077429658 @default.
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• W2900258564 date "2019-04-01" @default.
• W2900258564 modified "2023-10-18" @default.
• W2900258564 title "Thermal denaturation of bovine β-lactoglobulin in different protein mixtures in relation to antigenicity" @default.
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• W2900258564 doi "https://doi.org/10.1016/j.idairyj.2018.10.004" @default.
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