抗原性
变性(裂变材料)
牛血清白蛋白
化学
乳清蛋白
表位
乳清蛋白
生物化学
抗体
血清白蛋白
色谱法
分子生物学
生物
免疫学
核化学
作者
Dimuthu Bogahawaththa,Jayani Chandrapala,Todor Vasiljevic
标识
DOI:10.1016/j.idairyj.2018.10.004
摘要
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.
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