化学
帕尔瓦布明
低过敏性
食品科学
敏化
蛋白质二级结构
微观结构
生物化学
结晶学
生物
过敏
神经科学
过敏原
免疫学
作者
Xiaomin Li,Yun Deng,Weiqiang Qiu,Yuhui Feng,Yu Jin,Lanming Chen,Li Li,Ashily Ling Wang,Ningping Tao,Yinzhe Jin
出处
期刊:Food Chemistry
[Elsevier]
日期:2024-01-01
卷期号:432: 137257-137257
被引量:2
标识
DOI:10.1016/j.foodchem.2023.137257
摘要
We investigated the effects of ohmic heating (OH) on the structural properties and allergenicity of parvalbumin (PV). Compared to other heating methods (water bath heating (WH), OH combined with WH, and OH combined with air thermostatic heating (AH)), pure OH heating expended the least time and total energy. PV sensitization was reduced by approximately 65% by pure OH heating. SDS-PAGE, tricine-SDS-PAGE, and western blotting analyses revealed a molecular weight of sensitized β-PV of about 12 kDa. Band intensity decreased with increasing OH time, and significant changes were observed in amino acid content, secondary structure, microstructure, and dielectric properties. Reducing PV, allergenicity through protein unfolding and secondary structural changes, thereby possibly reducing the allergenicity of eel, provides a theoretical basis for developing hypoallergenic products.
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