The effect of roasting on peanut allergens’ digestibility, allergenicity, and structure
The effect of roasting on peanut allergens’ digestibility, allergenicity, and structure
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烘烤对花生过敏原消化率、过敏性和结构的影响
DOI：
10.1016/j.fbio.2021.101454
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发表时间：
2021
期刊：
影响因子：
5.2
通讯作者：
陈红兵
中科院分区：
文献类型：
--
作者：
周红菲;吴志华;常雪娇;唐宇;袁娟丽;李欣;杨安树;佟平;陈红兵
花生过敏是最普遍且危及生命的食物过敏之一。烘烤是为了改善花生的感官品质，改变过敏原的结构和致敏性。消化的脱脂花生粉的潜在过敏性在生花生和烤花生之间没有显着差异。用胰蛋白酶消化生/烤花生蛋白，然后使用同量异位标签进行相对和绝对定量（iTRAQ）分析，以发现肽量的变化。在检测到的44种肽中，有29种肽在烘烤后丰度显着增加，增幅高达36.78倍。在这 29 种肽中，有 17 种肽与线性 IgE 结合表位重叠，这些表位在烘烤后要么被破坏，要么暴露。结合空间结构模型，iTRAQ结果表明烘焙过程中蛋白质二硫键断裂和解聚。烘烤改变了蛋白质的构象结构，增加了过敏原的消化率，但并不能保证花生的潜在过敏性降低。
Peanut allergy is among the most widespread and life-threatening food allergies. Roasting was conducted to improve the sensorial quality of peanut and to change the structure and allergenicity of allergens. The potential allergenicity of digested defatted peanut powder did not significantly differ between raw and roasted peanuts. The raw/roasted peanut proteins were digested by trypsin and then analyzed with isobaric tags for relative and absolute quantitation (iTRAQ) to discover the changes in peptide quantity. Among the 44 detected peptides, the abundance of 29 peptides significantly increased by up to 36.78 times after roasting. Among those 29 peptides, seventeen peptides overlapped with linear IgE-binding epitopes, which were either destroyed or exposed after roasting. Combined with the spatial structure model, the iTRAQ result indicated the breaking of disulfide bonds and depolymerization of proteins during roasting. Roasting changed the conformational structure of protein, which increased allergen digestibility but did not guarantee a decrease in the potential allergenicity of peanut.