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首页> 外文期刊>Food Science & Nutrition >In vitro evaluation of digestive and endolysosomal enzymes to cleave CML‐modified Ara h 1 peptides
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In vitro evaluation of digestive and endolysosomal enzymes to cleave CML‐modified Ara h 1 peptides

机译：体外评估消化酶和溶酶体酶以裂解CML修饰的Ara h 1肽

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AbstractAra h 1 is a major peanut allergen. Processing-induced modifications may modulate the allergenic potency of Ara h 1. Carboxymethyl lysine (CML) modifications are a commonly described nonenzymatic modification on food proteins. In the current study, we tested the ability of digestive and endolysosomal proteases to cleave CML-modified and unmodified Ara h 1 peptides. Mass spectrometric analyses of the digested peptides demonstrate that carboxymethylation of lysine residues renders these peptides refractory to trypsin digestion. We did not detect observable differences in the simulated gastric fluid or endolysosomal digestion between the parental and CML-modified peptides. One of the tested peptides contains a lysine residue previously shown to be CML modified laying in a previously mapped linear IgE epitope, but we did not observe a difference in IgE binding between the modified and parental peptides. Our findings suggest a molecular mechanism for the increased resistance of peanut allergens modified by thermal processing, such as Ara h 1, to digestion in intestinal fluid after heating and could help explain how food processing-induced modifications may lead to more potent food allergens by acting to protect intact IgE epitopes from digestion by proteases targeting lysine residues.
机译：摘要Ara h 1是主要的花生过敏原。加工诱导的修饰可能会调节Ara h 1的变应原效力。羧甲基赖氨酸（CML）修饰是通常描述的对食物蛋白质的非酶修饰。在当前的研究中，我们测试了消化酶和溶酶体蛋白酶切割CML修饰和未修饰的Ara h 1肽的能力。消化的肽的质谱分析表明，赖氨酸残基的羧甲基化使这些肽对胰蛋白酶消化具有抵抗力。我们没有发现亲本和CML修饰的肽在模拟胃液或溶酶体消化中可观察到的差异。一种被测试的肽含有一个赖氨酸残基，该赖氨酸残基先前显示为CML修饰，位于一个先前定位的线性IgE表位中，但我们没有观察到修饰肽和亲本肽之间IgE结合的差异。我们的发现表明，通过加热处理（例如Ara h 1）修饰的花生过敏原对加热后肠液中消化的抵抗力增强的分子机制，并可能有助于解释食品加工诱导的修饰如何通过发挥作用而导致更有效的食物过敏原保护完整的IgE表位免受针对赖氨酸残基的蛋白酶的消化。

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