质谱法分析烘焙对花生过敏原Ara h 1潜在致敏性的影响

doi:10.7506/spkx1002-6630-20200113-144

食品科学 ›› 2021, Vol. 42 ›› Issue (3): 1-6.doi: 10.7506/spkx1002-6630-20200113-144

• 基础研究 • 下一篇

质谱法分析烘焙对花生过敏原Ara h 1潜在致敏性的影响

周红菲，吴志华，张英，陈红兵

（1.南昌大学食品科学与技术国家重点实验室，江西南昌 330047；2.南昌大学食品学院，江西南昌 330031； 3.南昌大学中德联合研究院，江西南昌 330047）

发布日期:2021-02-25
基金资助:
国家自然科学基金面上项目（31771924）；国家自然科学基金地区科学基金项目（31660446）；江西省主要学科学术和技术带头人资助计划项目（20172BCB22003）

Effect of Roasting on the Potential Allergenicity of Peanut Allergen Ara h 1 Evaluated by Mass Spectrometry

ZHOU Hongfei, WU Zhihua, ZHANG Ying, CHEN Hongbing

(1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; 2. College of Food Science and Technology, Nanchang University, Nanchang 330031, China; 3. Sino-German Joint Research Institute, Nanchang University, Nanchang 330047, China)

Published:2021-02-25

摘要/Abstract

摘要： 为研究烘焙对花生过敏原Ara h 1潜在致敏性的影响，采用高离液序列盐溶液从鲜花生和烘焙花生中提取总蛋白，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析烘焙前后蛋白条带变化情况，并对其中的花生主要过敏蛋白Ara h 1条带进行质谱和Swiss-Model模型分析。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳结果显示，烘焙花生蛋白出现了大分子聚合物条带以及较多弥散状蛋白条带，说明烘焙过程中蛋白质会发生聚集，同时也可能发生降解。对鲜花生Ara h 1条带的质谱分析结果显示，检测出70 条肽段，覆盖率达到79.2%；而烘焙后其中40 条肽段未能检出，但新增1 条肽段，且覆盖率降至43.9%。全部71 个肽段涉及到Ara h 1的18 个过敏原线性表位，酶解后鲜花生中检出16 个过敏原线性表位被破坏，烘焙花生中仅发现12 个被破坏。结论：烘焙加工会破坏蛋白质高级结构，掩盖了部分酶切位点，减少了酶解对过敏原线性表位的破坏，这可能是导致烘焙加工后Ara h 1致敏性强于未加工样品的原因。

关键词: 烘焙；花生；Ara?h?1；质谱；结构；致敏性

Abstract: In order to evaluate the effect of roasting on the potential allergenicity of peanut allergen Ara h 1, total protein was extracted from raw and roasted peanuts with chaotropic salt solution and submitted to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The major peanut allergen Ara h 1 separated in the gel was analyzed by mass spectrometry (MS) and Swiss-Model. SDS-PAGE results showed that the roasted peanut protein sample were separated into one macromolecular aggregate band and multiple scattered protein bands, indicating that the protein could aggregate or degrade during roasting. In raw peanut samples, 70 Ara h 1 peptides were detected with a coverage rate of 79.2%. After roasting, 40 of these peptides were found to disappear, but one new peptide was acquired, and the coverage rate consequently decreased to 43.9%. The 71 peptides involved 18 linear IgE-binding epitopes of Ara h 1, and 16 epitopes in raw peanuts were destroyed after enzymatic hydrolysis, while only 12 were destroyed in roast peanuts. Roasting could enhance the allergenicity of peanut Ara h 1 by damaging the spatial structure of the protein and masking some cleavage sites to protect linear IgE-binding epitopes from enzymatic cleavage.

Key words: roasting; peanut; Ara h 1; mass spectrometry; structure; allergenicity

中图分类号:

TS255.1

周红菲，吴志华，张英，陈红兵. 质谱法分析烘焙对花生过敏原Ara h 1潜在致敏性的影响[J]. 食品科学, 2021, 42(3): 1-6.

ZHOU Hongfei, WU Zhihua, ZHANG Ying, CHEN Hongbing. Effect of Roasting on the Potential Allergenicity of Peanut Allergen Ara h 1 Evaluated by Mass Spectrometry[J]. FOOD SCIENCE, 2021, 42(3): 1-6.

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质谱法分析烘焙对花生过敏原Ara h 1潜在致敏性的影响

Effect of Roasting on the Potential Allergenicity of Peanut Allergen Ara h 1 Evaluated by Mass Spectrometry

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