花生 Ara h 2.01 与各自还原糖的 Maillard 反应及其对 Ara h 2.01 致敏性影响的光谱研究。

IF 3.2 4区 化学 Q2 CHEMISTRY, ANALYTICAL
Luminescence Pub Date : 2024-11-04 DOI:10.1002/bio.70023
Minghao He, Qian Chen, Yuxin Wang, Qianqian Zhu, Hong Xu
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引用次数: 0

摘要

研究了花生 Ara h 2.01 与葡萄糖和木糖的马氏反应对其构象和过敏性的影响。圆二色性(CD)光谱研究表明,单独与还原糖进行短期加热不会改变蛋白质的二级结构,但经过马氏反应后,其二级结构发生了变化,一些 α 螺旋转变为 β 片和无规线圈。荧光光谱研究表明,随着温度的升高,蛋白质在还原糖的诱导下变得疏松和延伸。在较高温度下的长时间热处理会导致蛋白质内部水分子挤出,从而导致蛋白质塌陷,而在马氏反应中进入蛋白质的还原糖会部分阻碍这种挤出。共振光散射(RLS)光谱证实,由于麦拉德反应后木糖分子与蛋白质的相互作用更强,更多的木糖分子进入了蛋白质。酶联免疫吸附试验表明,100°C 的热处理会使一些致敏表位嵌入蛋白质分子内部,因为蛋白质会塌缩,部分表位会在马氏反应后被还原糖覆盖,从而降低其致敏性。此外,由于木糖与蛋白质之间的相互作用更强,因此木糖能更有效地降低蛋白质的致敏性。生物信息分析和分子对接合理地解释了上述所有实验结果。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Spectroscopic Studies on Maillard Reactions of Peanut Ara h 2.01 With Respective Reducing Sugars and Their Impacts on Ara h 2.01 Allergenicity

Spectroscopic Studies on Maillard Reactions of Peanut Ara h 2.01 With Respective Reducing Sugars and Their Impacts on Ara h 2.01 Allergenicity

The effects of the Maillard reactions of peanut Ara h 2.01 with respective glucose and xylose on its conformation and allergenicity were investigated. Circular dichroism (CD) spectral studies showed that short-term heating alone with reducing sugars did not change protein secondary structures, but after undergoing Maillard reactions, its secondary structures changed with some α-helices being transformed into β-sheets and random coils. Fluorescence spectral studies indicated that as temperature increased, protein became loose and extended induced by the reducing sugars. Long heat treatment at higher temperature caused protein collapse with the extrusion of its internal water molecules, which was hindered partially by the reducing sugars that entered the protein in Maillard reaction. Resonance light scattering (RLS) spectra confirmed that more xylose molecules entered protein due to its stronger interaction with the protein after Maillard reactions. ELISA assays exhibited that heat treatment at 100°C led to some allergenic epitopes being embedded inside protein molecules due to protein collapse and that partial epitopes were covered by the reducing sugars after Maillard reaction, resulting in decreases in its allergenicity. Also, xylose reduced the allergenicity of protein more efficiently owing to the stronger interaction between them. All above experimental results were explained reasonably by bioinformatic analysis and molecular docking.

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来源期刊
Luminescence
Luminescence 生物-生化与分子生物学
CiteScore
5.10
自引率
13.80%
发文量
248
审稿时长
3.5 months
期刊介绍: Luminescence provides a forum for the publication of original scientific papers, short communications, technical notes and reviews on fundamental and applied aspects of all forms of luminescence, including bioluminescence, chemiluminescence, electrochemiluminescence, sonoluminescence, triboluminescence, fluorescence, time-resolved fluorescence and phosphorescence. Luminescence publishes papers on assays and analytical methods, instrumentation, mechanistic and synthetic studies, basic biology and chemistry. Luminescence also publishes details of forthcoming meetings, information on new products, and book reviews. A special feature of the Journal is surveys of the recent literature on selected topics in luminescence.
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