糖基化联合磷酸化降低鲢鱼小清蛋白致敏性的机制

以鲢鱼小清蛋白（parvalbumin,PV）为研究对象,采用糖基化联合磷酸化对其进行修饰,运用光谱、质谱和KU812细胞实验等方法研究修饰后鲢鱼PV抗原表位和致敏性的变化。结果表明：糖基化联合磷酸化修饰可增加鲢鱼PV分子质量,降低游离氨基含量,且改变其二级结构和构象结构;糖基化联合磷酸化修饰后的鲢鱼PV含有8个糖基化位点（K33、K46、K55、K65、K84、K88、K97和K108）和1个磷酸化位点（S56）。糖基化联合磷酸化修饰能显著降低鲢鱼PV与IgG/IgE的结合能力,也能降低KU812细胞中组胺和白介素-6的释放能力。因此,糖基化联合磷酸化修饰通过糖基化和磷酸化位点遮掩鲢鱼PV的线性表位和破坏其构象表位,降低其致敏性。研究结果为开发低致敏性鱼类制品提供重要的理论依据。     

大豆过敏原蛋白及致敏性消减技术的研究进展

大豆是我国重要的粮食作物之一,其蛋白质含量高达35%~40%（m/m）。与此同时,大豆蛋白是人们日常生活中最常见的一类食物过敏原,大豆过敏已经成为了急需解决的公共安全问题。β-伴大豆球蛋白（β-Conglycinin,7S）、大豆球蛋白（Glycinin,11S）、Gly m Bd 28K和Gly m Bd 30K（P34）被认为是大豆过敏原中引发机体发生过敏反应的主要成分。迄今为止,国内外对于大豆过敏尚无根治办法,唯一的预防策略是严格避免摄入来防止过敏反应的发生。但研究指出,通过特殊的加工方法或技术手段可以降低大豆过敏原的致敏性,其中以热加工法、超高压法、酶处理法和基因工程法等方法为代表的消减技术得到广泛关注。因此,该文综述了大豆过敏原的类型,常用的过敏蛋白致敏性消减技术及各项技术的优缺点,以期为低敏性大豆食品的开发提供参考。     

Genetic variants of bovine β- and κ-casein result in different immunoglobulin E-binding epitopes after in vitro gastrointestinal digestion

Immunoglobulin E-mediated allergy to cow milk is a common allergy in industrialized countries, mainly affecting young children and infants. β-Casein (CN) and κ-CN belong to the major allergens in cow milk. Within these milk proteins, genetic polymorphisms occur, which are characterized by substitutions or deletions of AA, resulting in different variants for each protein. Until now, these variants have not been considered when discussing the allergenic potential of bovine milk. In this study, the focus was placed on the arising peptide pattern after in vitro gastrointestinal digestion of several β- and κ-CN variants to determine resistant fragments containing IgE-binding epitopes and to identify potential differences between these variants. β-Casein A¹, A², and B, as well as κ-CN A, B, and E, were separated and isolated from milk of cows homozygous for these variants and digested with an in vitro gastrointestinal digestion model. The resulting peptides were identified using mass spectrometry and compared with previously determined epitopes. Seven β-CN and 4 κ-CN peptides, common in all β- or κ-CN variants, remained of sufficient size to harbor IgE-binding epitopes. In addition, some peptides and, consequently, epitopes differ from each other due to the AA substitution occurring in the individual variants. The distinct peptides AA 108 to 129 of β-CN A¹ and A², AA 103 to 123 of β-CN B, as well as AA 59 to 72, AA 59 to 80, and AA 58 to 80 of all 3 β-CN variants correspond to the IgE-binding epitopes AA 107 to 120 and AA 55 to 70, respectively. In κ-CN, the 2 variant-specific peptides AA 136 to 149 (κ-CN A, E) and AA 134 to 150 (κ-CN B) are congruent with the IgE-binding epitope AA 137 to 148. The present study shows that genetic polymorphisms affected the arising peptide pattern of the caseins and thus modifications in the IgE-binding epitopes occurred. As a consequence, the casein variants could show differences in their allergenicity. Studies investigating the allergenic potential of these different peptides are currently in progress.     

虾类过敏原及消减方法研究进展

虾及其制品味道鲜美,营养丰富,但却具有较高的致敏性。本文综述国内外有关虾类主要过敏原——原肌球蛋白的结构、表位预测与定位、变态反应原性检测及脱敏方法等方面的研究进展,为进一步研究虾类过敏原及其消减技术提供一定的参考。     

Conformation affects the potential allergenicity of ovalbumin after heating and glycation

Ovalbumin (OVA), one of the major allergens in hen egg white, and has widespread use in experimental models of allergy. The aim of this research was to assess the effect of glycation and heat treatment on the potential allergenicity of OVA prepared from hen egg white. Secondary and tertiary structures of OVA were also characterised to show the relationship between potential allergenicity and the conformation of OVA after heating and glycation. Glycation significantly reduced the potential allergenicity of OVA tested with egg allergy patients’ sera, which was caused by conformation changes. An increased IgG reactivity was measured using rabbit anti-OVA and was supposed to be caused by protein unfolding which exposed hidden epitopes. Heating reduced the potential allergenicity of OVA at the expense of increased IgG reactivity. It is suggested that conformational changes of OVA induced by glycation and controlled heating significantly reduced its potential allergenicity.     

鸡卵类黏蛋白结构与性质研究进展

鸡卵类黏蛋白是鸡蛋中最主要也是过敏原性最强的过敏原蛋白。本文总结该蛋白的结构,包括氨基酸序列、糖基组成、二硫键位置、二级结构以及组成该蛋白的3 个结构域,并描述其理化性质,最后着重分析讨论其过敏原性,特别是其分子结构中二硫键、糖基和结构域等因素与过敏原性之间的内在联系。     

基因工程在降低植物性食品致敏性中应用

该文详细介绍食品过敏源及食品过敏机制,着重介绍基因工程在降低植物性食品致敏性中应用及最新进展。     

常见食物过敏原结构稳定因素与致敏性的关系研究进展

食物过敏原所引发的食品安全问题是目前亟待解决的卫生学问题,而分析过敏原蛋白结构稳定性与致敏性的关系,对于了解食品过敏的机理以及探索消减过敏原致敏性的方法具有十分重要的意义。本文选取几种主要食物过敏原蛋白,探讨维持过敏原蛋白结构稳定性的因素（二硫键、糖基、疏水作用以及氢键）,以及结构稳定与致敏性的关系,为如何消减过敏原致敏性提供一定的理论指导。     

不同热加工方式对核桃蛋白致敏性的影响

近年来,由核桃等坚果引起的食物过敏的发生率逐渐升高,并且该类过敏常伴随着严重的临床症状。不同 的加工方式能够改变核桃过敏原蛋白（如Jug r 1）的物理化学性质,从而影响其致敏性。本研究采用5 种不同的热处 理方式对核桃蛋白粗提取物进行处理,比较不同热处理方式对核桃蛋白质量浓度及抗原性的影响,从而分析不同热加 工方式对核桃蛋白致敏性的影响。结果显示,不同的热处理方式对核桃蛋白质量浓度和抗原性的影响不同,其中湿热、 高温高压的热处理方式能够有效降低核桃蛋白的质量浓度和抗原性,且高温高压处理效果更显著（P＜0.05）,而微波 处理能在一定程度上增加核桃蛋白的质量浓度和抗原性。本研究结果为进一步研发低致敏性核桃制品提供了科学依据。     

Review of conventional and novel food processing methods on food allergens

With the turn of this century, novel food processing techniques have become commercially very important because of their profound advantages over the traditional methods. These novel processing methods tend to preserve the characteristic properties of food including their organoleptic and nutritional qualities better when compared with the conventional food processing methods. During the same period of time, there is a clear rise in the populations suffering from food allergies, especially infants and children. Though, this fact is widely attributed to the changing livelihood of population in both developed and developing nations and to the introduction of new food habits with advent of novel foods and new processing techniques, their complete role is still uncertain. Under the circumstance, it is very important to understand the structural changes in the protein as food is processed to comprehend whether the specific processing technique (conventional and novel) is increasing or mitigating the allergenicity. Various modern means are now being employed to understand the conformational changes in the protein which can affect the allergenicity. In this review, the processing effects on protein structure and allergenicity are discussed along with the insinuations of recent studies and techniques for establishing a platform to investigate future pathway to reduce or eliminate allergenicity in the population.