Food Allergens: Is There a Correlation between Stability to Digestion and Allergenicity?

Food allergy is a major health problem in the Western countries, affecting 3–8% of the population. It has not yet been established what makes a dietary protein a food allergen. Several characteristics have been proposed to be shared by food allergens. One of these is resistance to digestion. This paper reviews data from digestibility studies on purified food allergens and evaluates the predictive value of digestibility tests on the allergenic potential. We point out that food allergens do not necessarily resist digestion. We discuss how the choice of in vitro digestibility assay condition and the method used for detection of residual intact protein as well as fragments hereof may greatly influence the outcome as well as the interpretation of results. The finding that digests from food allergens may retain allergenicity, stresses the importance of using immunological assays for evaluating the allergenic potential of food allergen digestion products. Studies assessing the allergenicity of digestion products, by either IgE-binding, elicitation or sensitizing capacity, shows that digestion may abolish, decrease, have no effect, or even increase the allergenicity of food allergens. Therefore, the predictive value of the pepsin resistance test for assessing the allergenic potential of novel proteins can be questioned.     

Why are some proteins allergenic? Implications for biotechnology

In recent years, a number of agricultural crops have been developed with recombinant DNA technology. Because the transferred genes code for proteins that are ordinarily not present in these particular foods, there is concern about the potential allergenicity of these new crop varieties. Foods contain many proteins; however, only a small fraction are allergens. Although the structural properties of proteins that cause allergic reactions have not been characterized completely, known food allergens in general have molecular weights between 10 and 70 kDa, stimulate the immune response (induce the production of allergen‐specific IgE), and are stable molecules that are resistant to processing, cooking, and digestion. Although any type of food is potentially allergenic, the majority of food allergies are caused by a small group of foods (cows’ milk, nuts, legumes, eggs, seafood). Cross‐reactivities occur within a given food group and between foods and seemingly unrelated proteins.

Even though most transgenic foods are considered safe, biotechnological manipulation can affect crop allergenicity. The safety evaluation of transgenic foods is relatively easy when the allergenicity of the gene sources are known. The recombinant food can be assayed using traditional in vitro inhibition assays. Recently, reduced allergen content of biotechnologically altered rice was shown. In contrast, increased allergenicity was demonstrated in transgenic soybeans after a methionine‐ and cystine‐rich protein from Brazil nuts, identified as a major Brazil nut allergen, was expressed in soybean to increase its content of sulfur‐rich amino acids. The most difficult issue regarding transgenic food allergenicity is the effect of transfer of proteins of unknown allergenicity. The challenge is to determine whether these proteins are allergenic as there is no generally accepted, established, definitive procedure to define or predict a protein's allergenicity. Comparing the structures of the transferred protein with known allergens and allergen epitopes could be one approach. Additionally, Th‐2 cell stimulation, the production of IL‐4, and IgE antibody induction in animal models may help to evaluate the potential allergenicity of a protein.

In conclusion, there is no evidence that recombinant proteins in newly developed foods are more allergenic than traditional proteins. The evidence suggests that the vast majority of these proteins will be completely safe for the consumer. The concern is that if a few transgenic foods cause serious allergic reactions, this could undermine the public's confidence in such products. It is essential that proper guidelines are established and tests are developed to assure that this will not occur.     

低致敏食品制备技术及其工业化应用研究进展

食物过敏是联合国粮农组织和世界卫生组织认定的全球性食品安全问题之一。在食品加工多元化的背景下,食物过敏患者要完全避免过敏原十分困难,研发低致敏食品对食物过敏患者的安全膳食至关重要。总结了低致敏食品制备技术的加工技术原理;以蒸煮、微波和烘烤为主的热加工技术通过加热诱导蛋白质变性的方式破坏致敏性构象性表位;高压、脉冲电场、脉冲光、低温等离子体、辐照和超声等非热加工技术可以通过过敏原蛋白结构修饰、多肽链断裂、新化学键的产生等方式直接破坏致敏性表位;酶水解、酶交联、糖基化、微生物发酵等其他加工方法则通过改变蛋白质构象或将蛋白质与糖类物质结合,破坏或隐藏过敏原致敏性表位。另外,对工业化低致敏蛋白配料的加工方法和生产现状进行了阐述分析。基于酶法水解的部分水解乳蛋白和深度水解乳蛋白已经可以工业化生产,其他消减食物致敏性的方法以及其他低致敏蛋白配料值得进一步研究。希望可以为工业化生产低致敏食品提供参考。     

食品过敏原检测与评价技术研究进展

过敏原生物活性包括过敏原性即引起致敏个体发生过敏症的活性和致敏原性即引起人群致敏的危险性两个方面。随着转基因作物及相应食品的大量出现，评价和检测食品过敏原生物活性日益受到重视。迄今，食品过敏原性的主要检测方法有：皮肤试验、双盲安慰剂对照激发试验、血清IgE检测和组胺释放试验等；对食品致敏原性还没有建立可靠的评价和监测技术，FAO/WHO采纳的分级评价策略包括血清学测定、过敏原分子结构和序列同源性比较及胃肠液消化稳定性评价等。本文对食品过敏原生物学活性的评价与检测技术研究进展进行综述。     

Development of a Biological Assay to Determine the Allergenic Potential of Foods

Food allergies represent a risk for many people in industrialized countries. Unrecognizable allergenic proteins of foodstuffs may be present as ingredients that are not labeled or as unknown cross-contamination. Such hidden allergens can cause severe reactions in allergics, even at minute quantities, sometimes with fatal outcome. For the verification of the presence of allergenic food constituents, analytical methods such as ELISA and PCR have been developed. However, these tests cannot measure allergenic potential. For this reason, a test system that measures the biological activity of allergens has been developed. It is based on the cellular mechanisms of the type I allergy. Rat basophilic leukemia cells (RBL-2H3) were transfected with the genes of the human high affinity receptor for IgE. The resulting cell line expressed the human receptor α-chain and could bind allergenspecific IgE from allergic subjects, in contrast to the parent cell line. After cross-linking of receptor-bound, allergen-specific human IgE by allergens, the cells released measurable inflammatory mediators. These cells were used for the analysis of a variety of allergen extracts, including extracts prepared from foods containing allergenic hazelnut and peanut. The comparative validation with existing ELISA and PCR for hazelnut and peanut demonstrated similar sensitivity and specificity. The established cell line will be a novel tool in the detection of allergens in complex mixtures, especially to address the issue of their allergenic potential, which cannot be accomplished by classical analytical methods. This will add valuable information about the allergenic potential of food constituents to the risk assessment of foods.     

甲壳类水产品过敏原及其致敏性消减技术研究进展

甲壳类水产品味道鲜美,营养丰富,广受消费者喜爱,但可诱发机体产生严重过敏反应,甚至危及生命,已成为全球范围内日益严重的食品安全问题。概述了目前已鉴定的甲壳类水产品过敏原的结构和免疫性质,及其致敏性消减技术原理和研究进展;已报道的甲壳类水产品过敏原有原肌球蛋白、精氨酸激酶、肌质钙结合蛋白、肌球蛋白轻链、磷酸丙糖异构酶和血蓝蛋白等,其中原肌球蛋白为甲壳类水产品的主要过敏原,可与72%~98%的甲壳类食品过敏患者血清产生特异性IgE反应。利用物理加工消减甲壳类水产品过敏原致敏性,主要通过传统热处理、微波、超高压、低温等离子体和辐照等物理作用力诱导蛋白质变性,进而破坏蛋白质的致敏性表位;酸处理和糖基化等化学修饰消减技术可以通过改变过敏原结构、形成新化学键等方式掩盖或直接破坏致敏性表位;酶处理和发酵处理等生物修饰消减技术则直接降解过敏原致敏性表位。未来仍需要通过过敏表位的靶向消减、多种消减技术协同、动物与人体试验开展,探究过敏原结构和表位修饰的影响机制,推进过敏原消减技术的实际应用,为低敏甚至脱敏甲壳类食品的研发提供参考。     

Characterization of plant food allergens: An overview on physicochemical and immunological techniques

Allergy to plant‐derived foods is a highly complex disorder with clinical manifestations ranging from mild oral, gastrointestinal, and cutaneous symptoms to life‐threatening systemic conditions. This heterogeneity in clinical manifestations has been attributed to different properties of allergenic molecules. Based on this fact, symptom elicitors were grouped into class I and pollinosis‐associated class II food allergens, but clear distinction is rather ambiguous. Moreover, mechanisms underlying food sensitization are not fully understood yet, and food allergy management most often relies on patient's compliance to avoid suspected foods. Therefore, recent efforts aim at the investigation of plant food allergies at the molecular level. This review provides an overview on currently available techniques for allergen characterization and discusses their application for investigation of plant food allergens. Data obtained by an array of physicochemical analyses, such as allergen structure, integrity, aggregation, and stability, need to be linked to results from immunological methods at the level of IgE and T‐cell reactivity. Such knowledge allows the development of computational algorithms to predict allergenicity of novel foods being introduced by biotechnological industry. Furthermore, molecular characterization is an indispensable tool for molecule‐based diagnosis and future development of safer patient‐tailored specific immunotherapy in plant food allergy.     

Advanced DNA- and Protein-based Methods for the Detection and Investigation of Food Allergens

Currently, food allergies are an important health concern worldwide. The presence of undeclared allergenic ingredients or the presence of traces of allergens due to contamination during food processing poses a great health risk to sensitized individuals. Therefore, reliable analytical methods are required to detect and identify allergenic ingredients in food products. The present review addresses the recent developments regarding the application of DNA- and protein-based methods for the detection of allergenic ingredients in foods. The fitness-for-purpose of reviewed methodology will be discussed, and future trends will be highlighted. Special attention will be given to the evaluation of the potential of newly developed and promising technologies that can improve the detection and identification of allergenic ingredients in foods, such as the use of biosensors and/or nanomaterials to improve detection limits, specificity, ease of use, or to reduce the time of analysis. Such rapid food allergen test methods are required to facilitate the reliable detection of allergenic ingredients by control laboratories, to give the food industry the means to easily determine whether its product has been subjected to cross-contamination and, simultaneously, to identify how and when this cross-contamination occurred.     

Food allergy—towards predictive testing for novel foods

The risks associated with IgE-mediated food allergy highlight the need for methods to screen for potential food allergens. Clinical and immunological tests are available for the diagnosis of food allergy to known food allergens, but this does not extend to the evaluation, or prediction of allergenicity in novel foods. This category includes foods produced using novel processes, genetically modified (GM) foods, and foods that might be used as alternatives to traditional foods. Through the collation and analysis of the protein sequences of known allergens and their epitopes, it is possible to identify related groups which correlate with observed clinical cross-reactivities. 3-D modelling extends the use of sequence data and can be used to display eptiopes on the surface of a molecule. Experimental models support sequence analysis and 3-D modelling. Observed crossreactivities can be examined by Western blots prepared from native 2-D gels of a whole food preparation (e.g. hazelnut, peanut), and common proteins identified. IgEs to novel proteins can be raised in Brown Norway rat (a high IgE responder strain), and the proteins tested in simulated digest to determine epitope stability. Using the CSL serum bank, epitope binding can be examined through the ability of an allergen to cross-link the high affinity IgE receptor and thereby release mediators using in vitro cell-based models. This range of methods, in combination with data mining, provides a variety of screening options for testing the potential of a novel food to be allergenic, which does not involve prior exposure to the consumer.     

Considerations on Developing Criteria to Determine Whether a Food Allergen is of Public Health Importance

Food allergy is the result of a particular type of immune response against one or more food components, usually proteins. The food allergy reactions that are the focus of regulatory measures are mediated by antibodies of the IgE class. Importantly, food allergy is a two-step process. The first step, the sensitisation phase, consists of an immune response resulting in production of IgE antibodies specific for the allergen. The second step, the provocation phase, is the triggering of a symptomatic allergic reaction as a result of exposure to the allergen after sensitisation has been established. For reasons not well understood, a majority of sensitised individuals never will experience clinical reactions. Determining the number of sensitised individuals (test positives) in a population will therefore grossly overestimate the prevalence of food allergy. The term ‘allergy’ should be used only if clinical reactions occur. For triggering a food allergic reaction in a sensitised individual, only the ‘acute’ food intake and not the intake over time is of importance, and food allergy in this aspect resembles acute poisoning. Because of the cultural, agricultural, economic and nutritional importance of the foods, society accepts that a small fraction of the population develops allergies to traditional food products. Prevention of allergic reactions is then sought by means of education and by labelling of the most important allergenic foods. However, some 200 allergenic foods have been described, but only a small minority of these appears to be of importance in terms of frequency and severity of reactions triggered in the population. When it comes to management of the allergens, however, there is a lack of clear criteria at two levels: at the level of defining what documentation should be required to enter a proposed new food allergen into one of the large allergen databases, as well as at the level of determining which food allergens are of sufficient public health importance to require special regulatory attention in terms of labelling. With the aim of increasing transparency and predictability of decision-making processes and obtaining more consistency between labelling of different allergens as well as between labelling of allergens in different food regulatory jurisdictions, ILSI Europe has taken an initiative to establish clear criteria and a framework to determine the public health importance of a given food allergen. These criteria will consist of factors relating to food properties, population factors, and exposure factors.     

Cleaning and other control and validation strategies to prevent allergen cross-contact in food-processing operations

Food allergies affect an estimated 10 to 12 million people in the United States. Some of these individuals can develop life-threatening allergic reactions when exposed to allergenic proteins. At present, the only successful method to manage food allergies is to avoid foods containing allergens. Consumers with food allergies rely on food labels to disclose the presence of allergenic ingredients. However, undeclared allergens can be inadvertently introduced into a food via cross-contact during manufacturing. Although allergen removal through cleaning of shared equipment or processing lines has been identified as one of the critical points for effective allergen control, there is little published information on the effectiveness of cleaning procedures for removing allergenic materials from processing equipment. There also is no consensus on how to validate or verify the efficacy of cleaning procedures. The objectives of this review were (i) to study the incidence and cause of allergen cross-contact, (ii) to assess the science upon which the cleaning of food contact surfaces is based, (iii) to identify best practices for cleaning allergenic foods from food contact surfaces in wet and dry manufacturing environments, and (iv) to present best practices for validating and verifying the efficacy of allergen cleaning protocols.     

Effect of roasting history and buffer composition on peanut protein extraction efficiency

Peanut is a major allergenic food. Undeclared peanut (allergens) from mis-formulation or contamination during food processing pose a potential risk for sensitized individuals and must be avoided. Reliable detection and quantification methods for food allergens are necessary in order to ensure compliance with food labelling and to improve consumer protection. The extraction of proteins from allergenic foods and complex food products is an important step in any allergen detection method. In this study, the protein extraction efficiency of various buffers prepared in-house and some extraction buffers included in some commercial allergen enzyme-linked immunosorbent assay (ELISA) test kits for peanut determination in food products were tested. In addition, the effect of roasting history on the extractability of peanut protein was investigated by the biuret and the bicinchoninic acid (BCA) assays. Elevated roasting temperatures in food processing were found to have a major impact on protein extraction efficiency by reducing protein yields of oil and dry roasted peanuts by 50-75% and 75-80%, respectively, compared with the raw material. Extraction buffers operating in the higher pH range (pH 8-11) showed best yields.     

水产品致敏蛋白的研究进展

水产品因营养丰富、味道鲜美而深受消费者喜爱,但水产品也是容易引起食物过敏反应的一类食品。目前, 全球水产品的加工难以满足过敏人群对食用安全性的需求,且针对水产品过敏的治疗,也尚无特效药物。因此,食用水产品能危害潜在过敏人群的健康,降低其生活水平。近年来,随着全球过敏发病率的上升,水产品致敏蛋白的研究已成为全球关注的公共卫生问题之一。本文介绍了水产品中的钙结合蛋白、原肌球蛋白、精氨酸激酶、肌球蛋白轻链、血蓝蛋白等主要致敏蛋白的生化特性及其抗原表位,阐述了基于致敏蛋白及其DNA为基础的酶联免疫吸附法、质谱法、生物传感器法、聚合酶链式反应检测水产品致敏蛋白的方法,同时介绍了利用物理、化学和生物方法消减致敏蛋白致敏性的研究现状,在此基础上提出了水产品致敏蛋白研究和应用中存在的问题及其发展趋势,旨为进一步认识水产品致敏蛋白,开发低致敏或无致敏性水产食品提供参考。     

Review of the development of methodology for evaluating the human allergenic potential of novel proteins

Safety assessment of novel proteins in genetic-engineered foods is a key component of the overall safety evaluation for these products. Since allergens are typically proteins, assessment of the potential allergenicity of the novel proteins in genetically engineered foods is critical. This article reviews methods available to assess the potential allergenicity of novel proteins, as well as problems and deficiencies in the existing methods. The role of bioinformatics and knowledge of allergenic epitopes in developing new approaches to this problem is discussed.     

甜荞麦16 kDa过敏原基因的克隆及其原核表达载体的构建

目的 对甜荞麦(common buckwheat)过敏原的分子生物学开展研究。方法 通过RT-PCR克隆甜荞麦16 kDa过敏原蛋白的全长基因, 并根据序列设计带有酶切位点的特异性引物, 扩增甜荞麦16 kDa过敏原基因的完整开放阅读框, 与pET-28a载体连接, 构建原核表达载体。 结果 本研究成功克隆了甜荞麦16 kDa过敏原蛋白的基因, 且构建了其原核表达载体。该基因含有长度为450 bp的开放阅读框, 编码149个氨基酸, 在GenBank数据库中的登录号为EU883600, 同源性分析发现其与数据库中已知的荞麦过敏原基因有高度的同源性。结论 本研究为甜荞麦16 kDa过敏原蛋白的重组表达和临床过敏性疾病的诊断奠定了基础。     

Immunogenic and allergenic potentials of natural and recombinant innocuous proteins

A new aspect of protein immunogenic and allergenic properties has become important recently, when there is a higher chance that our immune system will be exposed to novel protein antigens and/or familiar protein antigens with an unprecedented high frequency and large amount. These proteins are innocuous, nontoxic, and noninvasive by themselves, and include various natural proteins from the environment and recombinant proteins from industry. The technical term allergenic has been used for such proteins and their abilities to induce specific IgE production and to cross-link IgE/Fc epsilonRI on the surface of mast cells and basophiles have been recognized. As for the environmental proteins, some physicochemical properties (solubility, stability, and permeability across a mucosal epithelium) of the proteins indirectly play important roles in their allergenic potential because they do not originate from invasive pathogens as vehicles. Indeed, several lines of experimental evidences have been accumulated indicating that all proteins are absorbed across mucosal epithelia by transcellular transport and/or through interstitial spaces among the epithelial cells but not at equal levels. Some animal models have been established for natural sensitization to some allergenic proteins by feeding or intragastric administration without an adjuvant and, in a few cases, some symptoms resembling human allergy and even anaphylaxis have been induced by oral challenge with the proteins. Sometimes, even to self-proteins, the immunogenic or allergenic potential is given by post-translational modifications and possibly by unknown structural/conformational alterations, when they are exogenous self-proteins, such as recombinant human proteins for drug use. Despite the accumulation of knowledge and the progress in analytical technology on protein allergenicity, it is still crucial to predict the allergenic potential of novel and unused proteins. However, some animal models are applicable for assessing the relative allergenic potential of processed proteins in comparison with that of native proteins in preclinical studies.     

Allergen analysis and authenticity control: Development of mass spectrometry-based methods for animal-derived food products

Food allergy and food fraud involving animal-derived products are two of the most significant issues in food markets. On one hand, immunoglobulin E (IgE)-mediated allergic reactions after ingestion of fish, crustaceans, eggs, or milk are among the most prevalent and can happen even after ingestion of trace amounts. On the other hand, new rules regarding product commercialization (e.g., novel food regulation) are more and more created while fraudulent species substitution in fishery products is very common. Sensitive and accurate analytical methods for allergen quantification and species identification in commercial food products are therefore urgently required whether to help food industries inform allergic consumers, to ensure the food compliance with new regulations or to combat food fraud. In the past few years, bottom-up proteomic techniques, which rely on the detection of peptide biomarkers resulting from a tryptic digest of food proteins using liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS), have been emerging in this field. The selection of reliable allergen-specific or species-specific peptide biomarkers is one of the most crucial steps when developing such methods whether for qualitative protein detection (i.e., screening analysis) or protein absolute quantification. The first part of this dissertation relates therefore to the selection of allergen peptide biomarkers for fish, invertebrates, eggs, and milk in an experimental way using a single chaotropic urea extraction buffer. The allergenic proteins responsible for those severe reactions are mainly parvalbumin, tropomyosin, ovalbumin, and caseins. The protein extraction was first assessed via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the major allergens were well extracted. After that, data-dependent MS/MS spectra which were obtained using digest samples of authentic animals or pure allergenic ingredients were processed against a matching protein database, and identified peptides were filtered according to several criteria such as the sequence length, amino acid composition, specificity, reproducibility, and sensitivity. Myosin proteins were also a target of choice for fish detection due to their high prevalence and sequence homology even if they are non-allergenic. Contrary to fish and invertebrate databases which included entries for only one specific protein (i.e., parvalbumin, myosin, or tropomyosin), egg and milk databases contained all known allergenic proteins or even additional proteins for egg yolk. Two extra selection steps were achieved for egg and milk markers based on more stringent criteria regarding their sensitivity after targeting them in the corresponding allergenic ingredients. At this point, 17, 13, 10, 10 and 12 potential markers were respectively selected for fish, invertebrates, egg white, egg yolk and milk. An alignment algorithm was used for all those markers to get an idea about their biological specificity. The biological specificity was verified experimentally for fish and invertebrate potential markers by targeted analysis in digest samples of animal species that are relevant in the food industry (vertebrates and invertebrates). This verification was not done for egg and milk markers as it was not regarded as significant due to reported cross-reactivity among avian eggs and among mammalian milk. Two potential parvalbumin markers were detected in other nonfish vertebrates, while all potential tropomyosin markers except one were specific to at least an invertebrate class belonging to the same phylum. Parvalbumin and myosin markers as well as tropomyosin markers were exclusively found in vertebrates or invertebrates. Marker detectability was checked by analyzing processed fish products as well as cooked fish for potential parvalbumin and myosin markers, while commercial insect-based food products such as cereals bars or pasta were studied for potential tropomyosin markers. All expected fish and invertebrate markers were detectable in those complex food products. Detectability of egg and milk markers was assessed by analysis of bread, cookies, and chocolate samples contaminated at different stages of the sample preparation with trace amounts (100 pg/g) of eggs and milk (i.e, fortified, spiked, and incurred digest samples). Two egg white markers and seven milk markers were detected in all those samples. The most suitable markers in terms of sensitivity and specificity were finally chosen for each allergenic product. Thus, besides two myosin fish global markers, five parvalbumin markers were retained including at least one of the investigated fish species. In addition, five tropomyosin markers were chosen, their specificity allowing us to distinguish crustacean tropomyosin from that of insects/arachnids, or mollusks. At last, two ovalbumin markers and three casein markers were confirmed to be the most suitable allergen markers respectively for egg white and milk. All those retained markers could be compiled in a single multiplex method. The automation of the sample preparation could also be a promising improvement whether for qualitative or quantitative analysis.     

Analysis of the potential allergenicity of traditional apple cultivars by Multiplex Biochip-Based Immunoassay

Few apple cultivars are widespread in the markets worldwide. The characterisation of cultivars available only in local markets could reveal fruits with sufficiently low amounts of allergens to be tolerated by at least some allergic subjects. This study was focused on the characterisation of 10 ancient and 2 widespread apple cultivars cultivated in Southern Italy. Pomological characterisation showed good sensory features and high manipulation resistance for most of the selected ancient cultivars. Individual patterns of allergenic components were obtained when IgE, IgG and IgG4 inhibition tests were performed on a multiplexed allergen microarray, using sera from allergic subjects as probes. Results obtained allow the selection of potentially hypo- or hyper-allergenic apple cultivars. In addition, this study describes a possible use of allergen microarray technology to quickly investigate the potential allergenicity of specific foods that, after additional tests, can be considered for the inclusion in the diet of individual allergic subjects.     

New opportunities and perspectives of high pressure treatment to improve health and safety attributes of foods. A review

High pressure (HP) treatment has emerged as a novel, additive-free food preservation technology. It has been scientifically and commercially proven that HP can produce microbially safe and stable products with improved quality characteristics such as enhanced flavor and color. Recent studies have focused on the effects of HP on health attributes and allergenic potential of foodstuff to develop the next generation of convenience foods. This review provides an overview on the current knowledge of HP treatment to improve the extraction and bioavailability of bioactive compounds, to reduce allergenicity, to retain essential fatty acids, to reduce the salt content, and to reduce formation of processing contaminants. HP has shown encouraging potential to manipulate the functionality, extractability, allergenicity and bioavailability of micronutrients and components in a diverse variety of foods. However, the underlying principles and mechanisms are not yet fully understood and warrant further investigation. More studies are needed to optimize HP treatment conditions and develop a mechanistic understanding of the impacts of HP on different bioactive compounds in food products with health benefits. This can open the doors to new HP applications in the food industry.     

Effects of daily food processing on allergenicity

Daily food processing has the potential to alter the allergenicity of foods due to modification of the physico-chemical properties of proteins. The degree of such modifications depends on factors such as processing conditions, type of food considered, allergenic content, etc. The impact of daily food processing like boiling, roasting, frying or baking on food allergenicity have been extensively studied. The influence of other thermal treatments such as microwave heating or pressure cooking on allergenicity has also been analyzed. Non-thermal treatment such as peeling impacts on the allergenic content of certain foods such as fruits. In this review, we give an updated overview of the effects of daily processing treatments on the allergenicity of a wide variety of foods. The different variables that contribute to the modification of food allergenicity due to processing are also reviewed and discussed.