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Introduction: Prior to the introduction of novel food ingredients into the food supply, safety risk assessments are required, and numerous prediction models have been developed and validated to evaluate safety. Methods: The allergenic risk potential of Helaina recombinant human lactoferrin (rhLF, Effera™), produced in Komagataella phaffii (K. phaffii) was assessed by literature search, bioinformatics sequence comparisons to known allergens, glycan allergenicity assessment, and a simulated pepsin digestion model. Results: The literature search identified no allergenic risk for Helaina rhLF, K. phaffii, or its glycans. Bioinformatics search strategies showed no significant risk for cross-reactivity or allergenicity between rhLF or the 36 residual host proteins and known human allergens. Helaina rhLF was also rapidly digested in simulated gastric fluid and its digestibility profile was comparable to human milk lactoferrin (hmLF), further demonstrating a low allergenic risk and similarity to the hmLF protein. Conclusion: Collectively, these results demonstrate a low allergenic risk potential of Helaina rhLF and do not indicate the need for further clinical testing or serum IgE binding to evaluate Helaina rhLF for risk of food allergy prior to introduction into the food supply. [ABSTRACT FROM AUTHOR]

Ovalbumin (OVA) is the most abundant protein in egg white, with excellent functional properties (e.g., gelling, foaming, emulsifying properties). Nevertheless, OVA has strong allergenicity, which is usually mediated by specific IgE thus results in gut microbiota dysbiosis and causes atopic dermatitis, asthma, and other inflammation actions. Processing technologies and the interactions with other active ingredients can influence the functional properties and allergic epitopes of OVA. This review focuses on the non-thermal processing technologies effects on the functional properties and allergenicity of OVA. Moreover, the research advance about immunomodulatory mechanisms of OVA-mediated food allergy and the role of gut microbiota in OVA allergy was summarized. Finally, the interactions between OVA and active ingredients (such as polyphenols and polysaccharides) and OVA-based delivery systems construction are summarized. Compared with traditional thermal processing technologies, novel non-thermal processing techniques have less damage to OVA nutritional value, which also improve OVA properties. OVA can interact with various active ingredients by covalent and non-covalent interactions during processing, which can alter the structure or allergic epitopes to affect OVA/active components properties. The interactions can promote OVA-based delivery systems construction, such as emulsions, hydrogels, microencapsulation, nanoparticles to encapsulate bioactive components and monitor freshness for improving foods quality and safety. [ABSTRACT FROM AUTHOR]

The β′-component, a major allergen found in fish roe, is synthesized in the liver of female fish as part of the precursor of the egg yolk protein vitellogenin (Vg). Vg is distributed through the bloodstream and contributes to ovary development. In the present study, β′-component, present in Vg fragments, was detected in the muscles and internal organs of mature female salmon, with concentrations exceeding the recommended labeling level under Japan's food allergy labeling system. Additionally, total protein extracted from tissues of female salmon reacted with immunoglobulin E antibody against the salmon roe β′-component. No β′-component was detected in the tissues of mature male fish in the absence of sex hormone stimulation from females nor in immature salmon without sexual differentiation, but excess stimulation of the female sex hormone induced Vg synthesis containing the β′-component in the male fish. These findings suggest that taking into account fish sex, maturity, and sexual isolation of mature male fish could improve the safety of salmon meat for individuals with salmon roe allergy. [ABSTRACT FROM AUTHOR]

AbstractThe food matrix is a complex system encompassing all constituent elements in food production. It influences the digestibility of these elements through direct interactions and affects the digestive environment. Furthermore, the gastrointestinal system possesses precise mechanisms that efficiently process dietary components into essential nutrients, effectively preventing the onset of abnormal immune responses or dysfunctional host reactions in most instances. However, the incidence of adverse food reactions is constantly increasing, and evidence indicates that this process is environmental. Adverse reactions can be categorized as toxic or nontoxic. Toxic reactions are dose-dependent and can result from natural compounds, processing-induced substances, or contaminants. Nontoxic reactions like food intolerance and hypersensitivity depend on individual susceptibility and evoke specific pathological and physiological responses. This review aims to elucidate the mechanisms underlying the occurrence of immune- (food allergies and sensitivities) and non-immune-mediated (food intolerance) reactions, emphasizing the fundamental distinctions between these two categories. Enhanced comprehension and distinction of these mechanisms will significantly contribute to advancing preventive and therapeutic approaches and establishing guidelines for food labeling concerning immune-mediated reactions. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Food Safety & Quality is the property of Journal of Food Safety & Quality Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

BACKGROUND: The interaction between food allergens and plant polyphenols has become a safe and effective management strategy to prevent food allergies. Ovalbumin (OVA) is the most abundant allergen in egg whites. Resveratrol (RES) is a plant polyphenol that is abundant in red grapes, berries, and peanuts, and has an anti‐allergic effect on allergy‐related immune cells. However, there is little information about the effect of RES on the allergenicity of OVA. In this study, the effect of RES on the allergenicity of OVA was investigated. RESULTS: Molecular docking and spectroscopic studies indicated that the addition of RES changed the structure of OVA. The digestion and transfer rate of OVA–RES were effectively improved with an in vitro gastrointestinal digestion model and Caco‐2 cell model, especially when the molar ratio of OVA–RES was 1:20. Meanwhile, the KU812 cell degranulation assay proved that the potential allergenicity was remarkably decreased while the molar ratios of OVA–RES were increased to 1:20. Furthermore, hydrogen bonds and van der Waals forces were the dominating forces to stabilize the OVA–RES complexes. CONCLUSION: All the findings demonstrated that the potential allergenicity of OVA was reduced when interacting with RES, and RES can be a potential food material for preparing a hypoallergenic protein, especially for egg allergy. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Summary: The production and use of kiwifruit, and their derived products, has seen rapid growth in the food industry with some 4 467 099 tonnes produced in 2021. A key area of development has been the increased use of kiwifruit waste streams to support sustainable food production systems. However, kiwifruit is emerging as a common elicitor of food allergy worldwide. Therefore, the present research focuses on summarising the current literature on kiwifruit‐induced human food allergy. Of the available information, a total of 7098 titles were found and 107 articles were included in the current study following full‐text screening. Most research concentrated on the prevalence of allergenicity and was performed within Europe, North America, Asia, Africa, South America and Oceania. Food allergy to kiwifruit ranged from oral allergy syndrome to anaphylaxis in humans. Few studies considered the need for labelling or public education. Given the increased usage of kiwifruit across a range of food streams, further research is required due to the greater focus on utilisation of these products in the food industry. [ABSTRACT FROM AUTHOR]

Shrimp is a common cause of food allergies in allergic individuals. The management of patients suffering from shrimp allergy relies on avoidance of the specific food, which compromises nutritional requirements. In this study, fermentation was performed using Lactobacillus to reduce the allergenicity of Litopenaeus vannamei. The optimal fermentation conditions using Lactobacillus helveticus TS6024 were 1% glucose, 30% minced shrimp, 2.5% inoculum level, 3% NaCl, and 60 h of incubation at 37°C, whereas those using Lactobacillus acidophilus 6005 were 2% glucose, 20% minced shrimp, 15% inoculum level, 2% NaCl, and 48 h of incubation at 42°C. Under optimal conditions, Lactobacillus helveticus TS6024 and Lactobacillus acidophilus 6005 fermentation reduced the allergenicity of shrimp by 78.97% and 70.09%, respectively. SDS-PAGE analysis showed that the band intensity of tropomyosin (36KDa) reduced evidently after the selected Lactobacillus fermentation. The hypoallergenic shrimp/shrimp products will provide optimal nutrition with reduced risk of adverse reactions in hypersensitive individuals. [ABSTRACT FROM AUTHOR]

Purpose of Review: The globally rising food allergy prevalence is associated with the urgent need for new disease prevention methods, efficient treatment, and reliable risk assessment methods for characterization of food allergens. Due to inter-individual variations in the digestive system, food allergens are degraded to a different extent in each person. Food processing also influences allergen digestion. Recent Findings: In this review, we provide an overview of the digestive system with focus on relevance for food allergy. Main food proteins causing allergic reactions are evaluated, and the combined role of food processing and digestion for allergen stability is highlighted. Finally, clinical implications of this knowledge are discussed. Summary: Recent literature shows that allergen digestibility is dependent on food processing, digestive conditions, and food matrix. Digestion affects proteins allergenicity. It is currently not possible to predict the immunogenicity of allergens solely based on protein stability. [ABSTRACT FROM AUTHOR]

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Shellfish is widely consumed globally, one of the main reasons is because it contains good nutrition for health. The increased consumption also leads to adverse health problems such as food allergy. Food allergy is hypersensitivity reaction of the immune system caused by consumption or exposure to food. Various food processing methods has been proven to alter shellfish allergenicity with different effectiveness. This study aims to determine the most effective processing method to reduce shellfish allergenicity through meta-analysis. In total of 19 articles were obtained using PRISMA diagram, with publication year range 2006-2020. Data were analyzed to determine Standardized Mean Difference (SMD) with 95% confidence interval. Moist heating, high hydrostatic pressure, irradiation, and ultrasound processing have significant effect (p < 0,05) in reducing shellfish allergenicity. Meanwhile, boiling and roasting processing did not have a significant effect. Based on the results of the metaanalysis, high hydrostatic pressure is the most effective method in reducing shellfish allergenicity because it has the highest effect size value with -7,25 (95% CI: -9,11 s.d. -5,4; p < 0,00001). [ABSTRACT FROM AUTHOR]

Objective: Bioinformatics analyses have been becoming important research tools in the field of life science since 2000. New tools have been developed for the detection of allergens in food sources. This study investigated potential allergen proteins similar to the endochitinase class 1(Pers a 1) protein found in avocado using bioinformatics analysis tools. Materials and Methods: The potential allergens were examined with four different in silico tools: Clustal W for multiple sequence comparison, Swiss-MODEL for homology modeling, ProtParam for comparing protein parameters, and AlgPred for allergen prediction. Results: In silico analyses revealed high rates of similarities in protein sequences among the studied species. The highest percent identity was found in Cinnamomum micranthum f. kanehirae as 97.55 while the lowest percent identity was found in Diospyros kaki as 70.23. It is very important to note that 9 of the 10 potential allergen species investigated are plats consumed in daily life and these species were identified as allergens. According to the algorithm of BLAST search on allergen representative peptides (ARPs), ARPs were found in eight potential allergen proteins except for Prunus avium and Citrus unshiu. The ARP sequence related to Persea americana is LQLTWNYNYGAAGNSIGFNGLSNP. Conclusion: People who are allergic to avocado (Persea americana) may be advised to be careful while consuming foods such as Phoenix dactylifera, Allium sativum, Citrus unshiu, Diospyros kaki, and Spinacia oleracea. The present paper can be considered as a model study for understanding allergens in foods by using in silico tools. [ABSTRACT FROM AUTHOR]

To evaluate the safety of Terasi (Indonesian fermented shrimp paste), the product characteristics and allergenicity of 20 types of Indonesian commercial Terasi (ICT) that meet the Indonesian National Standard were evaluated, with a focus on the major shrimp allergen tropomyosin (TM). Marked protein hydrolysis of shrimp muscle occurred in all ICT samples, and no protein fragments or specific reaction of anti-TM immunoglobulin (Ig)G were observed in SDS-PAGE or immunoblot assays. In a competitive enzyme-linked immunosorbent assay using shrimp allergenic patient sera, we observed a markedly diminished specific IgE reaction of ICT compared with that of shrimp muscle, whereas the IgE-binding ability remained in all ICT samples. No clear correlation was found between the degree of protein hydrolysis and IgE reactivity. These results indicate that ICT could be defined as a low–allergenic processed seafood, but has the possibility to be a causative food for shrimp allergy. Direct immunological evaluation is required establishing the food safety of ICT, because assessments of protein profiles and hydrolysis are not useful for determining the safety of Terasi. [ABSTRACT FROM AUTHOR]

The use of seaweed and algal derived products in the food industry has grown rapidly in recent times. Major areas of expansion have been in Western countries where algae derived commodities are being utilised as edible foods or sources of high value ingredients. However, studies focused on potential allergenicity attributed to these food items, prevalence of allergenicity, and public health awareness are limited. Therefore, the current research summarises the existing literature focused on algal induced allergy in humans. Of the available literature, a total of 937 titles were identified, and 33 articles underwent subsequent full-text screening. Most research focused on prevalence and were derived from studies conducted in Europe (58%), North America and Canada (33%), and the remainder Australia and South Korea (9%). No studies addressed the need for public education or labelling of algal products. Our review reports that the available evidence identified points to algal derived products as being potential sources of allergens in the human food chain. Several components have been characterised that are shown to induce allergic responses in humans. Few studies have assessed the prevalence of algal allergenicity in the general population and as such further research is warranted given the increased usage of these products in the food industry. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Food Safety & Quality is the property of Journal of Food Safety & Quality Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The increasing prevalence of food allergies is a significant challenge to global food health and safety. Various strategies have been deployed to decrease the allergenicity of food for preventing and reducing related disorders. Compared to other methods, fermentation has unique advantages in reducing the allergenicity of food and may represent a new trend in preventing food-induced allergies. This review introduces the characteristics of allergens in various foods, including shellfish, soy, peanut, milk, tree nut, egg, wheat, and fish. The mechanism and pathological symptoms of allergic reactions are then summarized. Furthermore, the advantages of fermentation for reducing the allergenicity of these foods and preventing allergies are evaluated. Fermentation is an efficient approach for reducing or eliminating food allergenicity. Simultaneously, it improved the nutritional value and physicochemical properties of food materials. It is conceivable that a combination of mixed strain fermentation with additional processing, such as heat treatment, pulsed light, and ultrasonication, will efficiently reduce the allergenicity of various foods and preserve their unique taste and nutritional components, providing significance for patients with allergies. [ABSTRACT FROM AUTHOR]

The increasing incidence of food allergy cases is a public health problem of global concern. Producing hypoallergenic foods with high quality, low cost, and eco-friendly is a new trend for the food industry in the coming decades. Food irradiation, a non-thermal food processing technology, is a powerful tool to reduce the allergenicity with the above advantages. This review presents a summary of recent studies about food irradiation to reduce the allergenicity of food, including shellfish, soy, peanut, milk, tree nut, egg, wheat and fish. Principles of food irradiation, including mechanisms of allergenicity-reduction, irradiation types and characteristics, are discussed. Specific effects of food irradiation are also evaluated, involving microbial decontamination, improvement or preservation of nutritional value, harmful substances reduction of food products. Furthermore, the advantages, disadvantages and limitations of food irradiation are analyzed. It is concluded that food irradiation is a safety tool to reduce the allergenicity of food effectively, with high nutritional value and long shelf-life, making it a competitive alternative technology to traditional techniques such as heating treatments. Of note, a combination of irradiation with additional processing may be a trend for food irradiation. [ABSTRACT FROM AUTHOR]

Food allergy is a serious public health problem, which is mainly induced by food allergens (mainly allergenic proteins). Ultrasound can change protein structure, suggesting its potential to decrease food allergenicity. The review concluded the mechanism and influence factors of ultrasound to reduce food allergenicity. The effects of ultrasound alone on some major allergenic foods such as tree nuts, shellfish, fish, egg, soy, milk, and wheat were also discussed. Moreover, ultrasound pre- and post-treatments were combined with heating, glycation, germination, hydrolysis, fermentation, irradiation and polyphenol treatment for reducing food allergenicity were also evaluated. It was found that ultrasound induced structural changes even degradation of protein to reduce the allergenicity mainly due to cavitation effects. The reduction of allergenicity through ultrasound alone was affected by ultrasound power, time, frequency and food types, while, apart from these factors, it was affected by ultrasound order and the assisted technologies conditions during ultrasound-assisted technologies. Compared to ultrasound alone treatment, the ultrasound-assisted technology exhibited high efficiency of allergenicity reduction because ultrasound treatment caused protein unfolding to accelerate allergen modification of the assisted technologies for masking and disrupting more epitopes. Thus, ultrasound treatment, especially ultrasound-assisted technologies under appropriate conditions, was promising for producing hypoallergenic foods. • Ultrasound alone mainly alters protein structure to reduce food allergenicity. • Ultrasound assisted technologies is promising to reduce food allergenicity. • The efficiency of allergenicity reduction is affected by many factors. • Clinical experiments should be carried out to confirm the hypoallergenic results. [ABSTRACT FROM AUTHOR]

Reducing the allergenicity of edible insects is crucial for the comprehensive utilization of insect resources. Phospholipase A2 (PLA2) exists in various edible insects and mammalian tissues, which can cause serious allergic reactions. Herein, we constructed a magnetic nanocomposite with photo/chemical synergistic capability to mitigate the allergenicity of PLA2. The formation of prepared nanocomposite was systematically confirmed using various techniques. The nanocomposite exhibited uniform diameters, abundant functional groups, excellent magnetic capabilities. An effective photo/chemical method was established to reduce the allergenicity of PLA2 in vitro. The feasibility of the method was demonstrated through circular dichroism, fluorescence spectrum and IgE-binding analysis. The allergenicity and IgE-binding effect of PLA2 were significantly reduced due to conformational changes after nanomaterial treatment. These results demonstrate the sensitivity and effectiveness a strategy for reducing PLA2 allergenicity, providing a basis for development of nanomaterials to reduce the risk of novel food allergies in response to edible insect products. [Display omitted] • A novel nanocomposite was fabricated to photo/chemical mitigate PLA2 allergenicity. • The nanocomposite had a metal-polyphenol network with magnetic-photothermal properties. • The nanocomposite reduced allergenicity by altering PLA2 conformation. [ABSTRACT FROM AUTHOR]

Tropomyosin (TM) is the main allergen of Macrobrachium nipponense. Recombinant allergens have great prospects in the detection, diagnosis, and treatment of food allergens. The purpose of this study was to compare the differences in structure and allergenicity between natural TM and recombinant TM. Recombinant TM of M. nipponense with a molecular weight of 38 kDa was successfully expressed in the Escherichia coli system. The amino acid sequence as well as secondary structure between natural and recombinant TM were similar, which were verified by mass and CD spectrometry, respectively. Studies showed that both natural TM and recombinant TM had strong allergenicity, and recombinant TM was more allergenic, which could be used as a substitute for natural TM in the diagnosis and treatment of shrimp allergy. This study provided stable and reliable allergen components for the detection of crustacean allergens and the diagnosis and treatment of food allergies caused by crustacean allergens. [Display omitted] • Recombinant TM was induced and expressed by Escherichia coli expression system. • The characteristics of natural and recombinant TM were highly similar. • Recombinant TM was more allergenic compared with natural TM. • Recombinant TM could be used as a substitute for natural TM. [ABSTRACT FROM AUTHOR]

Allergen modification is a novel strategy for preventing and treating food allergy. Resveratrol (RES) can be used as a modifying ligand for allergens, but the interaction mechanism between RES and allergens is still not detailed, and the ramifications of this interaction on the structure, epitope and allergenicity of allergens are also lacking a clear explanation. In addition, the application of heat can promote protein structure to unfold and expose more binding sites to facilitate interaction. Therefore, in this study, ovalbumin (OVA) was selected as the allergen model and was heated to expose more binding sites. The effects of the interaction between RES and heat-stressed ovalbumin (HOVA) on allergen structure, epitope and allergenicity were investigated by combining routine experimental analysis and computer simulation. Results showed heat stress at 323 K for 15 min could better unfold the molecular structure of OVA. On this basis, the interaction between RES and OVA was strengthened, which showed a static quenching of the ground state complex with binding affinity of 1.25 × 106 L/mol. The binding of RES induced the variation of protein microenvironment, and the overall structure tended to disordered direction. Computer simulation had shown RES could directly act on the IgE epitope region (AA251-260) of the OVA. The allergenicity evaluation experiment further indicated the combination of RES alleviated the IgE binding capacity of HOVA. These findings are helpful to further study the mechanism of RES ligand modification to change food allergy. • Heat at 323 K for 15 min can better expose internal hydrophobic groups of OVA. • The interaction between RES and OVA was strengthed with the application of heat. • RES changed the microenvironment and structural composition of HOVA. • Molecular docking indicated RES interfered with the IgE epitope regions of OVA. • MD simulations can be used as an effective tool to predict bimolecular interaction. [ABSTRACT FROM AUTHOR]

Food allergies represent one of the most rapidly increasing and significant human challenges connected with global health. Soybean has high protein and fat quality; however, it is responsible for allergenicity in humans. Despite this, the requirement for protein will increase by 110% in 2050. Traditional methods such as heat treatments (boiling, roasting) are usually exploited to decrease food allergenicity, but they produce modifications in food quality (color, smell, flavor, and texture) due to high temperatures. Consequently, new potential approaches for reducing soybean allergenicity are described in this review, divided into two categories. The first is related to pressure techniques, such as extrusion, high hydrostatic pressure (HHP), high-pressure homogenization (HPH), and controlled instantaneous pressure drop (DIC). The second is related to waves: gamma irradiation (γ-irradiation), pulsed ultraviolet light (PUV), cold plasma, microwave, and ultrasonication. These techniques have the same common goal: lowering soybean allergenicity of the products with an impact on protein structure. The review found that physical treatments have better profiles on the food nutritional characteristics and sensory properties, maintaining the color, flavor, and freshness, as compared to the conventional methods (proteolysis, thermal, fermentation). The allergenicity may increase, decrease or persist unchanged depending on treatment intensity and protein structure. However, allergenicity can be minimized if optimal parameters (energy, time, temperature, and frequency) are applied during these processes. • The first review focused on the reduction of soybean allergenicity by physical treatments. • Physical treatments may reduce the allergens of soybean at different levels. • Extrusion seems to be the most convenient technology to reduce soybean allergenicity. • Combination of different processes provides new strategies for the reduction of soybean allergenicity. [ABSTRACT FROM AUTHOR]

Interactions between plant polyphenols and food allergens may be a new way to alleviate food allergies. The non-covalent interactions between the major allergen from peanut (Ara h 2) with procyanidin dimer (PA2) were therefore characterized using spectroscopic, thermodynamic, and molecular simulation analyses. The main interaction between the Ara h 2 and PA2 was hydrogen bonding. PA2 statically quenched the intrinsic fluorescence intensity and altered the conformation of the Ara h 2, leading to a more disordered polypeptide structure with a lower surface hydrophobicity. In addition, the in vitro allergenicity of the Ara h 2-PA2 complex was investigated using enzyme-linked immunosorbent assay (ELISA) kits. The immunoglobulin E (IgE) binding capacity of Ara h 2, as well as the release of allergenic cytokines, decreased after interacting with PA2. When the ratio of Ara h 2-to-PA2 was 1:50, the IgE binding capacity was reduced by around 43 %. This study provides valuable insights into the non-covalent interactions between Ara h 2 and PA2, as well as the potential mechanism of action of the anti-allergic reaction caused by binding of the polyphenols to the allergens. [ABSTRACT FROM AUTHOR]

An extensive safety assessment process exists for genetically-engineered (GE) crops. The assessment includes an evaluation of the introduced protein as well as the crop containing the protein with the goal of demonstrating the GE crop is “as-safe-as” non-GE crops in the food supply. One of the evaluations for GE crops is to assess the expressed protein for allergenic potential. Currently, no single factor is recognized as a predictor for protein allergenicity. Therefore, a weight-of-the-evidence approach, which accounts for a variety of factors and approaches for an overall assessment of allergenic potential, is conducted. This assessment includes an evaluation of the history of exposure and safety of the gene(s) source; protein structure (e.g. amino acid sequence identity to human allergens); stability of the protein to pepsin digestion in vitro; heat stability of the protein; glycosylation status; and when appropriate, specific IgE binding studies with sera from relevant clinically allergic subjects. Since GE crops were first commercialized over 20 years ago, there is no proof that the introduced novel protein(s) in any commercialized GE food crop has caused food allergy.

• Safety assessment of infant formulas requires testing of residual allergenicity. • Multi-parameter murine model is preferred over single-parameter guinea pig model. • Transferability of methods for testing residual allergenicity between centers. • Center-dependent gut microbial composition might affect the outcome variation. This 4-center study is part of a project to validate a food allergy murine model for safety testing of hydrolyzed infant formulas. The aim of the current multi-center experiment was to evaluate the residual allergenicity of three partial hydrolyzed whey proteins (pWH) in a multiple-parameter cow's milk allergy murine model and to compare to the classically used guinea pig model. Previous work showed differences in the magnitude of the allergic response to whey between centers. To get a first insight in the effect of housing on the robustness of the mouse model, microbiota composition of non-sensitized mice was analyzed and compared between centers. Mice were sensitized intragastrically (i.g.) with whey, pWH or eWH using cholera toxin as an adjuvant. In mice, whey-IgE/IgG1, acute allergic symptoms were determined upon whey challenge. Guinea pigs were orally sensitized ad libitum via the drinking water (day 0–37) and challenged intravenously with whey on day 49. The microbial composition in fecal samples was determined in non-sensitized mice in all 4 research centers before and after conduct of the study. Elevated levels of whey-IgG1 were detected in whey-sensitized mice in all centers. Except for pWH-A in center 4, we observed elevated levels of whey-IgE in whey-sensitized mice and mice sensitized with pWH-A, -B, -C. Center 2 was excluded from further analysis because of non-significant IgE levels in the positive control. In contrast to whey-mice, pWH-A treated mice showed no acute skin response, mMCP-1 release or change in body temperature upon whey challenge in all centers, which corresponds with the absence of anaphylactic shock symptoms in both the mouse and guinea pig model. pWH-B and -C induced anaphylactic shock symptoms in the guinea-pig and mice whereas results on the remaining allergic outcomes in mice were inconclusive. No differences in microbiota composition were measured in response to the challenge and Microbiota composition depended on the location of the centers. Both animal models showed comparable results on the residual allergenicity of partial hydrolyzed whey proteins, but none of the centers was able to differentiate between the residual sensitizing capacities of the pWH-B and -C based on a single elicitation parameter in the murine model. Differences in microbiota composition might contribute to the robustness of the food allergy murine model. For a well-balanced prediction on the potential allergenicity of hydrolyzed infant formulas a multiple murine parameter model is suggested to decrease the risk of false positive or false negative results. A future challenge is to develop an overall scoring system for proper risk assessment, taking all parameters into account. [ABSTRACT FROM AUTHOR]

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Food allergy has become a major public health and food safety issue concerned by the world . In the world, 0.2% -0.9% of adults and 0.4%-1.3% of children suffer from wheat allergy, which seriously affects the lives of allergic patients. The structure of food allergens can be changed by processing, which maight affect their allergenicities. Therefore, it is meaningful to study the influence of different processing on the allergenicity of gliadin in non-fermented dough. Here non-fermented dough were treated by different processing such as thermal processing (boiled, baked, microwave, high temperature and high pressure), cold treatments (liquid nitrogen, quick freezing machine) and non-thermal processing (static ultrahigh pressure, irradiation, pulsed light, ozone and ultrasonic). The molecular weight and the allergenity of wheat gliadin in non-fermented dough after various processing were determined by SDS-PAGE and the double antibody sandwich ELISA. SDS-PAGE electrophoresis results showed that the molecular weight of wheat gliadin in non-fermented dough changed significantly after boiled, baked or high temperature and high pressure treatment. The results of Sandwich ELISA showed that when the holding pressure temperature was 35℃ and the holding time was 20 min, the non-fermented dough wheat gliadin was treated with 100 -300 MPa ultra-high static pressure, its allergenicity increased first, then decreased, and then increased again, of which its allergenicity significantly decreased to 80.94% when treated at 250 MPa, and significantly increased to 127.27% or 128.17% when treated at 200 or 300 MPa, respectively, indicating that ultra-high static pressure treatment has a allergenicity increasing effect of gliadin in non-fermented dough; Irradiation treatment with γ-60Co at a dose of 1-15 kGy resulted in the allergenicity of gliadin in non-fermented dough decreased first, then increased and then decreased again, at 7, 13 kGy, the allergenicity decreased to 72.32% or 84.03%, respectively; The allergenicity of non-fermented dough wheat gliadin was significantly reduced after these hot, cold and non-heat processing treatments (P<0.05). After 2 hours of 500-watt ultrasonic treatment, its allergenicity was reduced to 90.23%; after Microwave, Quick-freezer, Pulsed light, or Baked treatment, it was reduced to 85.36%, 79.49%, 79.08% or 76.69%, respectively. Among them, the most significant (P<0.01) reduction in allergy was observed after Boiled, High temperature and high pressure, Liquid nitrogen, Ozone and Pulsed light (PL-1) treatment, and all of which decreased to about 60%, and ranked following by Boiled> Ozone fumigation 30 min (O3-1)> Liquid nitrogen> Pulsed glare 1 (PL-1)> High temperature and high pressure> Ozone fumigation for 60 min (O3-2). In short, the processing modes can significantly affect the allergenicity of non-fermented dough wheat gliadin, which can be used as an effective method for the safety control of food allergens and provide an effective reference for the production of desensitized food. At the same time, people's daily diet can be healthier by choosing a suitable processing method, especially for wheat susceptible people. Of course, the influence of different processing methods on the decreasing allergenicity of non-fermented dough wheat gliadin need to be further validated in combination with other in vivo experiments and especially the clinical trials of wheat susceptible people. [ABSTRACT FROM AUTHOR]

BACKGROUND: Peanut is among the most common of food allergies, and one of its allergens is Ara h 2. A previous study revealed that this allergen was recognized by serum immunoglobulin E (IgE) in over 90% of a peanut‐allergic patient population. Enzymatic cross‐linking is a popular processing method used to tailor food functionality, such as antigenicity. RESULT: The cross‐linking reactions of Ara h 2 were catalyzed by polyphenol oxidase (PPO), and the relevant reaction sites were identified using mass spectrometry and StavroX software. Two pairs of intramolecular cross‐linking peptides and two intermolecular cross‐linking peptides were found. Intramolecular cross‐linking was speculated to occur between ARG131 (amino acids 116–131) and TYR65 (amino acids 63–80) and between TYR60 (amino acids 56–62) and ARG92 (amino acids 92–102); the intermolecular cross‐linking sites were ARG31 with TYR84 or TYR89 and TYR65 or TYR72 with ARG92 or ARG102. Three out of four cross‐linking peptides were found in α‐helices, and destruction of this secondary structure resulted in a loose tertiary structure. Although seven linear allergen epitopes were involved in cross‐linking, the IgE binding capacity of protein changed slightly, while its sensitization potential decreased in mouse model. CONCLUSION: Exploring the structural change of Ara h 2 after cross‐linking is beneficial in further understanding the influence of structure on sensitization. This result indicated the future possibility of precision processing on structure of proteins to improve their properties. © 2019 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

An extensive safety assessment process exists for genetically-engineered (GE) crops. The assessment includes an evaluation of the introduced protein as well as the crop containing the protein with the goal of demonstrating the GE crop is "as-safe-as" non-GE crops in the food supply. One of the evaluations for GE crops is to assess the expressed protein for allergenic potential. Currently, no single factor is recognized as a predictor for protein allergenicity. Therefore, a weight-of-the-evidence approach, which accounts for a variety of factors and approaches for an overall assessment of allergenic potential, is conducted. This assessment includes an evaluation of the history of exposure and safety of the gene(s) source; protein structure (e.g. amino acid sequence identity to human allergens); stability of the protein to pepsin digestion in vitro; heat stability of the protein; glycosylation status; and when appropriate, specific IgE binding studies with sera from relevant clinically allergic subjects. Since GE crops were first commercialized over 20 years ago, there is no proof that the introduced novel protein(s) in any commercialized GE food crop has caused food allergy. [ABSTRACT FROM AUTHOR]

Food allergies are worldwide public health problems. Enzymatic hydrolysis has mild conditions, and high efficiency and stability, meaning it is widely used to reduce the allergenicity of food allergens. However, using only enzymatic hydrolysis allows allergens to retain some allergenicity, thereby limiting its application; combining enzymatic hydrolysis with processing represents a potentially effective solution to solve this issue. Here, the effects of three combinations of enzymatic hydrolysis and processing on food allergen allergenicity were reviewed: pre-processing before hydrolysis, hydrolysis under processing , and hydrolysis before processing. The mechanisms, advantages, and limitations of each combination were discussed. Combing pre-processing and enzymatic hydrolysis more effectively reducing allergenicity than a single treatment. However, each combination affects allergenicity through different mechanisms: (1) most pre-processing procedures (heating, ultrasound, high hydrostatic pressure, pulsed electric field, and pulsed ultraviolet light) disrupted conformational epitopes and increased enzyme accessibility by altering protein spatial structures; (2) cold plasma and fermentation reduced allergenicity mainly by hydrolyzing epitopes , yet combined with enzymatic hydrolysis further reduced allergenicity owing to the differences in hydrolysis sites; (3) glycation and polyphenols binding reduce allergenicity by masking linear epitopes , whereas enzymatic hydrolysis eliminates unmasked epitopes. Hydrolysis under processing improves hydrolysis efficiency; however, only limited research exists on the enzymatic changes that occur during processing. Hydrolysis before processing (especially fermentation) produces proteins with hypoallergenic, good sensory, and functional properties. The allergen allergenicity may increase, decrease, or remain unchanged depending on the processing method, conditions, enzyme type, and allergen source. [Display omitted] • Enzymatic hydrolysis combined with processing can effectively reduce allergenicity. • Optimal conditions and enzymes need to be explored for different allergens. • Hydrolysis before fermentation is used to produce superior hypoallergenic foods. • Safety of hydrolyzed proteins produced by new methods needs more evaluation. • Allergenicity reduction should not come at the expense of other characteristics. [ABSTRACT FROM AUTHOR]

The popularity of quinoa seeds has increased in the last decade due to their high nutritional value and natural gluten-free composition. Consumption of new proteins may pose a risk of introducing new allergies. In the present study the immunogenicity and sensitising capacity of quinoa proteins were assessed in a dose-response experiment in Brown Norway rats in comparison to proteins from spinach and peanut. Cross-reactivity between quinoa proteins and known allergens was evaluated by in silico analyses followed by analyses with 11 selected protein extracts and their anti-sera by means of ELISAs and immunoblotting. Further, an in vitro simulated gastro-duodenal digestion was performed. Quinoa proteins were found to have an inherent medium to high immunogenicity and sensitising capacity, being able to induce specific IgG1 and IgE levels higher than spinach but lower than peanut and elicit reactions of clinical relevance similar to peanut. Quinoa proteins were generally shown to resist digestion and retain capacity to bind quinoa-specific antibodies. Quinoa proteins were shown to be cross-reactive with peanut and tree nut allergens as high sequence homology and antibody cross-binding were demonstrated. Present study suggests that quinoa pose a medium to high level of allergenicity that should be further investigated in human studies. [Display omitted] • Quinoa had an inherent medium to high sensitising capacity in an animal model. • Likely the basic subunit of 11S globulin was the most sensitising allergen. • Quinoa proteins were in general resistant to digestion retaining antibody binding capacity. • Quinoa proteins showed potential cross-reactivity to certain tree nut allergens. [ABSTRACT FROM AUTHOR]

Highlights • Glycation of tropomyosin could destruct and mask epitopes. • Glycated tropomyosin by maltose insignificantly suppressed allergenicity. • Saccharides of larger molecular sizes reduced tropomyosin allergenicity. • Larger saccharides suppressed allergy reactivity of Caco-2 and KU812 cells. Abstract The allergenicity suppression of tropomyosin (TM) from Exopalaemon modestus by glycation with saccharides of different molecular sizes (glucose, maltose, maltotriose, maltopentaose and maltoheptaose) was investigated using immunoblotting, human colon epithelial cell line (Caco-2) and human basophil cell line (KU812). Glycation of TM by glucose, maltotriose, maltopentaose and maltoheptaose significantly destructed and masked TM epitopes to obtain lower allergenicity, while glycation of TM by maltose had insignificant suppression on TM allergenicity. In addition, the glycated TM by glucose, maltotriose, maltopentaose and maltoheptaose inhibited the proliferation and IL-8 secretion of Caco-2, and the CD63 and CD203c expression, MAPK signaling of KU812 basophils, while the glycated TM by maltose had insignificant suppression on the allergy reactivities of Caco-2 cells and KU812 basophils. Glycation of TM by saccharides with larger molecular sizes (such as maltoheptaose) could provide new insight into the desensitization of shrimp-induced food allergy. [ABSTRACT FROM AUTHOR]

Many food innovations rely on the introduction and use of new or modified proteins. New or modified food proteins may lead to major health risks due to their inherent potential to cause food allergy. Currently, the pre-market allergenicity assessment for new or modified food proteins and protein sources relies on methods for identifying allergenic hazards based on characteristics of known allergens. However, there is no general consensus on the allergenicity parameters to use and the criteria that should apply for the evaluation and decisions to be made. In this paper, we propose that the strategy for allergenicity risk assessment of new or modified food proteins and the methodologies applied should be governed by the risk management questions to be answered, reflected in the information needed by risk managers to enable their informed decision making. We generated an inventory of health outcome-related assessment parameters and criteria potentially important for risk management decision-making and we discuss the implications of selecting different optional criteria (e.g. cut-off values) for what could be accepted as safe with regards to the health outcomes in the (at risk) population. The impact of these various options on both method development and risk management practices was investigated. • New or modified food proteins may lead to food allergy and require risk assessment. • There is no guidance on allergenicity parameters and evaluation criteria to use. • Allergenicity risk assessment should be governed by the risk management questions. • Methodologies should be governed by the information needed by the risk manager. • We present an inventory of optional assessment parameters and evaluation criteria. [ABSTRACT FROM AUTHOR]

Abstract Background Aspirin enhances food allergy symptoms by increasing absorption of ingested allergens. The objective of this study is to elucidate the role of aspirin in facilitating intestinal absorption of the wheat allergen, gliadin, in rats. Methods Plasma concentrations of gliadin were determined after oral administration by gavage or administration into a closed intestinal loop in rats. We used an in situ intestinal re-circulating perfusion experiment to examine the effect of pepsin on aspirin-facilitated gliadin absorption. Fluorescein isothiocyanate (FITC)-labeled dextran-40 (FD-40) was used as a marker of non-specific absorption. The molecular size of gliadin and its allergenicity in plasma were examined using immunoblot analysis and intradermal reaction tests with Evans blue dye (EBD) extravasation, respectively. Results Aspirin increased plasma concentrations of gliadin after oral administration but had no effect in the closed intestinal loop study. An in situ intestinal re-circulating perfusion study showed that FITC-labeled gliadin was absorbed similarly to FD-40. Aspirin increased absorption of both intact and pepsin-digested gliadin, with a more significant effect on absorption of pepsin-treated gliadin. Immunoblotting showed that most gliadin was absorbed in intact form. When the gliadin fraction was extracted from rat plasma after gavage and injected intradermally into gliadin-sensitized rats, EBD extravasation was observed at injection sites in a gliadin dose-dependent manner. Conclusions Aspirin increased the absorption of intact and pepsin-digested gliadin via the paracellular pathway, maintaining their allergenicity. Moreover, the effect of aspirin on gliadin absorption was enhanced by modification and digestion of gliadin in the stomach. Graphical abstract Image 1 [ABSTRACT FROM AUTHOR]

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BACKGROUND Peanuts and tree nut allergies pose an increasing food safety problem. The aim of our study was to test the accuracy of different commercial enzyme‐linked immunosorbent assay (ELISA) kits in the detection of the presence of walnuts in untreated and heat exposed food samples. The effects of thermal treatment of samples were evaluated by exposing walnuts to different heat treatments. All samples were first analysed by two different commercial ELISA assays. Then, we performed a skin prick test (SPT) on nine patients with proven nut allergy using small walnut pieces from raw and treated samples. RESULTS: The presence of nuts proteins in thermally processed foods was not accurately detected by ELISA kits. All patients had a positive SPT reaction with raw walnut, while thermal treatments affected walnut allergenicity. The ELISA test gives a negative result in the case of strong thermal treatment, but at the same time allergic subjects react positively to stimulation with the same sample. CONCLUSION: This study suggests that commercial ELISA kits may not be able to accurately determine the amount of proteins present in thermally processed foods due to changes in the solubility and immunoreactivity of the target proteins. Finally, the clinical results highlight that thermal treatment might induce a reduction in walnut allergenicity. © 2018 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

Background: Allergic sensitisation towards cashew nut often happens without a clear history of eating cashew nut. IgE cross-reactivity between cashew and pistachio nut is well described; however, the ability of cashew nut-specific IgE to cross-react to common tree nut species and other Anacardiaceae, like mango, pink peppercorn, or sumac is largely unknown. Objectives: Cashew nut allergic individuals may cross-react to foods that are phylogenetically related to cashew. We aimed to determine IgE cross-sensitisation and cross-reactivity profiles in cashew nut-sensitised subjects, towards botanically related proteins of other Anacardiaceae family members and related tree nut species. Method: Sera from children with a suspected cashew nut allergy (n = 56) were assessed for IgE sensitisation to common tree nuts, mango, pink peppercorn, and sumac using dot blot technique. Allergen cross-reactivity patterns between Anacardiaceae species were subsequently examined by SDS-PAGE and immunoblot inhibition, and IgE-reactive allergens were identified by LC-MS/MS. Results: From the 56 subjects analysed, 36 were positive on dot blot for cashew nut (63%). Of these, 50% were mono-sensitised to cashew nuts, 19% were co-sensitised to Anacardiaceae species, and 31% were co-sensitised to tree nuts. Subjects co-sensitised to Anacardiaceae species displayed a different allergen recognition pattern than subjects sensitised to common tree nuts. In pink peppercorn, putative albumin- and legumin-type seed storage proteins were found to cross-react with serum of cashew nut-sensitised subjects in vitro. In addition, a putative luminal binding protein was identified, which, among others, may be involved in cross-reactivity between several Anacardiaceae species. Conclusions: Results demonstrate the in vitro presence of IgE cross-sensitisation in children towards multiple Anacardiaceae species. In this study, putative novel allergens were identified in cashew, pistachio, and pink peppercorn, which may pose factors that underlie the observed cross-sensitivity to these species. The clinical relevance of this widespread cross-sensitisation is unknown. [ABSTRACT FROM AUTHOR]

This paper presents the results of pollen and spore concentration of yellow drops in the Lucknow environs during the summer of 2014. The yellow spots were procured from the surface of a number of leaves and other objects from three different localities of Lucknow District of Uttar Pradesh. The size and shapes of these spots vary, ranging from linear to circular. Pollen grains recovered in good frequencies chiefly belong to angiosperms, whereas some gymnosperm pollen was also observed in trace frequencies. Other microbiota include fern spores, fungal remains and insect body parts in lower values. The study broadly suggests that palynomorphs recovered from yellow droppings are not fully airborne; rather, they are the types that honey bees gather from crop fields to feed their young. Brassica campestris and Asteroideae are the dominant plant taxa recorded in yellow rain samples. On investigation, it was noticed that yellow drop falling occurred for a few minutes on limited days during the summer of 2014, when the atmosphere experienced optimal temperature conditions with relatively humid environs. The observation also confirms that the yellow spots are nothing but faecal droppings, as suggested by the bee faeces theory which proposed that the origin of yellow rain is a phenomenon of nature. The study, in addition to aiding in understanding yellow rain occurrence, could also be helpful in aerobiological research, especially in examining the allergenicity of various pollen grains/spores in the area of investigation, causing bronchial asthma, hay fever (allergic rhinitis/pollinosis), nasobronchial allergy and other respiratory disorders along with conjunctivitis, contact dermatitis, eczema, food allergies and other health ailments. A multivariate principal component analysis (PCA) was applied to quantified data obtained from pollen frequency analyses of different areas of Lucknow, which clearly revealed a significant group variation in vegetation type on the basis of dispersal and deposition of pollen in yellow spots. [ABSTRACT FROM AUTHOR]

Cow's milk proteins allergy (CMA) is an atypical immune system response to cow's milk and dairy products. It's one of the most common food allergies in children affecting 8% of the total pediatric population pediatric population. This comprehensive review examines recent studies in CMA, especially regarding mammalian milk allergies such as goat's, sheep's, buffalo's, camel's, mare's and donkey's milk allergies in order to increase awareness of these selective allergies and to reduce allergy risks for those who have them. The consumption of other mammalian milk types is not recommended because of the significant homology between milk proteins from cow, sheep, goat and buffalo resulting in clinical cross-reactivity. However, camel's, mare's or donkey's milk may be tolerated by some allergic patients. Selective mammalian milk allergies are unusual and rare disorders characterized by severe symptoms including angio-oedema, urticaria, respiratory manifestations and anaphylaxis. Based on the reported allergic cases, cheese products including Ricotta, Romano, Pecorino and Mozzarella, are considered as the most common source of allergens especially in goat's, sheep's and buffalo's milk allergies, while the major allergens in donkey's and mare's milk seems to be whey proteins including lysozyme, α-lactalbumin and β-lactogloblin due to the low casein/whey proteins ratio in equine's milk. [Display omitted] • Mammalian milk can induce unusual and rare food allergies characterized by severe symptoms. • The most common source of allergens in goat's, sheep's and buffalo's milk allergies are cheese products. • The main allergens in donkey's and mare's milk are whey proteins (α-lactalbumin and β-lactogloblin). • There is a strong need to promote awareness of various food ingredients. [ABSTRACT FROM AUTHOR]

The levels of food allergens in worm-wounded or non-wounded green soybeans (edamame) and mature soybeans were investigated by immunoblotting and enzyme-linked immunosorbent assay (ELISA), using allergen-specific antibodies. Non-wounded and worm-wounded soybeans showed similar total protein profiles after Coomassie brilliant blue staining, but some protein bands were observed to have been changed by worm wounding. Immunoblotting with specific antibodies for major soybean allergens (Gly m 5, Gly m 6, Gly m Bd 30 K, and Kunitz soybean trypsin inhibitor) revealed that protein band profiles and intensities were not significantly changed by worm wounding. In contrast, levels of the pollen-related soybean allergens Gly m 4 and Gly m 3 were strongly increased by worm wounding in both green and mature soybeans, as detected by immunoblotting and ELISA. These results suggested that the pollen-related food allergen risk (i.e., oral allergy syndrome; OAS) from soybeans might be enhanced by worm wounding of soybeans. [ABSTRACT FROM AUTHOR]

Abstract: Background: The galactose‐α‐1,3‐galactose (α‐Gal) epitope is involved in red meat allergy. As α‐Gal is structurally similar to the blood group B‐antigen, we explored the relationship between the immune responses to α‐Gal‐ and the B‐antigen in red meat‐allergic patients compared to healthy A/O or B blood donors. Methods: Sera from 51 red meat‐allergic patients IgE‐positive to α‐Gal and 102 healthy blood donors (51 blood group A/O; 51 blood group B) were included. α‐Gal‐ and B‐antigen‐specific IgE (ImmunoCAP) and IgG/IgG1‐4 (ELISA) responses were determined. Basophil activation tests were performed. Results: Fifteen healthy donors were IgE positive to α‐Gal, of which 3 had blood group B. The allergic patients had significantly higher α‐Gal IgE levels compared to the healthy donors. The majority of the allergic patients, but none of the healthy donors, had IgE against the B‐antigen. Inhibition studies revealed cross‐reactivity between α‐Gal and the B‐antigen. The biological activity of the B‐antigen was confirmed by basophil activation tests. Anti‐α‐Gal IgG1 and IgG4 levels were significantly higher in the patients compared to the healthy donors. Moreover, the IgG response to the B‐antigen was comparable between the allergic patients and healthy A/O donors. Conclusion: Red meat‐allergic patients showed significantly higher α‐Gal IgE, IgG1, and IgG4 levels, reflecting a Th2 response, compared to healthy blood donors. Blood group B donors had significantly reduced antibody responses to α‐Gal, due to similarities with the B‐antigen, resulting in a lower risk of sensitization to α‐Gal and development of red meat allergy. [ABSTRACT FROM AUTHOR]

Background The increasing prevalence of food allergy cases is an issue of global concern. As a result, scientific innovations have been taking place to induce chemical modifications for achieving attenuation of allergenic responses in sensitive individuals or for manufacturing hypoallergenic foods using food processing technologies. Conventional processing techniques involving heat treatment are usually exploited, but may be accompanied by dramatic changes in food quality attributes due to high temperature. Therefore, alternative nonthermal technologies may be a new direction for attaining hypoallergenicity. Scope and approach This review presents the current knowledge and recent findings on the possibility of engaging nonthermal technologies including pulsed light, high pressure processing, irradiation, cold plasma, ultrasound and pulsed electric field, for the elimination of allergenic proteins in foods and their underlying mechanisms. In contrast to heat-based methods, nonthermal treatments can adequately retain sensorial and nutritional quality of the food products, while altering allergenicity. Food allergy classification, clinical manifestations, epitope characterization and detection methods are also presented. Key findings and conclusions To date, studies show that nonthermal processes have complicated effects on food allergens. Much further research efforts should be made for using nonthermal processing technologies as alternatives to replace traditional techniques. Nonetheless, it is expected that in the near future, susceptible individuals will benefit from different hypoallergenic products processed with novel nonthermal technologies at an affordable cost. [ABSTRACT FROM AUTHOR]

Food allergens have a notable potential to induce various health concerns in susceptible individuals. The majority of allergenic foods are usually subjected to thermal processing prior to their consumption. However, during thermal processing and long storage of foods, Maillard reaction (MR) often takes place. The MR is a non-enzymatic glycation reaction between the carbonyl group of reducing sugars and compounds having free amino groups. MR may sometimes be beneficial by damaging epitope of allergens and reducing allergenic potential, while exacerbation in allergic reactions may also occur due to changes in the motifs of epitopes or neoallergen generation. Apart from these modulations, nonenzymatic glycation can also modify the food protein(s) with various type of advance glycation end products (AGEs) such as Ne-(carboxymethyl-)lysine (CML), pentosidine, pyrraline, and methylglyoxal-H1 derived from MR. These Maillard products may act as immunogen by inducing the activation and proliferation of various immune cells. Literature is available to understand pathogenesis of glycation in the context of various diseases but there is hardly any review that can provide a thorough insight on the impact of glycation in food allergy. Therefore, present review explores the pathogenesis with special reference to food allergy caused by non-enzymatic glycation as well as AGEs. [ABSTRACT FROM AUTHOR]

Lupin seeds are already widely used as an ingredient in different food products. Their attractiveness is related mainly to their high protein content that is characterised by a favourable amino acid composition, as well as the desired technological properties. However, with the increase of lupin seeds usage in food manufacture, their potential allergic properties have been demonstrated. The aim of this work was to study the immunoreactivity changes taking place during the enzymatic hydrolysis of the major seed proteins of narrow-leafed ( Lupinus angustifolius, varieties Zeus and Bojar) and yellow ( L. luteus, var. Lord and Parys) lupin species. Two digestion systems were used, namely the in vitro model simulating digestion taking place in digestive track, and specific hydrolysis carried out by trypsin. The obtained hydrolysates were analysed by means of one-dimensional electrophoresis, and their immunoreactivity was assessed with the use of a sera pool from patients with lupin-specific IgE. An important reduction in allergenicity of lupin seed proteins was observed when trypsin digestion was applied. The digestion in the in vitro model revealed the possibility of formation of neoallergens which were identified on the basis of mass spectrometry results as β-conglutin fraction. [ABSTRACT FROM AUTHOR]

[Display omitted] • Wheat products often cause food allergies as well as intolerances. • Future methods to detect allergens aim to be efficient, economical, time-saving. • Biological modification methods are a better way to reduce wheat allergens. • Editing Wheat Allergen Genes by Biotechnology is a Promising Method. • Desensitization findings require extensive validation before application. Wheat is widely available in people's daily diets. However, some people are currently experiencing IgE-mediated allergic reactions to wheat-based foods, which seriously impact their quality of life. Thus, it is imperative to provide comprehensive knowledge and effective methods to reduce the risk of wheat allergy (WA) in food. In the present review, recent advances in WA symptoms, the major allergens, detection methods, opportunities and challenges in establishing animal models of WA are summarized and discussed. Furthermore, an updated overview of the different modification methods that are currently being applied to wheat-based foods is provided. This study concludes that future approaches to food allergen detection will focus on combining multiple tools to rapidly and accurately quantify individual allergens in complex food matrices. Besides, biological modification has many advantages over physical or chemical modification methods in the development of hypoallergenic wheat products, such as enzymatic hydrolysis and fermentation. It is worth noting that using biotechnology to edit wheat allergen genes to produce allergen-free food may be a promising method in the future which could improve the safety of wheat foods and the health of allergy sufferers. [ABSTRACT FROM AUTHOR]

Acrylamide (AA) forms during the thermal processing of food, but adversely affects human health. As the consumption of heat-processed foods increases, the potentially harmful effect of AA on food allergies needs to be clarified. Here, we investigated how AA affects the allergenicity of OVA in vivo using a mouse model of orally induced OVA allergy. AA enhanced OVA-induced food allergic response by increasing IgE, IgG, IgG1, histamine, and MCP-1. AA promoted the Th2 cell response to modulate the imbalance in Th1/Th2. Furthermore, AA reduced the expression of intestinal tight junction proteins, and disrupted the permeability of the intestine, which impaired the intestinal epithelial barrier, resulting in more OVA crossing it. These actions aggravated the allergic reaction of OVA. In conclusion, this study confirmed the potentially harmful effect of AA on food allergy. • Acrylamide enhanced OVA-induced food allergic response. • Acrylamide promoted the Th2 cell response to modulate the imbalance in Th1/Th2. • Acrylamide impaired the intestinal epithelial barrier, resulting in more OVA crossing it. [ABSTRACT FROM AUTHOR]

The edible yellow mealworm (Tenebrio molitor), contains an extremely diverse panel of soluble proteins, including proteins with structural functions such as muscle proteins, as well as proteins involved in metabolic functions such as enzymes. Most of these proteins display a more or less pronounced allergenic character toward previously sensitized people, especially people allergic to shrimps and other shellfish. A mass spectrometry approach following the separation of a mealworm protein, extracted by sodiumdodecyl sulfate-polyacrylamide gel electrophoresis, allowed us to identify up to 106 distinct protein fractions including molecules with structural and functional functions, susceptible to developing an allergenic potential due to the possibility of immunoglobulin E-binding cross-reactions with their counterparts occurring in shellfish. In this respect, most of the sera from people allergic to shrimps reacted with the mealworm protein extract in Western blot experiments. Moreover, the potential mealworm allergens triggered the in vitro degranulation of rat leukemic basophils transfected with the human high-affinity IgE receptor (FcεRI), upon sensitization by the IgE-containing sera from people allergic to shrimps and other shellfish foods. Owing to the large repertoire of IgE-binding cross-reacting allergens the yellow mealworm shares with other phylogenetically-related groups of arthropods, it would seem prudent to inform the consumers, especially those allergic to shellfish, by appropriate labeling on edible mealworm packages about the potential risk of developing an allergic reaction.

Ovalbumin (OVA), an (hen) egg allergen, is one of the most abundant glycoprotein allergens associated with IgE-mediated hypersensitivity through the T-helper type 2 immune response. The effect of deglycosylation of the N- terminal glycan in OVA on allergenicity and antigenicity after N- acetylglucosaminidase treatment was studied. N- acetylglucosaminidase-treated OVA (N-OVA) evaluated using an enzyme-linked immunosorbent assay, respectively. N-OVA significantly ( p < 0.05) OVA-specific IgE and histamine levels. In addition, N-OVA decreased the antigenicity of OVA 1000-fold. These results suggest that the degree of allergenicity and antigenicity reduced with deglycosylation of N- terminal glycan in OVA. [ABSTRACT FROM AUTHOR]