Allergens in Food: Identification, Detection, and Mitigation

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Quality and Safety".

Deadline for manuscript submissions: closed (30 December 2024) | Viewed by 4449

Special Issue Editors


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Guest Editor
Molecular and Cell Biology, James Cook University, Townsville, QLD 4811, Australia
Interests: food allergies; seafood allergies; molecular allergology; allergy diagnostics; allergen immunology; antibody cross-reactivity; allergen characterisation
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Guest Editor
Tropical Futures Institute, James Cook University Singapore, Singapore 387380, Singapore
Interests: food allergies; seafood allergies; proteomics; food safety; food authenticity and quality; aquatic and human health

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Guest Editor
Department of Paediatrics, Yong Loo Lin School of Medicine, National University of Singapore, 1E Kent Ridge Road, NUHS Tower Block Level 12, Singapore 119228, Singapore
Interests: atopic dermatitis; food allergy & anaphylaxis; skin microbiome; developmental origins of health and disease (DoHAD)

Special Issue Information

Dear Colleagues,

Food allergies and consequent anaphylaxis have become major public health and food safety problems worldwide. It is estimated that over 500 million people live with food allergies. Without a realistic cure for food allergies, the diligent avoidance of allergenic foods is the best management option for allergic individuals. Subsequently, regulatory bodies mandate food allergen labelling to help affected consumers make informed food choices and avoid accidental exposure.

Vital progress has been made regarding the characterisation of food allergens, the study of their immunological properties, and their application in molecular allergy diagnosis. Known food allergens belong to a relatively restricted number of protein families characterized by biochemical and physicochemical properties. Understanding the molecular relationship of allergenic proteins enables the understanding of cross-reactivity and determining the allergenic risk, supported by recent advanced computational approaches.

Analytical tools for the detection and quantification of allergens and their residues in foods are integral parts of evidence-based risk assessments for labelling decisions. Detection methodologies start with the reproducible extraction of proteins (including allergens); the characterisation of molecular identity using biochemical and computational approaches; and sensitive quantification methods, including biosensors, ELISAs, PCR, and advanced mass spectrometry.

The global human population’s rapid growth over the last few centuries has raised the need for increased food protein production. Subsequently, the domestication of food sources and the substitution of traditional animal-based food with novel sustainable and healthy alternatives are topics that have gained increasing interest in academia and industry, as well as among governments and other stakeholders of food innovation systems. The ultimate aim of alternative food production and processing approaches is to achieve high production yields of cost-efficient food products with high nutritional values, low environmental impacts, and the desired functional and sensory properties for use as ingredients. Aquatic-based proteins and microalgae, fungi, plant-based proteins, cultured meat, and insects are the most promising solutions to date; however, their allergen profiles and allergenicities require close investigations in order to mitigate risks.

For this Special Issue, submissions in the form of original research and review papers that contribute to advancing the identification, detection, quantification, and alteration of allergens, starting from food ingredients and processing to conventional and novel food products, are welcome. Special attention will be paid to allergen detection and different mitigation approaches, including characterisation methods for food allergens, new detection technologies, new analytical platforms (e.g., mass spectrometric methods, PCR, ELISAs), and validation approaches.

Prof. Dr. Andreas L. Lopata
Dr. Thimo Ruethers
Dr. Elizabeth Huiwen Tham
Guest Editors

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Keywords

  • food allergens
  • food allergies
  • alternative proteins
  • allergen characterisation
  • biosensors
  • plant-based proteins
  • insect proteins
  • food processing
  • allergenicity
  • allergenomics
  • food allergen management
  • cross-reactivity
  • PCR and mass spectrometry
  • allergen detection
  • bioinformatics of allergens
  • food safety
  • molecular allergology

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Published Papers (3 papers)

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Research

12 pages, 989 KiB  
Article
Food Allergen Quantitative Risk Assessment at a Crossroads: A Critical Evaluation of Laboratory Performance for Quantifying Total Egg and Milk Protein in Cookies
by Elena Cubero-Leon, Jørgen Nørgaard, Pieter Dehouck and Piotr Robouch
Foods 2025, 14(6), 957; https://doi.org/10.3390/foods14060957 - 11 Mar 2025
Viewed by 687
Abstract
The accurate quantification of food allergens is crucial for ensuring consumer safety and compliance with regulatory requirements. A proficiency test (PT) was organised to evaluate the performance of laboratories in quantifying total egg and total milk protein in cookies. The PT involved 20 [...] Read more.
The accurate quantification of food allergens is crucial for ensuring consumer safety and compliance with regulatory requirements. A proficiency test (PT) was organised to evaluate the performance of laboratories in quantifying total egg and total milk protein in cookies. The PT involved 20 laboratories, which reported results using mainly commercial ELISA kits and liquid chromatography–tandem mass spectrometry (LC-MS/MS). The findings indicate a satisfactory performance for milk protein determination among the majority of participant laboratories. However, the quantification of egg proteins in heated products remains a challenge, with most laboratories reporting results significantly below the reference value. Several potential factors contributing to this challenge are discussed, including the denaturation of egg proteins during heat treatment, differences in extraction strategies and the antibodies used in ELISA kits, and the lack of standardised methods and conversion factors for LC-MS/MS analysis. These findings underscore the importance of regular PT exercises to evaluate laboratory performance and ensure compliance with WHO/FAO recommendations. The results of this study aim to guide the development of improved analytical methods and strategies for ensuring the accurate quantification of food allergens. Full article
(This article belongs to the Special Issue Allergens in Food: Identification, Detection, and Mitigation)
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20 pages, 3625 KiB  
Article
Effects of Low-Allergen Wheat and Bayberry Leaf on Wheat Bread: A Comparison with Commercial Wheat
by Yoko Tsurunaga and Eishin Morita
Foods 2025, 14(3), 364; https://doi.org/10.3390/foods14030364 - 23 Jan 2025
Viewed by 731
Abstract
Gliadin and glutenin wheat proteins are major food allergens. The allergenicity of various wheat products, such as bread, can be reduced by substituting flour with plant-derived tannins. Here, we investigated a technique for reducing the allergenicity of wheat by utilizing the properties of [...] Read more.
Gliadin and glutenin wheat proteins are major food allergens. The allergenicity of various wheat products, such as bread, can be reduced by substituting flour with plant-derived tannins. Here, we investigated a technique for reducing the allergenicity of wheat by utilizing the properties of proanthocyanidins (PAs), which strongly bind to proteins. We compared commercial bread wheat (BW), low-allergen wheat (1BS-18 “Minamino Kaori”; 1BS-18M), and bayberry leaves (BBLs). Allergenicity was investigated through enzyme-linked immunosorbent assays (ELISAs) and Western blotting (WB). The immunoreactivity of wheat allergens in both BW and 1BS-18M decreased in a concentration-dependent manner with BBL substitution, and the effect was greatest at 10%. The antioxidative properties also increased with BBL substitution, and the highest antioxidative property was observed at 10%. The specific volumes of both BW and 1BS-18M decreased while the a* value (green to red) increased with increasing BBL substitution. In contrast, no significant differences were observed in the texture of breads with 0% (control), 3%, or 5% BBL substitution. However, 10% BBL substitution led to a significant (p < 0.05) reduction in the texture of the bread. Therefore, 5% BBL substitution is optimal for achieving low allergenicity and improved antioxidative properties while maintaining quality. Full article
(This article belongs to the Special Issue Allergens in Food: Identification, Detection, and Mitigation)
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23 pages, 8612 KiB  
Article
Allergen Diversity and Abundance in Different Tissues of the Redclaw Crayfish (Cherax quadricarinatus)
by Emily M. Jerry, Shaymaviswanathan Karnaneedi, Thimo Ruethers, Dean R. Jerry, Kelly Condon and Andreas L. Lopata
Foods 2024, 13(2), 315; https://doi.org/10.3390/foods13020315 - 19 Jan 2024
Cited by 1 | Viewed by 2282
Abstract
Shellfish allergy affects ~2.5% of the global population and is a type I immune response resulting from exposure to crustacean and/or molluscan proteins. The Australian Redclaw crayfish (Cherax quadricarinatus) is a freshwater species endemic to and farmed in northern Australia and [...] Read more.
Shellfish allergy affects ~2.5% of the global population and is a type I immune response resulting from exposure to crustacean and/or molluscan proteins. The Australian Redclaw crayfish (Cherax quadricarinatus) is a freshwater species endemic to and farmed in northern Australia and is becoming an aquaculture species of interest globally. Despite being consumed as food, allergenic proteins from redclaw have not been identified or characterised. In addition, as different body parts are often consumed, it is conceivable that redclaw tissues vary in allergenicity depending on tissue type and function. To better understand food-derived allergenicity, this study characterised allergenic proteins in various redclaw body tissues (the tail, claw, and cephalothorax) and how the stability of allergenic proteins was affected through cooking (raw vs. cooked tissues). The potential of redclaw allergens to cross-react and cause IgE-binding in patients allergic to other shellfish (i.e., shrimp) was also investigated. Raw and cooked extracts were prepared from each body part. SDS-PAGE followed by immunoblotting was performed to determine allergen-specific antibody reactivity to sarcoplasmic calcium-binding protein and hemocyanin, as well as to identify redclaw proteins binding to IgE antibodies from individual and pooled sera of shrimp-allergic patients. Liquid chromatography-mass spectrometry (LC/MS) was utilised to identify proteins and to determine the proportion within extracts. Known crustacean allergens were found in all tissues, with a variation in tissue distribution (e.g., higher levels of hemocyanin in the claw and cephalothorax than in the tail). The proportion of some allergens as a percentage of remaining heat-stable proteins increased in cooked tissues. Previously described heat-stable allergens (i.e., hemocyanin and sarcoplasmic calcium-binding protein) were found to be partially heat-labile. Immunoblotting indicated that shrimp-allergic patients cross-react to redclaw allergens. IgE-binding bands, analysed by LC/MS, identified up to 11 known shellfish allergens. The findings of this study provide fundamental knowledge into the diagnostic and therapeutic field of shellfish allergy. Full article
(This article belongs to the Special Issue Allergens in Food: Identification, Detection, and Mitigation)
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