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Food Allergen Detection and Characterisation
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Food Allergen Detection and Characterisation

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Analytical Methods".

Deadline for manuscript submissions: closed (30 March 2024) | Viewed by 7548

Special Issue Editor

Dr. Nanju Alice Lee

E-Mail Website
Guest Editor
School of Chemical Engineering, University of New South Wales, Sydney, NSW 2052, Australia
Interests: food safety; food allergy; molecular allergenomics; food immunology; novel food processing; in vitro diagnostics technology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food allergy and anaphylaxis have become significant public health and food safety issues worldwide. The World Allergy Organization (WAO) has estimated that at least 250 million people live with food allergies. Without a practical cure for food allergy, diligent avoidance of allergenic foods is the best management option for allergic individuals. As a result, many regulatory bodies mandate food allergen labelling to help allergic consumers to make an informed food choice and avoid accidental exposure.

This Special Issue will be focusing on molecular aspects of allergens for food allergy. It will publish original research articles and review papers that contribute to the broad theme of food allergen detection and characterisation. This includes but is not limited to new analytical methodologies, allergen modification (through food technology/engineering) and characterisation, and nanoallergens for immunotherapy. 

Dr. Nanju Alice Lee
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • food allergy 
  • food allergens 
  • allergenomics 
  • biosensors 
  • processing 
  • food safety 
  • immunoassay 
  • PCR 
  • nanoallergens 
  • molecular allergology

Published Papers (5 papers)

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Research

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17 pages, 2876 KiB  
Article
Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR
by Bruno Beyer, Dominik Obrist, Philipp Czarda, Katharina Pühringer, Filip Vymyslicky, Barbara Siegmund, Stefano D’Amico and Margit Cichna-Markl
Foods 2024, 13(5), 673; https://doi.org/10.3390/foods13050673 - 23 Feb 2024
Viewed by 590
Abstract
Seeds of “sweet lupins” have been playing an increasing role in the food industry. Lupin proteins may be used for producing a variety of foods, including pasta, bread, cookies, dairy products, and coffee substitutes. In a small percentage of the population, lupin consumption [...] Read more.
Seeds of “sweet lupins” have been playing an increasing role in the food industry. Lupin proteins may be used for producing a variety of foods, including pasta, bread, cookies, dairy products, and coffee substitutes. In a small percentage of the population, lupin consumption may elicit allergic reactions, either due to primary sensitization to lupin or due to cross-allergy with other legumes. Thus, lupin has to be declared on commercial food products according to EU food regulations. In this study, we investigated the influence of roasting seeds of the L. angustifolius cultivar “Boregine” on the detectability of lupin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), ELISAs, LC-MS/MS, and real-time PCR. Seeds were roasted by fluidized bed roasting, and samples were drawn at seed surface temperatures ranging from 98 °C to 242 °C. With increasing roasting temperature, the extractability of proteins and DNA decreased. In addition, roasting resulted in lower detectability of lupin proteins by ELISAs and LC-MS/MS and lower detectability of DNA by real-time PCR. Our results suggest reduced allergenicity of roasted lupin seeds used for the production of “lupin coffee”; however, this has to be confirmed in in vivo studies. Full article
(This article belongs to the Special Issue Food Allergen Detection and Characterisation)
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12 pages, 4854 KiB  
Article
Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen
by Ricarda Zeindl, Annika L. Franzmann, Monica L. Fernández-Quintero, Clarissa A. Seidler, Valentin J. Hoerschinger, Klaus R. Liedl and Martin Tollinger
Foods 2023, 12(21), 3939; https://doi.org/10.3390/foods12213939 - 27 Oct 2023
Viewed by 1011
Abstract
Allergies related to kiwi consumption have become a growing health concern, with their prevalence on the rise. Many of these allergic reactions are attributed to cross-reactivity, particularly with the major allergen found in birch pollen. This cross-reactivity is associated with proteins belonging to [...] Read more.
Allergies related to kiwi consumption have become a growing health concern, with their prevalence on the rise. Many of these allergic reactions are attributed to cross-reactivity, particularly with the major allergen found in birch pollen. This cross-reactivity is associated with proteins belonging to the pathogenesis-related class 10 (PR-10) protein family. In our study, we determined the three-dimensional structures of the two PR-10 proteins in gold and green kiwi fruits, Act c 8 and Act d 8, using nuclear magnetic resonance (NMR) spectroscopy. The structures of both kiwi proteins closely resemble the major birch pollen allergen, Bet v 1, providing a molecular explanation for the observed immunological cross-reactivity between kiwi and birch pollen. Compared to Act d 11, however, a kiwi allergen that shares the same architecture as PR-10 proteins, structural differences are apparent. Moreover, despite both Act c 8 and Act d 8 containing multiple cysteine residues, no disulfide bridges are present within their structures. Instead, all the cysteines are accessible on the protein’s surface and exposed to the surrounding solvent, where they are available for reactions with components of the natural food matrix. This structural characteristic sets Act c 8 and Act d 8 apart from other kiwi proteins with a high cysteine content. Furthermore, we demonstrate that pyrogallol, the most abundant phenolic compound found in kiwi, binds into the internal cavities of these two proteins, albeit with low affinity. Our research offers a foundation for further studies aimed at understanding allergic reactions associated with this fruit and exploring how interactions with the natural food matrix might be employed to enhance food safety. Full article
(This article belongs to the Special Issue Food Allergen Detection and Characterisation)
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13 pages, 937 KiB  
Article
Comparative Analysis of the Immune Response and the Clinical Allergic Reaction to Papain-like Cysteine Proteases from Fig, Kiwifruit, Papaya, Pineapple and Mites in an Italian Population
by Ivana Giangrieco, Maria Antonietta Ciardiello, Maurizio Tamburrini, Lisa Tuppo, Chiara Rafaiani, Adriano Mari and Claudia Alessandri
Foods 2023, 12(15), 2852; https://doi.org/10.3390/foods12152852 - 27 Jul 2023
Cited by 2 | Viewed by 1099
Abstract
Several plant papain-like cysteine proteases are exploited by the food, cosmetic, pharmaceutical and textile industries. However, some of these enzymes can cause allergic reactions. In this context, we investigated the frequency of sensitization and allergic reactions to some fruit and/or latex cysteine proteases, [...] Read more.
Several plant papain-like cysteine proteases are exploited by the food, cosmetic, pharmaceutical and textile industries. However, some of these enzymes can cause allergic reactions. In this context, we investigated the frequency of sensitization and allergic reactions to some fruit and/or latex cysteine proteases, which are used as additives by the food industry to improve and modify the quality of their products. The FABER test was used to analyse the patients‘ sensitization towards five plants and, for comparison, two homologous mite cysteine proteases. In an Italian population of 341 allergic patients, 133 (39%) had IgE specific for at least one of the seven cysteine proteases under investigation. Most of the patients were IgE positive for Der p 1 and/or Der f 1 (96.38%) reported a clinical history suggestive of respiratory allergy to mites, whereas none of the subjects sensitized to the homologs from papaya, pineapple and fig reported allergy symptoms following ingestion of these foods. Only one patient referred symptoms from ingesting kiwifruit. Therefore, the obtained results showed that sensitization to the fruit enzymes was only rarely concomitant with allergic reactions. These observations, together with the literature reports, suggest that the allergy to plant papain-like cysteine proteases might mainly be an occupational disease. Full article
(This article belongs to the Special Issue Food Allergen Detection and Characterisation)
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14 pages, 2425 KiB  
Article
Long Non-Coding RNAs Expressed in the Peanut Allergy for Understanding the Pathophysiology of Peanut Allergy Rat Model
by Manman Liu, Sen Li, Boya Li, Shanfeng Sun, Guirong Liu, Junjuan Wang, Mengzhen Hao and Huilian Che
Foods 2022, 11(23), 3760; https://doi.org/10.3390/foods11233760 - 22 Nov 2022
Cited by 1 | Viewed by 1221
Abstract
Background: Peanut allergy (PA) has become a clinical and public health problem, which is mainly regulated by genetics, immune responses, and environmental factors. Diagnosis and treatment for PA have always remained huge challenges due to its multiple triggers. Studies have shown that long [...] Read more.
Background: Peanut allergy (PA) has become a clinical and public health problem, which is mainly regulated by genetics, immune responses, and environmental factors. Diagnosis and treatment for PA have always remained huge challenges due to its multiple triggers. Studies have shown that long non-coding RNAs (lncRNAs) play a critical role in the development of allergic diseases. Method and Results: In the current study, we examined the plasma lncRNA expression profiles of peanut allergy Brown Norway rats and healthy controls and 496 differently expressed lncRNAs were identified, including 411 up-regulated genes and 85 down-regulated genes. We screened 8 lncRNAs based on the candidate principle and the candidates were verified in individual samples by quantitative real-time PCR. Then, the four lncRNA-based diagnostic model was established by least absolute shrinkage and selection operator (LASSO) and logistic regression, which was proved by area under the receiver operating characteristic curve (AUC). Conclusions: In summary, we assessed the correlation between lncRNA expression levels and the diagnosis of peanut allergy, which may perform a vital role in guiding the management of peanut allergy. Full article
(This article belongs to the Special Issue Food Allergen Detection and Characterisation)
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Review

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18 pages, 1399 KiB  
Review
Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing
by Elissa Haidar, Jack Lakkis, Marc Karam, Mohamed Koubaa, Nicolas Louka and Espérance Debs
Foods 2023, 12(6), 1253; https://doi.org/10.3390/foods12061253 - 15 Mar 2023
Cited by 6 | Viewed by 2530
Abstract
Peanuts are the seeds of a legume crop grown for nuts and oil production. Peanut allergy has gained significant attention as a public health issue due to its increasing prevalence, high rate of sensitization, severity of the corresponding allergic symptoms, cross-reactivity with other [...] Read more.
Peanuts are the seeds of a legume crop grown for nuts and oil production. Peanut allergy has gained significant attention as a public health issue due to its increasing prevalence, high rate of sensitization, severity of the corresponding allergic symptoms, cross-reactivity with other food allergens, and lifelong persistence. Given the importance of peanuts in several sectors, and taking into consideration the criticality of their high allergic potential, strategies aiming at mitigating their allergenicity are urgently needed. In this regard, most of the processing methods used to treat peanuts are categorized as either thermal or thermomechanical techniques. The purpose of this review is to provide the reader with an updated outlook of the peanut’s allergens, their mechanisms of action, the processing methods as applied to whole peanuts, as well as a critical insight on their impact on the allergenicity. The methods discussed include boiling, roasting/baking, microwaving, ultrasonication, frying, and high-pressure steaming/autoclaving. Their effectiveness in alleviating the allergenicity, and their capacity in preserving the structural integrity of the treated peanuts, were thoroughly explored. Research data on this matter may open further perspectives for future relevant investigation ultimately aiming at producing hypoallergenic peanuts. Full article
(This article belongs to the Special Issue Food Allergen Detection and Characterisation)
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