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Advances in the Approach Food Allergy
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Advances in the Approach Food Allergy

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

Deadline for manuscript submissions: closed (20 December 2020) | Viewed by 14401

Special Issue Editor

Dr. Beatriz Cabanillas

E-Mail Website
Guest Editor
1. Department of Allergy, Research Institute Hospital 12 de Octubre, Madrid, Spain
2. Department of Dermatology and Allergy, University of Bonn Medical Center, Bonn, Germany
Interests: food allergy; food chemistry; allergy & clinical immunology; food science & technology

Special Issue Information

Dear Colleagues,

The research field of food allergy is experiencing an important development with essential advances in the understanding of the pathophysiology of food allergy, sensitization routes, and the roles that specific immune cells, receptors, and pathways have in the initiation, development, and regulation of food allergies. Furthermore, novel insights on allergen characterization are not only providing advances in the description of new allergens and their properties, but they are also creating accurate maps of the epitopes that are highly recognized by IgE. The numerous advances that the research field of food allergy is currently experiencing, are creating potential for improved strategies in the diagnosis and treatment of food allergy.

Your contribution to this Special Issue, in which you are invited to share your findings and insights in the form of research articles, reviews, or short communications, will be a valuable asset and a compelling contribution that will potentially have an important impact on the field of food allergy.

Dr. Beatriz Cabanillas
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
  • Sensitization
  • Regulation
  • Allergens
  • Epitopes
  • Component-resolved diagnostics
  • Immunotherapy
  • Food processing

Published Papers (5 papers)

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Research

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14 pages, 1595 KiB  
Article
Development of Immunohistochemical Methods for Casein Detection in Meat Products
by Ludmila Kalčáková, Matej Pospiech, Bohuslava Tremlová, Zdeňka Javůrková and Irina Chernukha
Foods 2021, 10(1), 28; https://doi.org/10.3390/foods10010028 - 24 Dec 2020
Cited by 1 | Viewed by 2064
Abstract
To increase production efficiency of meat products, milk protein additives are often used. Despite a number of advantages, use of dairy ingredients involves a certain risk, namely the allergenic potential of milk proteins. A number of methods have been developed to detect milk-origin [...] Read more.
To increase production efficiency of meat products, milk protein additives are often used. Despite a number of advantages, use of dairy ingredients involves a certain risk, namely the allergenic potential of milk proteins. A number of methods have been developed to detect milk-origin raw materials in foodstuffs, including immunological reference methods. This study presents newly developed immunohistochemical (IHC) methods for casein detection in meat products. Casein was successfully detected directly in meat products where sensitivity was determined at 1.21 and specificity at 0.28. The results obtained from the IHC were compared with the Enzyme-Linked Immuno Sorbent Assay (ELISA) and there was no statistically significant difference between the IHC and ELISA methods (p > 0.05). The correspondence between the methods was 72% in total. The highest correspondence was reached in frankfurters (90%), the lowest in canned pâté (44%). Full article
(This article belongs to the Special Issue Advances in the Approach Food Allergy)
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11 pages, 1444 KiB  
Article
Oxidative Stability of Protease Treated Peanut with Reduced Allergenicity
by Jianmei Yu, Ivy N. Smith, Nadia Idris, Nicole Gregory and Nona Mikiashvili
Foods 2020, 9(6), 762; https://doi.org/10.3390/foods9060762 - 10 Jun 2020
Cited by 2 | Viewed by 2838
Abstract
Oxidative stability and allergenicity are two major concerns of peanuts. This study evaluated the impact of protease treatment of peanuts on its oxidative stability during storage. The raw and dry-roasted peanut kernels were hydrolyzed with Alcalase solution at pH 7.5 for 3 h. [...] Read more.
Oxidative stability and allergenicity are two major concerns of peanuts. This study evaluated the impact of protease treatment of peanuts on its oxidative stability during storage. The raw and dry-roasted peanut kernels were hydrolyzed with Alcalase solution at pH 7.5 for 3 h. The contents of Ara h 1, Ara h 2, and Ara h 6 in peanuts were determined before and after enzyme treatment by a sandwich ELISA. After drying, the samples were packed in eight amber glass jars and stored at 37 °C for 1–8 weeks. Controls are untreated raw and dry-roasted peanuts packed and stored in the same way as their treated counterparts. Samples were taken biweekly to determine peroxide value (PV) and thiobarbituric acid reactive substances (TBARS) as indicators of oxidation (n = 3), and to determine antioxidant activity. Alcalase treatment reduced intact major allergens Ara h 1, Ara h 2, and Ara h 6 by 100%, 99.8%, and 85%, respectively. The PVs of Alcalase-treated raw and roasted peanuts was lower than those of untreated (p < 0.05) over the 8-week storage. The TBARS of Alcalase-treated raw peanuts were slightly higher than that of untreated (p < 0.05), but the TBARS of Alcalase-treated dry-roasted peanuts were slightly but significantly lower than that of untreated (p < 0.05). The protease treatment increased the antioxidant activities including reducing power, DPPH free radical scavenging capacity, and metal chelating capacity of peanuts. Full article
(This article belongs to the Special Issue Advances in the Approach Food Allergy)
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14 pages, 2769 KiB  
Article
Allergenicity of Deamidated and/or Peptide-Bond-Hydrolyzed Wheat Gliadin by Transdermal Administration
by Ryosuke Abe, Narumi Matsukaze, Hayato Kobayashi, Yusuke Yamaguchi, Harumi Uto-Kondo, Hitoshi Kumagai and Hitomi Kumagai
Foods 2020, 9(5), 635; https://doi.org/10.3390/foods9050635 - 15 May 2020
Cited by 7 | Viewed by 3036
Abstract
Hydrochloric acid (HCl)-treated wheat protein (HWP) is widely used in various products, including foods, cosmetics and shampoos. Recently, immediate hypersensitivity towards facial soap containing HWP has been reported. HCl treatment of protein causes hydrolysis not only of main-chain amide bonds (peptide-bond hydrolysis) but [...] Read more.
Hydrochloric acid (HCl)-treated wheat protein (HWP) is widely used in various products, including foods, cosmetics and shampoos. Recently, immediate hypersensitivity towards facial soap containing HWP has been reported. HCl treatment of protein causes hydrolysis not only of main-chain amide bonds (peptide-bond hydrolysis) but also of side-chain ones (deamidation). We have already reported that gliadin, the main allergen in wheat, reduces allergenicity and increases digestibility by deamidation, indicating that deamidation and peptide-bond hydrolysis are effective to reduce the allergenicity of wheat protein. However, transdermally administered HWP is assumed to induce sensitization to orally administered wheat protein even in those who have been taking wheat products daily before sensitization. The present study was conducted to examine which structural change is responsible for the induction of cutaneous sensitization by comparing the allergenicity of deamidated and/or peptide-bond-hydrolyzed wheat gliadin. Because we have developed a deamidation method without causing peptide-bond hydrolysis, only deamidated wheat gliadin is available. Therefore, after deamidated-only, hydrolyzed-only, and deamidated and hydrolyzed gliadins were transdermally administered to mice for several weeks, the corresponding gliadin was intraperitoneally administered and allergenicity was evaluated. Transdermal administration of deamidated and hydrolyzed gliadin induced severe allergic reaction, while that of deamidated-only and hydrolyzed-only gliadin showed almost no allergic response. This result indicates that both deamidation and peptide-bond hydrolysis are necessary to increase the allergenic potency of transdermally administered wheat gliadin. Full article
(This article belongs to the Special Issue Advances in the Approach Food Allergy)
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15 pages, 1463 KiB  
Article
Use of IHF-QD Microscopic Analysis for the Detection of Food Allergenic Components: Peanuts and Wheat Protein
by Ludmila Kalčáková, Bohuslava Tremlová, Matej Pospiech, Martin Hostovský, Dani Dordević, Zdeňka Javůrková, Hana Běhalová and Marie Bartlová
Foods 2020, 9(2), 239; https://doi.org/10.3390/foods9020239 - 23 Feb 2020
Cited by 3 | Viewed by 3211
Abstract
The aim of the study was to analytically evaluate quantum dots in immunohistofluorescence (IHF-QD) microscopic imaging as detectors of food allergens—peanut and wheat. The experiment was designed as two in silico experiments or simulations: (a) models of pastry samples were prepared with the [...] Read more.
The aim of the study was to analytically evaluate quantum dots in immunohistofluorescence (IHF-QD) microscopic imaging as detectors of food allergens—peanut and wheat. The experiment was designed as two in silico experiments or simulations: (a) models of pastry samples were prepared with the addition of allergenic components (peanut and wheat protein components) and without the addition of allergenic components, and (b) positive and negative commercial samples underwent food allergen detection. The samples from both simulations were tested by the ELISA and IHF-QD microscopic methods. The primary antibodies (secondary antibodies to a rabbit Fc fragment with labeled CdSe/ZnS QD) were labelled at 525, 585, and 655 nm emissions. The use of quantum dots (QDs) has expanded to many science areas and they are also finding use in food allergen detection, as shown in the study. The study indicated that differences between the ELISA and IHF-QD microscopic methods were not observable among experimentally produced pastry samples with and without allergenic components, although differences were observed among commercial samples. The important value of the study is certainly the differences found in the application of different QD conjugates (525, 585, and 655). The highest contrast was found in the application of 585 QD conjugates that can serve for the possible quantification of present food allergens—peanuts and wheat. The study clearly emphasized that QD can be used for the qualitative detection of food allergens and can represent a reliable analytical method for food allergen detection in different food matrixes. Full article
(This article belongs to the Special Issue Advances in the Approach Food Allergy)
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8 pages, 1195 KiB  
Brief Report
Interaction of Monocyte-Derived Dendritic Cells with Ara h 2 from Raw and Roasted Peanuts
by Natalija Novak, Soheila J. Maleki, Carmen Cuadrado, Jesus F. Crespo and Beatriz Cabanillas
Foods 2020, 9(7), 863; https://doi.org/10.3390/foods9070863 - 02 Jul 2020
Cited by 5 | Viewed by 2482
Abstract
Ara h 2 is a relevant peanut allergen linked to severe allergic reactions. The interaction of Ara h 2 with components of the sensitization phase of food allergy (e.g., dendritic cells) has not been investigated, and could be key to understanding the allergenic [...] Read more.
Ara h 2 is a relevant peanut allergen linked to severe allergic reactions. The interaction of Ara h 2 with components of the sensitization phase of food allergy (e.g., dendritic cells) has not been investigated, and could be key to understanding the allergenic potential of this allergen. In this study, we aimed to analyze such interactions and the possible mechanism involved. Ara h 2 was purified from two forms of peanut, raw and roasted, and labeled with a fluorescent dye. Human monocyte-derived dendritic cells (MDDCs) were obtained, and experiments of Ara h 2 internalization by MDDCs were carried out. The role of the mannose receptor in the internalization of Ara h 2 from raw and roasted peanuts was also investigated. Results showed that Ara h 2 internalization by MDDCs was both time and dose dependent. Mannose receptors in MDDCs had a greater implication in the internalization of Ara h 2 from roasted peanuts. However, this receptor was also important in the internalization of Ara h 2 from raw peanuts, as opposed to other allergens such as raw Ara h 3. Full article
(This article belongs to the Special Issue Advances in the Approach Food Allergy)
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