Article (Scientific journals)
Acid Hydrolysis of Gluten Enhances the Skin Sensitizing Potential and Drives Diversification of IgE Reactivity to Unmodified Gluten Proteins.
Ballegaard, Anne-Sofie Ravn; Castan, Laure; Larsen, Jeppe Madura et al.
2021In Molecular Nutrition and Food Research, 65 (23), p. 2100416
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Keywords :
Allergens; Immunoglobulin E; Glutens; Animals; Glutens/chemistry; Hydrolysis; Rats; Wheat Hypersensitivity; Brown Norway rats; deamidation; hydrolysis; skin sensitization; wheat allergy
Abstract :
[en] SCOPE: Personal care products containing hydrolyzed gluten have been linked to spontaneous sensitization through the skin, however the impact of the hydrolysate characteristics on the sensitizing capacity is generally unknown. METHODS AND RESULTS: The physicochemical properties of five different wheat-derived gluten products (one unmodified, one enzyme hydrolyzed, and three acid hydrolyzed) are investigated, and the skin sensitizing capacity is determined in allergy-prone Brown Norway rats. Acid hydrolyzed gluten products exhibited the strongest intrinsic sensitizing capacity via the skin. All hydrolyzed gluten products induced cross-reactivity to unmodified gluten in the absence of oral tolerance to wheat, but were unable to break tolerance in animals on a wheat-containing diet. Still, the degree of deamidation in acid hydrolyzed products is associated with product-specific sensitization in wheat tolerant rats. Sensitization to acid hydrolyzed gluten products is associated with a more diverse IgE reactivity profile to unmodified gluten proteins compared to sensitization induced by unmodified gluten or enzyme hydrolyzed gluten. CONCLUSION: Acid hydrolysis enhances the skin sensitizing capacity of gluten and drives IgE reactivity to more gluten proteins. This property of acid hydrolyzed gluten may be related to the degree of product deamidation, and could be a strong trigger of wheat allergy in susceptible individuals.
Disciplines :
Life sciences: Multidisciplinary, general & others
Author, co-author :
Ballegaard, Anne-Sofie Ravn;  National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.
Castan, Laure;  INRAE BIA UR1268, Nantes, 44316, France. ; Institut du thorax, INSERM CNRS, UNIV Nantes, Nantes, 44000, France.
Larsen, Jeppe Madura;  National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.
Piras, Cristian;  Department of Health Sciences, University Magna Graecia of Catanzaro, Catanzaro, 88100, Italy.
Villemin, Clélia;  INRAE BIA UR1268, Nantes, 44316, France.
Andersen, Daniel;  Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.
Madsen, Charlotte Bernhard;  National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.
Roncada, Paola;  Department of Health Sciences, University Magna Graecia of Catanzaro, Catanzaro, 88100, Italy.
Brix, Susanne ;  Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.
Denery-Papini, Sandra;  INRAE BIA UR1268, Nantes, 44316, France.
Mazzucchelli, Gabriel  ;  Université de Liège - ULiège > Département de chimie (sciences) > Laboratoire de spectrométrie de masse (L.S.M.)
Bouchaud, Grégory;  INRAE BIA UR1268, Nantes, 44316, France.
Bøgh, Katrine Lindholm ;  National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.
More authors (3 more) Less
Language :
English
Title :
Acid Hydrolysis of Gluten Enhances the Skin Sensitizing Potential and Drives Diversification of IgE Reactivity to Unmodified Gluten Proteins.
Publication date :
December 2021
Journal title :
Molecular Nutrition and Food Research
ISSN :
1613-4125
eISSN :
1613-4133
Publisher :
John Wiley & Sons, Gb
Volume :
65
Issue :
23
Pages :
e2100416
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
© 2021 Wiley-VCH GmbH.
Available on ORBi :
since 12 October 2025

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