Impact of Food Matrices on Digestibility of Allergens and Poorly Allergenic Homologs
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Le résumé fourni par la source
Background: Protease resistance is considered a risk factor for allergenicity of proteins, although the correlation is low. It is nonetheless a part of the weight-of-evidence approach, proposed by Codex, for assessing the allergenicity risk of novel food proteins. Susceptibility of proteins to pepsin is commonly tested with purified protein in solution. Objective: Food proteins are rarely consumed in purified form. Our aim was to evaluate the impact of experimental and endogenous food matrices on protease susceptibility of homologous protein pairs with different degrees of allergenicity. Methods: Porcine and shrimp tropomyosin (ST) were subjected to sequential exposure to amylase, pepsin, and pancreatin in their respective endogenous matrix (pork tenderloin/boiled shrimp) and in three different experimental matrices (dessert mousse [DM], soy milk [SM], and chocolate bar [CB]). Digestion was monitored by immunoblotting using tropomyosin-specific antibodies. Recombinant peach and strawberry lipid transfer protein were biotinylated, spiked into both peach and strawberry fruit pulp, and subjected to the same sequential digestion protocol. Digestion was monitored by immunoblotting using streptavidin for detection. Results: Chocolate bar, and to a lesser extent SM, had a clear protective effect against pepsin digestion of porcine tropomyosin (PT) and to a lesser extent of ST. Increased resistance was associated with increased protein content. Spiking experiments with bovine serum albumin (BSA) confirmed the protective effect of a protein-rich matrix. The two tropomyosins were both highly resistant to pepsin in their protein-rich and lean native food matrix. Pancreatin digestion remained rapid and complete, independent of the matrix. The fat-rich environment did not transfer protection against pepsin digestion. Spiking of recombinant peach and strawberry lipid transfer proteins into peach and strawberry pulp did not reveal any differential protective effect that could explain differences in allergenicity of both fruits. Conclusions: Protein-rich food matrices delay pepsin digestion by saturating the protease. This effect is most apparent for proteins that are highly pepsin susceptible in solution. The inclusion of food matrices does not help in understanding why some proteins are strong primary sensitizers while homologs are very poor allergens. Although for induction of symptoms in food allergic patients (elicitation), a protein-rich food matrix that may contribute to increased risk, our results indicate that the inclusion of food matrices in the weight-of-evidence approach for estimating the potential risks of novel proteins to become allergens (sensitization), is most likely of very limited value.
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Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- Impact of Food Matrices on Digestibility of Allergens and Poorly Allergenic Homologs
- Date Crossref
- 31/05/2022
- Éditeur
- Frontiers Media SA
- Type
- journal-article
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Où se fait cette recherche
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Amsterdam University Medical Centers Department of Experimental Immunology pays non établi dans la noticeÉtablissement de santé
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Children's Hospital of Philadelphia pays non établi dans la noticeOrganisme public
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BASF (United States) pays non établi dans la noticeEntreprise
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Environmental Protection Agency pays non établi dans la noticeOrganisme public
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Wilmington University pays non établi dans la noticeUniversité ou école supérieure
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Syngenta (United States) pays non établi dans la noticeEntreprise
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Gentofte Hospital pays non établi dans la noticeÉtablissement de santé
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Bayer (United States) pays non établi dans la noticeEntreprise
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Health and Environmental Sciences Institute pays non établi dans la noticeOrganisation à but non lucratif
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BASF Corporation pays non établi dans la noticeInstitution
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US EPA pays non établi dans la noticeInstitution
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Dupont Nutrition and Biosciences pays non établi dans la noticeInstitution
Department of Experimental Immunology — Amsterdam University Medical Centers, Children's Hospital of Philadelphia et BASF (United States), avec 9 autres affiliations.
Une affiliation ne permet pas de déduire la nationalité d’un auteur.