title: Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy.
abstract: METHODS
  The cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated.
  
  
  RESULTS
  The impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE.
  
  
  CONCLUSIONS
  Enzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.
authors.affiliation: University of Belgrade, Faculty of Chemistry, Belgrade, Serbia.
authors.forename: Jelena
authors.initials: J
authors.lastname: Radosavljevic
authors.forename: Emilia
authors.initials: E
authors.lastname: Nordlund
authors.forename: Luka
authors.initials: L
authors.lastname: Mihajlovic
authors.forename: Maja
authors.initials: M
authors.lastname: Krstic
authors.forename: Torsten
authors.initials: T
authors.lastname: Bohn
authors.forename: Johanna
authors.initials: J
authors.lastname: Buchert
authors.forename: Tanja Cirkovic
authors.initials: TC
authors.lastname: Velickovic
authors.forename: Joost
authors.initials: J
authors.lastname: Smit
mesh_terms: D055516:2S Albumins, Plant / Q000378:metabolism; D000818:Animals; D052179:Antigens, Plant / Q000378:metabolism; D010367:Arachis / Q000276:immunology*; D001682:Biological Availability; D018938:Caco-2 Cells; D003432:Cross-Linking Reagents / Q000737:chemistry; D004195:Disease Models, Animal; D000939:Epitopes / Q000378:metabolism; D005260:Female; D005511:Food Handling; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D007114:Immunization; D007073:Immunoglobulin E / Q000378:metabolism; D008809:Mice, Inbred C3H; D014442:Monophenol Monooxygenase / Q000737:chemistry; D021183:Peanut Hypersensitivity / Q000276:immunology*; D010940:Plant Proteins / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism / Q000493:pharmacokinetics
chemical_list: D055516:2S Albumins, Plant; D052179:Antigens, Plant; C500890:Ara h 2 allergen, Arachis hypogaea; C492737:Ara h 6 allergen, Arachis hypogaea; D003432:Cross-Linking Reagents; D000939:Epitopes; D006023:Glycoproteins; D010940:Plant Proteins; D007073:Immunoglobulin E; D014442:Monophenol Monooxygenase
keywords: Allergenicity; Peanut; Protein cross-linking; Tyrosinase