Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy

J. Radosavljevic, Emilia Nordlund, L. Mihajlovic, M. Krstic, T. Bohn, Johanna Buchert, T.C. Velickovic (Corresponding Author), J. Smit

Research output: Contribution to journalArticleScientificpeer-review

22 Citations (Scopus)

Abstract

Scope

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.

Methods and 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.

Conclusion

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.
Original languageEnglish
Pages (from-to)635-646
Number of pages12
JournalMolecular Nutrition and Food Research
Volume58
Issue number3
DOIs
Publication statusPublished - 2014
MoE publication typeA1 Journal article-refereed

Fingerprint

Peanut Hypersensitivity
peanut protein
hypersensitivity
peanuts
animal models
crosslinking
bioavailability
allergens
Proteins
Monophenol Monooxygenase
proteins
dietary protein
Biological Availability
Dietary Proteins
Trichoderma reesei
allergenicity
Agaricus bisporus
enzymatic treatment
protein aggregates
fluorescein

Keywords

  • allergenicity
  • peanut
  • protein cross-linking
  • tyrosinase

Cite this

Radosavljevic, J. ; Nordlund, Emilia ; Mihajlovic, L. ; Krstic, M. ; Bohn, T. ; Buchert, Johanna ; Velickovic, T.C. ; Smit, J. / Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. In: Molecular Nutrition and Food Research. 2014 ; Vol. 58, No. 3. pp. 635-646.
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title = "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy",
abstract = "ScopeThe 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.Methods and resultsThe 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.ConclusionEnzymatic 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.",
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Radosavljevic, J, Nordlund, E, Mihajlovic, L, Krstic, M, Bohn, T, Buchert, J, Velickovic, TC & Smit, J 2014, 'Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy', Molecular Nutrition and Food Research, vol. 58, no. 3, pp. 635-646. https://doi.org/10.1002/mnfr.201300403

Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. / Radosavljevic, J.; Nordlund, Emilia; Mihajlovic, L.; Krstic, M.; Bohn, T.; Buchert, Johanna; Velickovic, T.C. (Corresponding Author); Smit, J.

In: Molecular Nutrition and Food Research, Vol. 58, No. 3, 2014, p. 635-646.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy

AU - Radosavljevic, J.

AU - Nordlund, Emilia

AU - Mihajlovic, L.

AU - Krstic, M.

AU - Bohn, T.

AU - Buchert, Johanna

AU - Velickovic, T.C.

AU - Smit, J.

PY - 2014

Y1 - 2014

N2 - ScopeThe 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.Methods and resultsThe 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.ConclusionEnzymatic 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.

AB - ScopeThe 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.Methods and resultsThe 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.ConclusionEnzymatic 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.

KW - allergenicity

KW - peanut

KW - protein cross-linking

KW - tyrosinase

U2 - 10.1002/mnfr.201300403

DO - 10.1002/mnfr.201300403

M3 - Article

VL - 58

SP - 635

EP - 646

JO - Molecular Nutrition and Food Research

JF - Molecular Nutrition and Food Research

SN - 1613-4125

IS - 3

ER -