Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing

E.L. van Boxtel, S.J. Koppelman, L.A.M. van den Broek, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

8 Citations (Scopus)

Abstract

Ber e 1, a major allergen from Brazil nuts, is very stable to in vitro peptic digestion. As heat-induced denaturation may affect protein digestibility, the denaturation behaviour of Ber e 1 was investigated. The denaturation temperature of Ber e 1 varies from approximately 80¿110 °C, depending on the pH. Upon heating above its denaturation temperature at pH 7.0, the protein partly forms insoluble aggregates and partly dissociates into its polypeptides, whereas heating at pH 5.0 does neither induce aggregation, nor dissociation of the protein. The denaturation temperature of approximately 110 °C at pH values corresponding to the general pH values of foods (pH 5¿7) is very high and is expected to be even higher in Brazil nuts themselves. As a result, it is unlikely that heat processing causes the denaturation of all Ber e 1 present in food products. Consequently, the allergen is assumed to be consumed (mainly) in its native form, having a high stability towards pepsin digestion
Original languageEnglish
Pages (from-to)904-908
JournalFood Chemistry
Volume110
Issue number4
DOIs
Publication statusPublished - 2008

Fingerprint

Bertholletia
Brazil nuts
Food processing
Food Handling
Denaturation
allergens
denaturation
food processing
Allergens
Hot Temperature
heat
Digestion
Heating
Temperature
digestion
Protein Denaturation
Food
temperature
Proteins
in vitro digestion

Keywords

  • major allergen
  • in-vitro
  • digestion
  • protein
  • stabilization
  • stability
  • products
  • peanut

Cite this

van Boxtel, E.L. ; Koppelman, S.J. ; van den Broek, L.A.M. ; Gruppen, H. / Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing. In: Food Chemistry. 2008 ; Vol. 110, No. 4. pp. 904-908.
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title = "Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing",
abstract = "Ber e 1, a major allergen from Brazil nuts, is very stable to in vitro peptic digestion. As heat-induced denaturation may affect protein digestibility, the denaturation behaviour of Ber e 1 was investigated. The denaturation temperature of Ber e 1 varies from approximately 80¿110 °C, depending on the pH. Upon heating above its denaturation temperature at pH 7.0, the protein partly forms insoluble aggregates and partly dissociates into its polypeptides, whereas heating at pH 5.0 does neither induce aggregation, nor dissociation of the protein. The denaturation temperature of approximately 110 °C at pH values corresponding to the general pH values of foods (pH 5¿7) is very high and is expected to be even higher in Brazil nuts themselves. As a result, it is unlikely that heat processing causes the denaturation of all Ber e 1 present in food products. Consequently, the allergen is assumed to be consumed (mainly) in its native form, having a high stability towards pepsin digestion",
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author = "{van Boxtel}, E.L. and S.J. Koppelman and {van den Broek}, L.A.M. and H. Gruppen",
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Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing. / van Boxtel, E.L.; Koppelman, S.J.; van den Broek, L.A.M.; Gruppen, H.

In: Food Chemistry, Vol. 110, No. 4, 2008, p. 904-908.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing

AU - van Boxtel, E.L.

AU - Koppelman, S.J.

AU - van den Broek, L.A.M.

AU - Gruppen, H.

PY - 2008

Y1 - 2008

N2 - Ber e 1, a major allergen from Brazil nuts, is very stable to in vitro peptic digestion. As heat-induced denaturation may affect protein digestibility, the denaturation behaviour of Ber e 1 was investigated. The denaturation temperature of Ber e 1 varies from approximately 80¿110 °C, depending on the pH. Upon heating above its denaturation temperature at pH 7.0, the protein partly forms insoluble aggregates and partly dissociates into its polypeptides, whereas heating at pH 5.0 does neither induce aggregation, nor dissociation of the protein. The denaturation temperature of approximately 110 °C at pH values corresponding to the general pH values of foods (pH 5¿7) is very high and is expected to be even higher in Brazil nuts themselves. As a result, it is unlikely that heat processing causes the denaturation of all Ber e 1 present in food products. Consequently, the allergen is assumed to be consumed (mainly) in its native form, having a high stability towards pepsin digestion

AB - Ber e 1, a major allergen from Brazil nuts, is very stable to in vitro peptic digestion. As heat-induced denaturation may affect protein digestibility, the denaturation behaviour of Ber e 1 was investigated. The denaturation temperature of Ber e 1 varies from approximately 80¿110 °C, depending on the pH. Upon heating above its denaturation temperature at pH 7.0, the protein partly forms insoluble aggregates and partly dissociates into its polypeptides, whereas heating at pH 5.0 does neither induce aggregation, nor dissociation of the protein. The denaturation temperature of approximately 110 °C at pH values corresponding to the general pH values of foods (pH 5¿7) is very high and is expected to be even higher in Brazil nuts themselves. As a result, it is unlikely that heat processing causes the denaturation of all Ber e 1 present in food products. Consequently, the allergen is assumed to be consumed (mainly) in its native form, having a high stability towards pepsin digestion

KW - major allergen

KW - in-vitro

KW - digestion

KW - protein

KW - stabilization

KW - stability

KW - products

KW - peanut

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JO - Food Chemistry

JF - Food Chemistry

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