Oxidative modification of a proline-rich gliadin peptide

Xin Huang, Päivi Kanerva, Hannu Salovaara, Jussi Loponen, Tuula Sontag-Strohm

Research output: Contribution to journalArticleScientificpeer-review

Abstract

Prolamins are proline-rich proteins occurring in cereal grains. Prolamins of wheat, barley and rye, or gluten protein, can cause coeliac disease in individuals not tolerating gluten. Degrading harmful prolamins can reduce their toxicity. A model peptide sequenced in α-gliadin, 33-mer (LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF), was chosen for our study. The metal-catalysed oxidation of 33-mer was studied, instead of enzymatic hydrolysis. Peptide 33-mer was treated in several oxidative systems. Iron-catalysed hydrogen peroxide-induced oxidation showed the greatest modification of 33-mer. Carbonyl groups and dityrosine cross-links were readily formed. At best, the immunological activity of 33-mer was reduced to 18% of its initial level after 24 h of oxidation. Oxidative treatment can be further applied for the modification of cereal prolamin proteins, since it appears to be a potential alternative for reduction of coeliac immunological activities in gluten proteins.
Original languageEnglish
JournalFood Chemistry
Volume141
Issue number3
Pages (from-to)2011-2016
Number of pages6
ISSN0308-8146
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 416 Food Science
  • protein oxidation
  • proline
  • Degradation
  • ELISA
  • Fenton reaction
  • Coeliac disease
  • Dityrosine

Cite this

Huang, Xin ; Kanerva, Päivi ; Salovaara, Hannu ; Loponen, Jussi ; Sontag-Strohm, Tuula. / Oxidative modification of a proline-rich gliadin peptide. In: Food Chemistry. 2013 ; Vol. 141, No. 3. pp. 2011-2016.
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title = "Oxidative modification of a proline-rich gliadin peptide",
abstract = "Prolamins are proline-rich proteins occurring in cereal grains. Prolamins of wheat, barley and rye, or gluten protein, can cause coeliac disease in individuals not tolerating gluten. Degrading harmful prolamins can reduce their toxicity. A model peptide sequenced in α-gliadin, 33-mer (LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF), was chosen for our study. The metal-catalysed oxidation of 33-mer was studied, instead of enzymatic hydrolysis. Peptide 33-mer was treated in several oxidative systems. Iron-catalysed hydrogen peroxide-induced oxidation showed the greatest modification of 33-mer. Carbonyl groups and dityrosine cross-links were readily formed. At best, the immunological activity of 33-mer was reduced to 18{\%} of its initial level after 24 h of oxidation. Oxidative treatment can be further applied for the modification of cereal prolamin proteins, since it appears to be a potential alternative for reduction of coeliac immunological activities in gluten proteins.",
keywords = "416 Food Science, protein oxidation, proline, Degradation, ELISA, Fenton reaction, Coeliac disease, Dityrosine",
author = "Xin Huang and P{\"a}ivi Kanerva and Hannu Salovaara and Jussi Loponen and Tuula Sontag-Strohm",
year = "2013",
doi = "10.1016/j.foodchem.2013.05.066",
language = "English",
volume = "141",
pages = "2011--2016",
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Oxidative modification of a proline-rich gliadin peptide. / Huang, Xin; Kanerva, Päivi; Salovaara, Hannu; Loponen, Jussi; Sontag-Strohm, Tuula.

In: Food Chemistry, Vol. 141, No. 3, 2013, p. 2011-2016.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Oxidative modification of a proline-rich gliadin peptide

AU - Huang, Xin

AU - Kanerva, Päivi

AU - Salovaara, Hannu

AU - Loponen, Jussi

AU - Sontag-Strohm, Tuula

PY - 2013

Y1 - 2013

N2 - Prolamins are proline-rich proteins occurring in cereal grains. Prolamins of wheat, barley and rye, or gluten protein, can cause coeliac disease in individuals not tolerating gluten. Degrading harmful prolamins can reduce their toxicity. A model peptide sequenced in α-gliadin, 33-mer (LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF), was chosen for our study. The metal-catalysed oxidation of 33-mer was studied, instead of enzymatic hydrolysis. Peptide 33-mer was treated in several oxidative systems. Iron-catalysed hydrogen peroxide-induced oxidation showed the greatest modification of 33-mer. Carbonyl groups and dityrosine cross-links were readily formed. At best, the immunological activity of 33-mer was reduced to 18% of its initial level after 24 h of oxidation. Oxidative treatment can be further applied for the modification of cereal prolamin proteins, since it appears to be a potential alternative for reduction of coeliac immunological activities in gluten proteins.

AB - Prolamins are proline-rich proteins occurring in cereal grains. Prolamins of wheat, barley and rye, or gluten protein, can cause coeliac disease in individuals not tolerating gluten. Degrading harmful prolamins can reduce their toxicity. A model peptide sequenced in α-gliadin, 33-mer (LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF), was chosen for our study. The metal-catalysed oxidation of 33-mer was studied, instead of enzymatic hydrolysis. Peptide 33-mer was treated in several oxidative systems. Iron-catalysed hydrogen peroxide-induced oxidation showed the greatest modification of 33-mer. Carbonyl groups and dityrosine cross-links were readily formed. At best, the immunological activity of 33-mer was reduced to 18% of its initial level after 24 h of oxidation. Oxidative treatment can be further applied for the modification of cereal prolamin proteins, since it appears to be a potential alternative for reduction of coeliac immunological activities in gluten proteins.

KW - 416 Food Science

KW - protein oxidation

KW - proline

KW - Degradation

KW - ELISA

KW - Fenton reaction

KW - Coeliac disease

KW - Dityrosine

U2 - 10.1016/j.foodchem.2013.05.066

DO - 10.1016/j.foodchem.2013.05.066

M3 - Article

VL - 141

SP - 2011

EP - 2016

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

IS - 3

ER -