Journal
FOOD CHEMISTRY
Volume 214, Issue -, Pages 597-605Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2016.07.108
Keywords
Barley; Hordein; Proline oxidation; Proline; Gluten-free; Metal-catalyzed oxidation; Prolamin
Funding
- Finnish Food and Drink Industries' Federation
- Finnish Coeliac Society
- University of Helsinki
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Elimination of celiac-toxic prolamin peptides and proteins is essential for Triticeae products to be gluten-free. Instead of enzymatic hydrolysis, in this study we investigated metal-catalyzed oxidation of two model peptides, QQPFP, and PQPQLPY, together with a hordein isolate from barley (Hordeum vulgare L.). We established a multiple reaction monitoring (MRM) LC-MS method to detect and quantify proline oxidation fragments. In addition to fragmentation, aggregation and side chain modifications were identified, including free thiol loss, carbonyl formation, and dityrosine formation. The immunoreactivity of the oxidized hordein isolate was considerably decreased in all metal-catalyzed oxidation systems. Cleavage of peptides or protein fragments at the numerous proline residues partially accounts for the decrease. Metal-catalyzed oxidation can thus be used in the modification and elimination of celiac-toxic peptides and proteins. (C) 2016 Elsevier Ltd. All rights reserved.
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