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Food Science and Technology International
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Identification of Novel Phosphopeptides After Simulated Digestion of {alpha}s2-casein by Tandem Mass Spectrometry

E. Miquel

A. Alegría

R. Barberá

Nutrition and Food Chemistry, Faculty of Pharmacy, University of Valencia. Av. Vicent Andrés Estellés s/n, 46100–Burjassot, Valencia, Spain

R. Farré

CESNID Recinte Torribera–La Masia, 08921 Santa Coloma de Gramanet, Barcelona, Spain; rfarre{at}cesnid.es

Casein phosphopeptides (CPPs) are encrypted in {alpha}s1-, {alpha}s2-and ß-casein (CN) and can be released by in vitro, in vivohydrolysis or food processing of dairy foods. Bovine {alpha}s2-CN contains two cluster sequences of anionic phosphoseryl and glutamyl residues SpSpSpEE in its structure (residues 8–12 and 56–63), which can modulate mineral bioavailability. In this study {alpha}s2-casein ({alpha}s2-CN) was subjected to simulated gastrointestinal digestion. CPPs released were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation tandem mass spectrometry (RP-HPLC-ESIMS/MS). Six novel {alpha}s2-CN derived CPPs, Three of them ({alpha}s2-CN(54–87)4P,{alpha}s2-CN(24–70)4P and {alpha}s2-CN(14–73)5P) with the mineral binding cluster sequence SpSpSpEE were identified and characterised. CPPs from {alpha}s2-CN identified in this study resist simulated gastrointestinal digestion. As the molecular weights of these CPPs are approx. 2,165–7,112Da, they could be absorbed by intestinal cells. Consequently, these {alpha}s2-CN derived CPPs could be promising candidates for incorporation to mineral fortified foods as functional ingredients.

Key Words: {alpha}s2-casein • casein phosphopeptides • mineral bioavailability • identification

Food Science and Technology International, Vol. 12, No. 6, 531-537 (2006)
DOI: 10.1177/1082013206072906
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