6533b824fe1ef96bd1280887
RESEARCH PRODUCT
Identification of Novel Phosphopeptides After Simulated Digestion of αs2-casein by Tandem Mass Spectrometry
Esther MiquelRosaura FarréAmparo AlegríaReyes Barberásubject
0301 basic medicineElectrosprayChromatography030102 biochemistry & molecular biologyMolecular massChemistryPhosphopeptideGeneral Chemical EngineeringMass spectrometryTandem mass spectrometryHigh-performance liquid chromatographyIndustrial and Manufacturing Engineering03 medical and health sciences030104 developmental biologyBiochemistryCaseinDigestionFood Sciencedescription
Casein phosphopeptides (CPPs) are encrypted in αs1-, αs2-and β-casein (CN) and can be released by in vitro, in vivohydrolysis or food processing of dairy foods. Bovine αs2-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 αs2-casein (αs2-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 αs2-CN derived CPPs, Three of them (αs2-CN(54–87)4P,αs2-CN(24–70)4P and αs2-CN(14–73)5P) with the mineral binding cluster sequence SpSpSpEE were identified and characterised. CPPs from αs2-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 αs2-CN derived CPPs could be promising candidates for incorporation to mineral fortified foods as functional ingredients.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2006-12-01 | Food Science and Technology International |