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Profiling of Multiphosphorylated Peptides in Kefir and Their Release During Simulated Gastrointestinal Digestion
[Image: see text] Casein phosphopeptides are multiphosphorylated milk peptides, which can have anticariogenic activity and improve mineral absorption by binding bivalent metal ions. The present study investigated phosphopeptides in kefir because fermentation may lead to their enhanced release from m...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6545566/ https://www.ncbi.nlm.nih.gov/pubmed/31172034 http://dx.doi.org/10.1021/acsomega.8b03105 |
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author | Savastano, Maria Luisa Liu, Yufang Mels, Jennifer Dittrich, Daniel Haus, Sabrina Gensberger-Reigl, Sabrina Pischetsrieder, Monika |
author_facet | Savastano, Maria Luisa Liu, Yufang Mels, Jennifer Dittrich, Daniel Haus, Sabrina Gensberger-Reigl, Sabrina Pischetsrieder, Monika |
author_sort | Savastano, Maria Luisa |
collection | PubMed |
description | [Image: see text] Casein phosphopeptides are multiphosphorylated milk peptides, which can have anticariogenic activity and improve mineral absorption by binding bivalent metal ions. The present study investigated phosphopeptides in kefir because fermentation may lead to their enhanced release from milk proteins. After selective enrichment by hydroxyapatite extraction, phosphopeptides and their phosphorylation degree were identified by matrix-assisted desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) before and after enzymatic dephosphorylation. Peptide structures were determined by ultrahigh-performance liquid chromatography coupled to electrospray ionization tandem mass spectrometry (UHPLC–ESI–MS/MS) revealing 27 phosphopeptides in kefir, including nine peptides containing the motif pSpSpSEE, which binds minerals most efficiently. The majority (18) of phosphopeptides were derived from β-casein, but only three were derived from the most abundant milk protein α(s1)-casein. After simulated gastrointestinal digestion, MALDI-TOF-MS analysis detected eight putative phosphopeptides in kefir, four of which were assigned by UHPLC–ESI–MS/MS to α(s2)-casein(124–133), α(s2)-casein(137–146), β-casein(30–40), and κ-casein(147–161). These results indicate that kefir is a good dietary source of multiphosphorylated peptides. |
format | Online Article Text |
id | pubmed-6545566 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-65455662019-06-04 Profiling of Multiphosphorylated Peptides in Kefir and Their Release During Simulated Gastrointestinal Digestion Savastano, Maria Luisa Liu, Yufang Mels, Jennifer Dittrich, Daniel Haus, Sabrina Gensberger-Reigl, Sabrina Pischetsrieder, Monika ACS Omega [Image: see text] Casein phosphopeptides are multiphosphorylated milk peptides, which can have anticariogenic activity and improve mineral absorption by binding bivalent metal ions. The present study investigated phosphopeptides in kefir because fermentation may lead to their enhanced release from milk proteins. After selective enrichment by hydroxyapatite extraction, phosphopeptides and their phosphorylation degree were identified by matrix-assisted desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) before and after enzymatic dephosphorylation. Peptide structures were determined by ultrahigh-performance liquid chromatography coupled to electrospray ionization tandem mass spectrometry (UHPLC–ESI–MS/MS) revealing 27 phosphopeptides in kefir, including nine peptides containing the motif pSpSpSEE, which binds minerals most efficiently. The majority (18) of phosphopeptides were derived from β-casein, but only three were derived from the most abundant milk protein α(s1)-casein. After simulated gastrointestinal digestion, MALDI-TOF-MS analysis detected eight putative phosphopeptides in kefir, four of which were assigned by UHPLC–ESI–MS/MS to α(s2)-casein(124–133), α(s2)-casein(137–146), β-casein(30–40), and κ-casein(147–161). These results indicate that kefir is a good dietary source of multiphosphorylated peptides. American Chemical Society 2019-05-01 /pmc/articles/PMC6545566/ /pubmed/31172034 http://dx.doi.org/10.1021/acsomega.8b03105 Text en Copyright © 2019 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes. |
spellingShingle | Savastano, Maria Luisa Liu, Yufang Mels, Jennifer Dittrich, Daniel Haus, Sabrina Gensberger-Reigl, Sabrina Pischetsrieder, Monika Profiling of Multiphosphorylated Peptides in Kefir and Their Release During Simulated Gastrointestinal Digestion |
title | Profiling of Multiphosphorylated Peptides in Kefir
and Their Release During Simulated Gastrointestinal Digestion |
title_full | Profiling of Multiphosphorylated Peptides in Kefir
and Their Release During Simulated Gastrointestinal Digestion |
title_fullStr | Profiling of Multiphosphorylated Peptides in Kefir
and Their Release During Simulated Gastrointestinal Digestion |
title_full_unstemmed | Profiling of Multiphosphorylated Peptides in Kefir
and Their Release During Simulated Gastrointestinal Digestion |
title_short | Profiling of Multiphosphorylated Peptides in Kefir
and Their Release During Simulated Gastrointestinal Digestion |
title_sort | profiling of multiphosphorylated peptides in kefir
and their release during simulated gastrointestinal digestion |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6545566/ https://www.ncbi.nlm.nih.gov/pubmed/31172034 http://dx.doi.org/10.1021/acsomega.8b03105 |
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