Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics
The aim of this paper was the development of an analytical strategy for the production of purified bioactive peptides from cauliflower waste proteins, by testing two different extraction protocols and screening different enzymes for protein hydrolysis. The purification of peptides was carried out by...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2016-12-01
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| Series: | Journal of Functional Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464616302869 |
| _version_ | 1828962615577018368 |
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| author | Riccardo Zenezini Chiozzi Anna Laura Capriotti Chiara Cavaliere Giorgia La Barbera Susy Piovesana Aldo Laganà |
| author_facet | Riccardo Zenezini Chiozzi Anna Laura Capriotti Chiara Cavaliere Giorgia La Barbera Susy Piovesana Aldo Laganà |
| author_sort | Riccardo Zenezini Chiozzi |
| collection | DOAJ |
| description | The aim of this paper was the development of an analytical strategy for the production of purified bioactive peptides from cauliflower waste proteins, by testing two different extraction protocols and screening different enzymes for protein hydrolysis. The purification of peptides was carried out by multidimensional liquid chromatography employing reversed phase chromatography and hydrophilic interaction chromatography; the resulting fractions were tested for antihypertensive and antioxidative activities. The most active ones were characterized by nano-liquid chromatography-tandem mass spectrometry and identified by database search. The identified peptides were further mined by in-silico analysis using PeptideRanker to ascribe a bioactivity rank to each peptide. Thus, six potential ACE-inhibitory peptides were synthesized and validated checking their retention times and fragmentation patterns for consistency. Pure peptide standards were finally in-vitro tested for the specific bioactivity. In this way, three novel ACE-inhibitory peptides were successfully identified and validated from cauliflower waste hydrolysate, showing good IC50 values. |
| first_indexed | 2024-12-14T10:07:32Z |
| format | Article |
| id | doaj.art-ce9fcdfdc0544c709e10ab93eaebabc8 |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-14T10:07:32Z |
| publishDate | 2016-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-ce9fcdfdc0544c709e10ab93eaebabc82022-12-21T23:07:05ZengElsevierJournal of Functional Foods1756-46462016-12-0127262273Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformaticsRiccardo Zenezini Chiozzi0Anna Laura Capriotti1Chiara Cavaliere2Giorgia La Barbera3Susy Piovesana4Aldo Laganà5Dipartimento di Chimica, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Rome, ItalyCorresponding author: Dipartimento di Chimica, Sapienza Università di Roma, Box no 34 - Roma 62, Piazzale Aldo Moro 5, 00185 Rome, Italy. Fax: +39 06 4906 31.; Dipartimento di Chimica, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Rome, ItalyDipartimento di Chimica, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Rome, ItalyDipartimento di Chimica, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Rome, ItalyDipartimento di Chimica, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Rome, ItalyDipartimento di Chimica, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Rome, ItalyThe aim of this paper was the development of an analytical strategy for the production of purified bioactive peptides from cauliflower waste proteins, by testing two different extraction protocols and screening different enzymes for protein hydrolysis. The purification of peptides was carried out by multidimensional liquid chromatography employing reversed phase chromatography and hydrophilic interaction chromatography; the resulting fractions were tested for antihypertensive and antioxidative activities. The most active ones were characterized by nano-liquid chromatography-tandem mass spectrometry and identified by database search. The identified peptides were further mined by in-silico analysis using PeptideRanker to ascribe a bioactivity rank to each peptide. Thus, six potential ACE-inhibitory peptides were synthesized and validated checking their retention times and fragmentation patterns for consistency. Pure peptide standards were finally in-vitro tested for the specific bioactivity. In this way, three novel ACE-inhibitory peptides were successfully identified and validated from cauliflower waste hydrolysate, showing good IC50 values.http://www.sciencedirect.com/science/article/pii/S1756464616302869ACE-inhibitory peptidesCauliflower by-productsOff-line multidimensional dimensional chromatographyHigh resolution mass spectrometryBioinformatic tools |
| spellingShingle | Riccardo Zenezini Chiozzi Anna Laura Capriotti Chiara Cavaliere Giorgia La Barbera Susy Piovesana Aldo Laganà Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics Journal of Functional Foods ACE-inhibitory peptides Cauliflower by-products Off-line multidimensional dimensional chromatography High resolution mass spectrometry Bioinformatic tools |
| title | Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics |
| title_full | Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics |
| title_fullStr | Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics |
| title_full_unstemmed | Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics |
| title_short | Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics |
| title_sort | identification of three novel angiotensin converting enzyme inhibitory peptides derived from cauliflower by products by multidimensional liquid chromatography and bioinformatics |
| topic | ACE-inhibitory peptides Cauliflower by-products Off-line multidimensional dimensional chromatography High resolution mass spectrometry Bioinformatic tools |
| url | http://www.sciencedirect.com/science/article/pii/S1756464616302869 |
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