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.

Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics / ZENEZINI CHIOZZI, Riccardo; Capriotti, ANNA LAURA; Cavaliere, Chiara; LA BARBERA, Giorgia; Piovesana, Susy; Lagana', Aldo. - In: JOURNAL OF FUNCTIONAL FOODS. - ISSN 1756-4646. - STAMPA. - 27:(2016), pp. 262-273. [10.1016/j.jff.2016.09.010]

Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics

ZENEZINI CHIOZZI, RICCARDO;CAPRIOTTI, ANNA LAURA
;
CAVALIERE, CHIARA;LA BARBERA, GIORGIA;PIOVESANA, SUSY;LAGANA', Aldo
2016

Abstract

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.
2016
ACE-inhibitory peptides; bioinformatic tools; cauliflower by-products; high resolution mass spectrometry; off-line multidimensional dimensional chromatography; medicine (miscellaneous); food science; utrition and dietetics
01 Pubblicazione su rivista::01a Articolo in rivista
Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics / ZENEZINI CHIOZZI, Riccardo; Capriotti, ANNA LAURA; Cavaliere, Chiara; LA BARBERA, Giorgia; Piovesana, Susy; Lagana', Aldo. - In: JOURNAL OF FUNCTIONAL FOODS. - ISSN 1756-4646. - STAMPA. - 27:(2016), pp. 262-273. [10.1016/j.jff.2016.09.010]
File allegati a questo prodotto
File Dimensione Formato  
Zenizini_Identification_2016.pdf

solo gestori archivio

Tipologia: Versione editoriale (versione pubblicata con il layout dell'editore)
Licenza: Tutti i diritti riservati (All rights reserved)
Dimensione 2.41 MB
Formato Adobe PDF
2.41 MB Adobe PDF   Contatta l'autore

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/938995
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 36
  • ???jsp.display-item.citation.isi??? 31
social impact