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

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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; Laganà, Aldo.

I: Journal of Functional Foods, Bind 27, 2016, s. 262-273.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Zenezini Chiozzi, R, Capriotti, AL, Cavaliere, C, La Barbera, G, Piovesana, S & Laganà, A 2016, 'Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics', Journal of Functional Foods, bind 27, s. 262-273. https://doi.org/10.1016/j.jff.2016.09.010

APA

Zenezini Chiozzi, R., Capriotti, A. L., Cavaliere, C., La Barbera, G., Piovesana, S., & Laganà, A. (2016). Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. Journal of Functional Foods, 27, 262-273. https://doi.org/10.1016/j.jff.2016.09.010

Vancouver

Zenezini Chiozzi R, Capriotti AL, Cavaliere C, La Barbera G, Piovesana S, Laganà A. Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. Journal of Functional Foods. 2016;27:262-273. https://doi.org/10.1016/j.jff.2016.09.010

Author

Zenezini Chiozzi, Riccardo ; Capriotti, Anna Laura ; Cavaliere, Chiara ; La Barbera, Giorgia ; Piovesana, Susy ; Laganà, Aldo. / Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. I: Journal of Functional Foods. 2016 ; Bind 27. s. 262-273.

Bibtex

@article{504bd3b86b064e29a8905017326e6c55,
title = "Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics",
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.",
keywords = "ACE-inhibitory peptides, Bioinformatic tools, Cauliflower by-products, High resolution mass spectrometry, Off-line multidimensional dimensional chromatography",
author = "{Zenezini Chiozzi}, Riccardo and Capriotti, {Anna Laura} and Chiara Cavaliere and {La Barbera}, Giorgia and Susy Piovesana and Aldo Lagan{\`a}",
note = "(Ekstern)",
year = "2016",
doi = "10.1016/j.jff.2016.09.010",
language = "English",
volume = "27",
pages = "262--273",
journal = "Journal of Functional Foods",
issn = "1756-4646",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics

AU - Zenezini Chiozzi, Riccardo

AU - Capriotti, Anna Laura

AU - Cavaliere, Chiara

AU - La Barbera, Giorgia

AU - Piovesana, Susy

AU - Laganà, Aldo

N1 - (Ekstern)

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

KW - ACE-inhibitory peptides

KW - Bioinformatic tools

KW - Cauliflower by-products

KW - High resolution mass spectrometry

KW - Off-line multidimensional dimensional chromatography

UR - http://www.scopus.com/inward/record.url?scp=84988948154&partnerID=8YFLogxK

U2 - 10.1016/j.jff.2016.09.010

DO - 10.1016/j.jff.2016.09.010

M3 - Journal article

AN - SCOPUS:84988948154

VL - 27

SP - 262

EP - 273

JO - Journal of Functional Foods

JF - Journal of Functional Foods

SN - 1756-4646

ER -

ID: 231311619