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

Riccardo Zenezini Chiozzi; Anna Laura Capriotti; Chiara Cavaliere; Giorgia La Barbera; Susy Piovesana; Aldo Laganà

doi: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

Riccardo Zenezini Chiozzi, Anna Laura Capriotti^*, Chiara Cavaliere, Giorgia La Barbera, Susy Piovesana, Aldo Laganà

^*Corresponding author for this work

Nutrition and Health

23 Citations (Scopus)

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.

Original language	English
Journal	Journal of Functional Foods
Volume	27
Pages (from-to)	262-273
Number of pages	12
ISSN	1756-4646
DOIs	https://doi.org/10.1016/j.jff.2016.09.010
Publication status	Published - 1 Dec 2016

Keywords

ACE-inhibitory peptides
Bioinformatic tools
Cauliflower by-products
High resolution mass spectrometry
Off-line multidimensional dimensional chromatography

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10.1016/j.jff.2016.09.010

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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

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 et al.

In: Journal of Functional Foods, Vol. 27, 01.12.2016, p. 262-273.

Research output: Contribution to journal › Journal article › Research › peer-review

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, vol. 27, pp. 262-273. https://doi.org/10.1016/j.jff.2016.09.010

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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",

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doi = "10.1016/j.jff.2016.09.010",

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AU - Capriotti, Anna Laura

AU - Cavaliere, Chiara

AU - La Barbera, Giorgia

AU - Piovesana, Susy

AU - Laganà, Aldo

PY - 2016/12/1

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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.

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KW - Bioinformatic tools

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

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Keywords

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