Identification of three novel angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. (December 2016)

• Record Type: Journal Article
• Authors: Zenezini Chiozzi, Riccardo; Capriotti, Anna Laura; Cavaliere, Chiara; La Barbera, Giorgia; Piovesana, Susy; Laganà, Aldo
• Is Part Of: Journal of functional foods. Volume 27(2016)
• Page Start: 262
• Page End: 273
• Publication Date: 2016-12
• Subjects: ACE-inhibitory peptides -- Cauliflower by-products -- Off-line multidimensional dimensional chromatography -- High resolution mass spectrometry -- Bioinformatic tools; ACE angiotensin-converting enzyme -- AO antioxidant -- BAPs bioactive peptides -- BSA bovine serum albumin -- DPPH 2, 2-diphenyl-1-picrylhydrazyl -- DTT dithiothreitol -- EDTA ethylenediaminetetraacetic acid -- HHL N-hippuryl-L-histidyl-L-leucine -- HILIC hydrophilic interaction chromatography -- IAA iodacetamide -- SDS sodium dodecyl sulphate -- SPE solid phase extraction -- RP reversed phase -- TCA trichloroacetic acid -- TFA trifluoroacetic acid; Functional foods -- Analysis -- Periodicals; Food -- Biotechnology -- Periodicals; Nutrition -- Periodicals; 613.2
• DOI: 10.1016/j.jff.2016.09.010
• Languages: English
• ISSNs: 1756-4646

Abstract

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. Highlights: Cauliflower by-products are a potential source of value-added compounds. Bioactive peptides from cauliflower waste proteins have potent biological activities. Multidimensional liquid chromatography for purification of bioactive peptides. Three novel ACE-inhibitory peptides identified from cauliflower waste.