Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics

• Main Authors: Carmela Maria Montone, Anna Laura Capriotti, Chiara Cavaliere, Giorgia La Barbera, Susy Piovesana, Riccardo Zenezini Chiozzi, Aldo Laganà
• Format: Article
• Language: English
• Published: Elsevier 2018-05-01
• Series: Journal of Functional Foods
• Subjects: Peptidomics; Cauliflower waste; Antioxidant peptides; ACE-inhibitory peptides
• Online Access: http://www.sciencedirect.com/science/article/pii/S1756464618300677

In the present paper, bioactive peptides from cauliflower by-products (leaves and stems) were investigated. Alcalase® protein hydrolysis time and pH conditions were optimized, then the hydrolysates were fractionated by preparative RP-HPLC into 12 fractions. Each fraction was tested for the ABTS (2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)), and DPPH (2,2-diphenyl-1-picrylhydrazyl) radical scavenging activity and for ACE (angiotensin-converting enzyme) inhibitor activity. The peptides in the most active fractions were identified by peptidomics technologies and screened for bioactivity by the use of bioinformatics. For ACE-inhibitor activity, two peptides were synthetized, APYDPDWYYIR and SKGFTSPLF, which provided an EC50 value of 2.59 μmol L−1 and 15.26 μmol L−1, respectively. For the ABTS radical scavenging activity, SKGFTSPLF and LDDPVFRPL were tested, and provided an EC50 of 10.35 μmol L−1 and 8.29 μmol L−1, respectively. For the DPPH radical scavenging activity, SKGFTSPLF and LRAPPGWTGR were tested and provided an EC50 of 8.2 μmol L−1 and 5.26 μmol L−1, respectively.