Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics
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Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. / Montone, Carmela Maria; Capriotti, Anna Laura; Cavaliere, Chiara; La Barbera, Giorgia; Piovesana, Susy; Zenezini Chiozzi, Riccardo; Laganà, Aldo.
I: Journal of Functional Foods, Bind 44, 2018, s. 40-47.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics
AU - Montone, Carmela Maria
AU - Capriotti, Anna Laura
AU - Cavaliere, Chiara
AU - La Barbera, Giorgia
AU - Piovesana, Susy
AU - Zenezini Chiozzi, Riccardo
AU - Laganà, Aldo
N1 - (Ekstern)
PY - 2018
Y1 - 2018
N2 - 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.
AB - 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.
KW - ACE-inhibitory peptides
KW - Antioxidant peptides
KW - Cauliflower waste
KW - Peptidomics
UR - http://www.scopus.com/inward/record.url?scp=85042659914&partnerID=8YFLogxK
U2 - 10.1016/j.jff.2018.02.022
DO - 10.1016/j.jff.2018.02.022
M3 - Journal article
AN - SCOPUS:85042659914
VL - 44
SP - 40
EP - 47
JO - Journal of Functional Foods
JF - Journal of Functional Foods
SN - 1756-4646
ER -
ID: 231310138