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

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Standard

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, 05.2018, s. 40-47.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Montone, CM, Capriotti, AL, Cavaliere, C, La Barbera, G, Piovesana, S, Zenezini Chiozzi, R & Laganà, A 2018, 'Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics', Journal of Functional Foods, bind 44, s. 40-47. https://doi.org/10.1016/j.jff.2018.02.022

APA

Montone, C. M., Capriotti, A. L., Cavaliere, C., La Barbera, G., Piovesana, S., Zenezini Chiozzi, R., & Laganà, A. (2018). Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. Journal of Functional Foods, 44, 40-47. https://doi.org/10.1016/j.jff.2018.02.022

Vancouver

Montone CM, Capriotti AL, Cavaliere C, La Barbera G, Piovesana S, Zenezini Chiozzi R o.a. Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. Journal of Functional Foods. 2018 maj;44:40-47. https://doi.org/10.1016/j.jff.2018.02.022

Author

Montone, Carmela Maria ; Capriotti, Anna Laura ; Cavaliere, Chiara ; La Barbera, Giorgia ; Piovesana, Susy ; Zenezini Chiozzi, Riccardo ; Laganà, Aldo. / Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics. I: Journal of Functional Foods. 2018 ; Bind 44. s. 40-47.

Bibtex

@article{922858f33c274248b25ca8a6393c18b8,
title = "Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics",
abstract = "In the present paper, bioactive peptides from cauliflower by-products (leaves and stems) were investigated. Alcalase{\circledR} 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.",
keywords = "ACE-inhibitory peptides, Antioxidant peptides, Cauliflower waste, Peptidomics",
author = "Montone, {Carmela Maria} and Capriotti, {Anna Laura} and Chiara Cavaliere and {La Barbera}, Giorgia and Susy Piovesana and {Zenezini Chiozzi}, Riccardo and Aldo Lagan{\`a}",
year = "2018",
month = "5",
doi = "10.1016/j.jff.2018.02.022",
language = "English",
volume = "44",
pages = "40--47",
journal = "Journal of Functional Foods",
issn = "1756-4646",
publisher = "Elsevier",

}

RIS

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

PY - 2018/5

Y1 - 2018/5

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