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

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

doi:10.1016/j.jff.2018.02.022

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

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

^*Corresponding author for this work

Nutrition and Health

19 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Journal of Functional Foods
Volume	44
Pages (from-to)	40-47
Number of pages	8
ISSN	1756-4646
DOIs	https://doi.org/10.1016/j.jff.2018.02.022
Publication status	Published - May 2018

Keywords

ACE-inhibitory peptides
Antioxidant peptides
Cauliflower waste
Peptidomics

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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

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 et al.

In: Journal of Functional Foods, Vol. 44, 05.2018, p. 40-47.

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

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, vol. 44, pp. 40-47. https://doi.org/10.1016/j.jff.2018.02.022

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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{\textregistered} 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}",

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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

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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

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SN - 1756-4646

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EP - 47

JO - Journal of Functional Foods

JF - Journal of Functional Foods

ER -

Characterization of antioxidant and 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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