Peptide identification from a: Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities

Maria Cermeño; Julianne Stack; Paul R. Tobin; Martina B. O'Keeffe; Pádraigín A. Harnedy; Dagmar B. Stengel; Richard J. Fitzgerald

doi:10.1039/c9fo00680j

Peptide identification from a: Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities

Maria Cermeño, Julianne Stack, Paul R. Tobin, Martina B. O'Keeffe, Pádraigín A. Harnedy, Dagmar B. Stengel, Richard J. Fitzgerald

Department of Biological Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

A Porphyra dioica protein extract was enzymatically hydrolysed and then fractionated using semi-preparative reverse-phase high performance chromatography. The hydrolysate and its fractions were tested for their oxygen radical absorbance capacity (ORAC) along with their angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities. The most potent fraction was analysed by liquid chromatography mass spectrometry. Eight peptide sequences were selected for synthesis based on their structure-activity criteria for bioactivity. Asp-Tyr-Tyr-Lys-Arg showed the highest ORAC activity (4.27 ± 0.15 μmol Trolox equivalent per μM). Thr-Tyr-Ile-Ala had the highest ACE inhibitory activity (IC₅₀: 89.7 ± 7.10 μM). Tyr-Leu-Val-Ala was the only peptide showing DPP-IV inhibitory activity (IC₅₀: 439 ± 44 μM). Apart from Asp-Tyr-Tyr-Lys-Arg and Thr-Tyr-Ile-Ala, which displayed increased ORAC activity, the bioactivities of the peptides were either maintained or decreased following in vitro simulated gastrointestinal digestion. The results indicate that P. dioica-derived peptides may have potential applications as health enhancing ingredients.

Original language	English
Pages (from-to)	3421-3429
Number of pages	9
Journal	Food and Function
Volume	10
Issue number	6
DOIs	https://doi.org/10.1039/c9fo00680j https://doi.org/10.1039/C9FO00680J
Publication status	Published - Jun 2019

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Cermeño, M., Stack, J., Tobin, P. R., O'Keeffe, M. B., Harnedy, P. A., Stengel, D. B., & Fitzgerald, R. J. (2019). Peptide identification from a: Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities. Food and Function, 10(6), 3421-3429. https://doi.org/10.1039/c9fo00680j, https://doi.org/10.1039/C9FO00680J

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title = "Peptide identification from a: Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities",

abstract = "A Porphyra dioica protein extract was enzymatically hydrolysed and then fractionated using semi-preparative reverse-phase high performance chromatography. The hydrolysate and its fractions were tested for their oxygen radical absorbance capacity (ORAC) along with their angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities. The most potent fraction was analysed by liquid chromatography mass spectrometry. Eight peptide sequences were selected for synthesis based on their structure-activity criteria for bioactivity. Asp-Tyr-Tyr-Lys-Arg showed the highest ORAC activity (4.27 ± 0.15 μmol Trolox equivalent per μM). Thr-Tyr-Ile-Ala had the highest ACE inhibitory activity (IC50: 89.7 ± 7.10 μM). Tyr-Leu-Val-Ala was the only peptide showing DPP-IV inhibitory activity (IC50: 439 ± 44 μM). Apart from Asp-Tyr-Tyr-Lys-Arg and Thr-Tyr-Ile-Ala, which displayed increased ORAC activity, the bioactivities of the peptides were either maintained or decreased following in vitro simulated gastrointestinal digestion. The results indicate that P. dioica-derived peptides may have potential applications as health enhancing ingredients.",

author = "Maria Cerme{\~n}o and Julianne Stack and Tobin, {Paul R.} and O'Keeffe, {Martina B.} and Harnedy, {P{\'a}draig{\'i}n A.} and Stengel, {Dagmar B.} and Fitzgerald, {Richard J.}",

note = "Publisher Copyright: {\textcopyright} 2019 The Royal Society of Chemistry.",

year = "2019",

month = jun,

doi = "10.1039/c9fo00680j",

language = "English",

volume = "10",

pages = "3421--3429",

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Cermeño, M, Stack, J, Tobin, PR, O'Keeffe, MB, Harnedy, PA, Stengel, DB & Fitzgerald, RJ 2019, 'Peptide identification from a: Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities', Food and Function, vol. 10, no. 6, pp. 3421-3429. https://doi.org/10.1039/c9fo00680j, https://doi.org/10.1039/C9FO00680J

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T2 - Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities

AU - Cermeño, Maria

AU - Stack, Julianne

AU - Tobin, Paul R.

AU - O'Keeffe, Martina B.

AU - Harnedy, Pádraigín A.

AU - Stengel, Dagmar B.

AU - Fitzgerald, Richard J.

PY - 2019/6

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N2 - A Porphyra dioica protein extract was enzymatically hydrolysed and then fractionated using semi-preparative reverse-phase high performance chromatography. The hydrolysate and its fractions were tested for their oxygen radical absorbance capacity (ORAC) along with their angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities. The most potent fraction was analysed by liquid chromatography mass spectrometry. Eight peptide sequences were selected for synthesis based on their structure-activity criteria for bioactivity. Asp-Tyr-Tyr-Lys-Arg showed the highest ORAC activity (4.27 ± 0.15 μmol Trolox equivalent per μM). Thr-Tyr-Ile-Ala had the highest ACE inhibitory activity (IC50: 89.7 ± 7.10 μM). Tyr-Leu-Val-Ala was the only peptide showing DPP-IV inhibitory activity (IC50: 439 ± 44 μM). Apart from Asp-Tyr-Tyr-Lys-Arg and Thr-Tyr-Ile-Ala, which displayed increased ORAC activity, the bioactivities of the peptides were either maintained or decreased following in vitro simulated gastrointestinal digestion. The results indicate that P. dioica-derived peptides may have potential applications as health enhancing ingredients.

AB - A Porphyra dioica protein extract was enzymatically hydrolysed and then fractionated using semi-preparative reverse-phase high performance chromatography. The hydrolysate and its fractions were tested for their oxygen radical absorbance capacity (ORAC) along with their angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities. The most potent fraction was analysed by liquid chromatography mass spectrometry. Eight peptide sequences were selected for synthesis based on their structure-activity criteria for bioactivity. Asp-Tyr-Tyr-Lys-Arg showed the highest ORAC activity (4.27 ± 0.15 μmol Trolox equivalent per μM). Thr-Tyr-Ile-Ala had the highest ACE inhibitory activity (IC50: 89.7 ± 7.10 μM). Tyr-Leu-Val-Ala was the only peptide showing DPP-IV inhibitory activity (IC50: 439 ± 44 μM). Apart from Asp-Tyr-Tyr-Lys-Arg and Thr-Tyr-Ile-Ala, which displayed increased ORAC activity, the bioactivities of the peptides were either maintained or decreased following in vitro simulated gastrointestinal digestion. The results indicate that P. dioica-derived peptides may have potential applications as health enhancing ingredients.

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SN - 2042-6496

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JO - Food and Function

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Peptide identification from a: Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities

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