Purification and identification of dipeptidyl peptidase (DPP) IV inhibitory peptides from the macroalga Palmaria palmata

Pádraigín A. Harnedy; Martina B. O'Keeffe; Richard J. Fitzgerald

doi:10.1016/j.foodchem.2014.09.083

Purification and identification of dipeptidyl peptidase (DPP) IV inhibitory peptides from the macroalga Palmaria palmata

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

Abstract

Dipeptidyl peptidase (DPP)-IV inhibitory peptides were purified and identified from an aqueous Palmaria palmata protein extract hydrolysed with Corolase PP. The hydrolysate was fractionated by solid phase extraction (SPE) using a C18 matrix followed by semi-preparative reverse phase-high performance liquid chromatography (SP RP-HPLC). IC₅₀ values of 1.47 ± 0.09, 0.54 ± 0.03 and 0.36 ± 0.03 mg/ml were obtained for the hydrolysate, the 25% - acetonitrile (ACN) SPE fraction and the most active SP RP-HPLC peptide fraction (SP RP-HPLC 25-F28), respectively. Thirteen peptide sequences were identified following UPLC-ESI MS/MS analysis of SP RP-HPLC 25-F28. Three novel DPP-IV inhibitory peptides, Ile-Leu-Ala-Pro, Leu-Leu-Ala-Pro and Met-Ala-Gly-Val-Asp-His-Ile, with IC₅₀ values in the range 43-159 μM were identified. The results indicate that P. palmata derived peptides may have potential as functional food ingredients in the prevention and management of type 2 diabetes.

Original language	English
Pages (from-to)	400-406
Number of pages	7
Journal	Food Chemistry
Volume	172
DOIs	https://doi.org/10.1016/j.foodchem.2014.09.083
Publication status	Published - 1 Apr 2015

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Bioactive peptide
Dipeptidyl peptidase IV
Palmaria palmate
Type 2 diabetes

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10.1016/j.foodchem.2014.09.083

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title = "Purification and identification of dipeptidyl peptidase (DPP) IV inhibitory peptides from the macroalga Palmaria palmata",

abstract = "Dipeptidyl peptidase (DPP)-IV inhibitory peptides were purified and identified from an aqueous Palmaria palmata protein extract hydrolysed with Corolase PP. The hydrolysate was fractionated by solid phase extraction (SPE) using a C18 matrix followed by semi-preparative reverse phase-high performance liquid chromatography (SP RP-HPLC). IC50 values of 1.47 ± 0.09, 0.54 ± 0.03 and 0.36 ± 0.03 mg/ml were obtained for the hydrolysate, the 25\% - acetonitrile (ACN) SPE fraction and the most active SP RP-HPLC peptide fraction (SP RP-HPLC 25-F28), respectively. Thirteen peptide sequences were identified following UPLC-ESI MS/MS analysis of SP RP-HPLC 25-F28. Three novel DPP-IV inhibitory peptides, Ile-Leu-Ala-Pro, Leu-Leu-Ala-Pro and Met-Ala-Gly-Val-Asp-His-Ile, with IC50 values in the range 43-159 μM were identified. The results indicate that P. palmata derived peptides may have potential as functional food ingredients in the prevention and management of type 2 diabetes.",

keywords = "Bioactive peptide, Dipeptidyl peptidase IV, Palmaria palmate, Type 2 diabetes",

author = "Harnedy, \{P{\'a}draig{\'i}n A.\} and O'Keeffe, \{Martina B.\} and Fitzgerald, \{Richard J.\}",

year = "2015",

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doi = "10.1016/j.foodchem.2014.09.083",

language = "English",

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journal = "Food Chemistry",

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T1 - Purification and identification of dipeptidyl peptidase (DPP) IV inhibitory peptides from the macroalga Palmaria palmata

AU - Harnedy, Pádraigín A.

AU - O'Keeffe, Martina B.

AU - Fitzgerald, Richard J.

PY - 2015/4/1

Y1 - 2015/4/1

N2 - Dipeptidyl peptidase (DPP)-IV inhibitory peptides were purified and identified from an aqueous Palmaria palmata protein extract hydrolysed with Corolase PP. The hydrolysate was fractionated by solid phase extraction (SPE) using a C18 matrix followed by semi-preparative reverse phase-high performance liquid chromatography (SP RP-HPLC). IC50 values of 1.47 ± 0.09, 0.54 ± 0.03 and 0.36 ± 0.03 mg/ml were obtained for the hydrolysate, the 25% - acetonitrile (ACN) SPE fraction and the most active SP RP-HPLC peptide fraction (SP RP-HPLC 25-F28), respectively. Thirteen peptide sequences were identified following UPLC-ESI MS/MS analysis of SP RP-HPLC 25-F28. Three novel DPP-IV inhibitory peptides, Ile-Leu-Ala-Pro, Leu-Leu-Ala-Pro and Met-Ala-Gly-Val-Asp-His-Ile, with IC50 values in the range 43-159 μM were identified. The results indicate that P. palmata derived peptides may have potential as functional food ingredients in the prevention and management of type 2 diabetes.

AB - Dipeptidyl peptidase (DPP)-IV inhibitory peptides were purified and identified from an aqueous Palmaria palmata protein extract hydrolysed with Corolase PP. The hydrolysate was fractionated by solid phase extraction (SPE) using a C18 matrix followed by semi-preparative reverse phase-high performance liquid chromatography (SP RP-HPLC). IC50 values of 1.47 ± 0.09, 0.54 ± 0.03 and 0.36 ± 0.03 mg/ml were obtained for the hydrolysate, the 25% - acetonitrile (ACN) SPE fraction and the most active SP RP-HPLC peptide fraction (SP RP-HPLC 25-F28), respectively. Thirteen peptide sequences were identified following UPLC-ESI MS/MS analysis of SP RP-HPLC 25-F28. Three novel DPP-IV inhibitory peptides, Ile-Leu-Ala-Pro, Leu-Leu-Ala-Pro and Met-Ala-Gly-Val-Asp-His-Ile, with IC50 values in the range 43-159 μM were identified. The results indicate that P. palmata derived peptides may have potential as functional food ingredients in the prevention and management of type 2 diabetes.

KW - Bioactive peptide

KW - Dipeptidyl peptidase IV

KW - Palmaria palmate

KW - Type 2 diabetes

UR - https://www.scopus.com/pages/publications/84907546008

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DO - 10.1016/j.foodchem.2014.09.083

M3 - Article

C2 - 25442570

AN - SCOPUS:84907546008

SN - 0308-8146

VL - 172

SP - 400

EP - 406

JO - Food Chemistry

JF - Food Chemistry

ER -

Purification and identification of dipeptidyl peptidase (DPP) IV inhibitory peptides from the macroalga Palmaria palmata

Abstract

UN SDGs

Keywords

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