Isolation of peptides from a novel brewers spent grain protein isolate with potential to modulate glycaemic response

Alan Connolly; Martina B. O'Keeffe; Alice B. Nongonierma; Charles O. Piggott; Richard J. FitzGerald

doi:10.1111/ijfs.13260

Isolation of peptides from a novel brewers spent grain protein isolate with potential to modulate glycaemic response

Alan Connolly
, Martina B. O'Keeffe
, Alice B. Nongonierma
, Charles O. Piggott
, Richard J. FitzGerald

University of Limerick

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

Abstract

The in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory activity of a Brewers’ spent grain protein-enriched isolate (BSG-PI) Alcalase™ hydrolysate (AlcH), which had previously been identified as a relatively potent angiotensin-converting enzyme (ACE) inhibitor, was determined. The half maximal DPP-IV inhibitory concentration (IC₅₀) value of AlcH following 240-min digestion was 3.57 ± 0.19 mg mL⁻¹. Ultrafiltration fractionation did not significantly increase the DPP-IV inhibitory activity of the AlcH fractions. Subjection of AlcH to simulated gastrointestinal digestion (SGID), which yielded SAlcH, resulted in a significant increase in DPP-IV inhibitory activity (P < 0.05), particularly after the intestinal phase of digestion. Following semi-preparative reverse phase high performance liquid chromatography (RP-HPLC) fractionation of SAlcH, fraction 28 was identified as having highest mean DPP-IV inhibitory activity. Two novel DPP-IV inhibitory peptides, ILDL and ILLPGAQDGL, with IC₅₀ values of 1121.1 and 145.5 μm, respectively, were identified within fraction 28 of SAlcH following ultra-performance liquid chromatography (UPLC)-tandem mass spectrometry (MS/MS). BSG protein-derived peptides were confirmed as having dual ACE and DPP-IV inhibitory activities.

Original language	English
Pages (from-to)	146-153
Number of pages	8
Journal	International Journal of Food Science and Technology
Volume	52
Issue number	1
DOIs	https://doi.org/10.1111/ijfs.13260
Publication status	Published - 1 Jan 2017

Keywords

Barley
DPP-IV inhibition
bioactive peptides
brewers’ spent grain (BSG) protein
fractionation
simulated gastrointestinal digestion

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10.1111/ijfs.13260

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@article{f664e77dfc2e4d2e9c419c53d1ccbcbc,

title = "Isolation of peptides from a novel brewers spent grain protein isolate with potential to modulate glycaemic response",

abstract = "The in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory activity of a Brewers{\textquoteright} spent grain protein-enriched isolate (BSG-PI) Alcalase{\texttrademark} hydrolysate (AlcH), which had previously been identified as a relatively potent angiotensin-converting enzyme (ACE) inhibitor, was determined. The half maximal DPP-IV inhibitory concentration (IC50) value of AlcH following 240-min digestion was 3.57 ± 0.19 mg mL−1. Ultrafiltration fractionation did not significantly increase the DPP-IV inhibitory activity of the AlcH fractions. Subjection of AlcH to simulated gastrointestinal digestion (SGID), which yielded SAlcH, resulted in a significant increase in DPP-IV inhibitory activity (P < 0.05), particularly after the intestinal phase of digestion. Following semi-preparative reverse phase high performance liquid chromatography (RP-HPLC) fractionation of SAlcH, fraction 28 was identified as having highest mean DPP-IV inhibitory activity. Two novel DPP-IV inhibitory peptides, ILDL and ILLPGAQDGL, with IC50 values of 1121.1 and 145.5 μm, respectively, were identified within fraction 28 of SAlcH following ultra-performance liquid chromatography (UPLC)-tandem mass spectrometry (MS/MS). BSG protein-derived peptides were confirmed as having dual ACE and DPP-IV inhibitory activities.",

keywords = "Barley, DPP-IV inhibition, bioactive peptides, brewers{\textquoteright} spent grain (BSG) protein, fractionation, simulated gastrointestinal digestion",

author = "Alan Connolly and O'Keeffe, \{Martina B.\} and Nongonierma, \{Alice B.\} and Piggott, \{Charles O.\} and FitzGerald, \{Richard J.\}",

note = "Publisher Copyright: {\textcopyright} 2016 Institute of Food Science and Technology",

year = "2017",

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doi = "10.1111/ijfs.13260",

language = "English",

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pages = "146--153",

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AU - Connolly, Alan

AU - O'Keeffe, Martina B.

AU - Nongonierma, Alice B.

AU - Piggott, Charles O.

AU - FitzGerald, Richard J.

PY - 2017/1/1

Y1 - 2017/1/1

N2 - The in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory activity of a Brewers’ spent grain protein-enriched isolate (BSG-PI) Alcalase™ hydrolysate (AlcH), which had previously been identified as a relatively potent angiotensin-converting enzyme (ACE) inhibitor, was determined. The half maximal DPP-IV inhibitory concentration (IC50) value of AlcH following 240-min digestion was 3.57 ± 0.19 mg mL−1. Ultrafiltration fractionation did not significantly increase the DPP-IV inhibitory activity of the AlcH fractions. Subjection of AlcH to simulated gastrointestinal digestion (SGID), which yielded SAlcH, resulted in a significant increase in DPP-IV inhibitory activity (P < 0.05), particularly after the intestinal phase of digestion. Following semi-preparative reverse phase high performance liquid chromatography (RP-HPLC) fractionation of SAlcH, fraction 28 was identified as having highest mean DPP-IV inhibitory activity. Two novel DPP-IV inhibitory peptides, ILDL and ILLPGAQDGL, with IC50 values of 1121.1 and 145.5 μm, respectively, were identified within fraction 28 of SAlcH following ultra-performance liquid chromatography (UPLC)-tandem mass spectrometry (MS/MS). BSG protein-derived peptides were confirmed as having dual ACE and DPP-IV inhibitory activities.

AB - The in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory activity of a Brewers’ spent grain protein-enriched isolate (BSG-PI) Alcalase™ hydrolysate (AlcH), which had previously been identified as a relatively potent angiotensin-converting enzyme (ACE) inhibitor, was determined. The half maximal DPP-IV inhibitory concentration (IC50) value of AlcH following 240-min digestion was 3.57 ± 0.19 mg mL−1. Ultrafiltration fractionation did not significantly increase the DPP-IV inhibitory activity of the AlcH fractions. Subjection of AlcH to simulated gastrointestinal digestion (SGID), which yielded SAlcH, resulted in a significant increase in DPP-IV inhibitory activity (P < 0.05), particularly after the intestinal phase of digestion. Following semi-preparative reverse phase high performance liquid chromatography (RP-HPLC) fractionation of SAlcH, fraction 28 was identified as having highest mean DPP-IV inhibitory activity. Two novel DPP-IV inhibitory peptides, ILDL and ILLPGAQDGL, with IC50 values of 1121.1 and 145.5 μm, respectively, were identified within fraction 28 of SAlcH following ultra-performance liquid chromatography (UPLC)-tandem mass spectrometry (MS/MS). BSG protein-derived peptides were confirmed as having dual ACE and DPP-IV inhibitory activities.

KW - Barley

KW - DPP-IV inhibition

KW - bioactive peptides

KW - brewers’ spent grain (BSG) protein

KW - fractionation

KW - simulated gastrointestinal digestion

UR - https://www.scopus.com/pages/publications/85005767607

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DO - 10.1111/ijfs.13260

M3 - Article

AN - SCOPUS:85005767607

SN - 0950-5423

VL - 52

SP - 146

EP - 153

JO - International Journal of Food Science and Technology

JF - International Journal of Food Science and Technology

IS - 1

ER -

Isolation of peptides from a novel brewers spent grain protein isolate with potential to modulate glycaemic response

Abstract

Keywords

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