TY - JOUR
T1 - Isolation of peptides from a novel brewers spent grain protein isolate with potential to modulate glycaemic response
AU - Connolly, Alan
AU - O'Keeffe, Martina B.
AU - Nongonierma, Alice B.
AU - Piggott, Charles O.
AU - FitzGerald, Richard J.
N1 - Publisher Copyright:
© 2016 Institute of Food Science and Technology
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 - bioactive peptides
KW - brewers’ spent grain (BSG) protein
KW - DPP-IV inhibition
KW - fractionation
KW - simulated gastrointestinal digestion
UR - http://www.scopus.com/inward/record.url?scp=85005767607&partnerID=8YFLogxK
U2 - 10.1111/ijfs.13260
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 -