Generation and identification of angiotensin converting enzyme (ACE) inhibitory peptides from a brewers’ spent grain protein isolate

Connolly, Alan; O’Keeffe, Martina B.; Piggott, Charles O.; Nongonierma, Alice B.; Fitzgerald, Richard J.

doi:10.1016/j.foodchem.2014.12.027

Cited by 84 publications

(51 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…DPP-IV inhibition of the ProH sample also increased significantly (P < 0.05) from 42.88 AE 4.96% to 65.99 AE 1.03% after the gastric phase, however, unlike BSG-PI, the intestinal phase did not result in significantly increased DPP-IV inhibition. It has previously been suggested that the increase in bioactivity is due to the increase in low molecular mass peptides as a result of digestion by gastrointestinal enzymes (Connolly et al, 2015). The increase in inhibition for BSG-PI and ProH after intestinal digestion follows a similar trend observed previously where ACE inhibition also increased after intestinal digestion (Connolly et al, 2015).…”

Section: Dpp-iv Inhibitionð%þ ¼supporting

confidence: 73%

“…Ultra-performance liquid chromatography (UPLC)-tandem mass spectrometry (MS/MS) Identification of the peptides within UPLC-MS/MS of the semi-preparative RP-HPLC fraction 28, obtained from the alcalase hydrolysate subjected to SGID (SAlcH) was carried out using UPLC-MS/MS as previously described (Connolly et al, 2015).…”

Section: Semi-preparative Rp-hplcmentioning

confidence: 99%

“…3) indicated that the peptides yielding the highest mean DPP-IV inhibitory response occurred in fraction 28 of SAlcH (Fig. Fraction 28 of SAlcH was subjected to LC-MS/MS and 34 different peptide sequences were identified therein (Connolly et al, 2015). Fraction 28 of SAlcH was subjected to LC-MS/MS and 34 different peptide sequences were identified therein (Connolly et al, 2015).…”

Section: Dpp-iv Inhibitory Activity Of Synthetic Peptides Identified mentioning

confidence: 99%

“…Industrial-scale food processing co-products are increasingly being viewed as potential sources of bioactive ingredients. BSG protein hydrolysates have previously demonstrated in vitro a-glucosidase, angiotensin-converting enzyme (ACE) and DPP-IV inhibitory effects while a number of ACE inhibitory peptides have also been identified within BSG protein hydrolysates (Connolly et al, 2014(Connolly et al, , 2015. BSG protein hydrolysates have previously demonstrated in vitro a-glucosidase, angiotensin-converting enzyme (ACE) and DPP-IV inhibitory effects while a number of ACE inhibitory peptides have also been identified within BSG protein hydrolysates (Connolly et al, 2014(Connolly et al, , 2015.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

Connolly

O’Keeffe

Nongonierma

et al. 2016

Int J of Food Sci Tech

Self Cite

View full text Add to dashboard Cite

Summary 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.

show abstract

Section: Dpp-iv Inhibitionð%þ ¼supporting

confidence: 73%

Section: Semi-preparative Rp-hplcmentioning

confidence: 99%

Section: Dpp-iv Inhibitory Activity Of Synthetic Peptides Identified mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

Connolly

O’Keeffe

Nongonierma

et al. 2016

Int J of Food Sci Tech

Self Cite

View full text Add to dashboard Cite

show abstract

“…[32,33] The correlation between hydrophobicity and α-glucosidase inhibitory activity (data from Table 1) showed a weak correlation (r 2 value of .0958). [32,33] The correlation between hydrophobicity and α-glucosidase inhibitory activity (data from Table 1) showed a weak correlation (r 2 value of .0958).…”

Section: Effect Of Net Charge Hydrophobicity and Isoelectric Pointmentioning

confidence: 99%

Structural properties of bioactive peptides with α‐glucosidase inhibitory activity

et al. 2017

View full text Add to dashboard Cite

Bioactive peptides are emerging as promising class of drugs that could serve as α-glucosidase inhibitors for the treatment of type 2 diabetes. This article identifies structural and physicochemical requirements for the design of therapeutically relevant α-glucosidase inhibitory peptides. So far, a total of 43 fully sequenced α-glucosidase inhibitory peptides have been reported and 13 of them had IC values several folds lower than acarbose. Analysis of the peptides indicates that the most potent peptides are tri- to hexapeptides with amino acids containing a hydroxyl or basic side chain at the N-terminal. The presence of proline within the chain and alanine or methionine at the C-terminal appears to be relevant for high activity. Hydrophobicity and isoelectric points are less important variables for α-glucosidase inhibition whilst a net charge of 0 or +1 was predicted for the highly active peptides. In silico simulated gastrointestinal digestion revealed that the high and moderately active peptides, including the most potent peptide (STYV), were gastrointestinally unstable, except SQSPA. Molecular docking of SQSPA, STYV, and STY (digestion fragment of STYV) with α-glucosidase suggested that their hydrogen bonding interactions and binding energies were comparable with acarbose. The identified criteria will facilitate the design of new peptide-derived α-glucosidase inhibitors.

show abstract

Microbial Production of Bioactive Peptides

Gennari,

Leonhardt,

Paludo

et al. 2023

Microbial Bioreactors for Industrial Molecules

View full text Add to dashboard Cite

Generation and identification of angiotensin converting enzyme (ACE) inhibitory peptides from a brewers’ spent grain protein isolate

Cited by 84 publications

References 33 publications

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

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

Structural properties of bioactive peptides with α‐glucosidase inhibitory activity

Microbial Production of Bioactive Peptides

Contact Info

Product

Resources

About