Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties. Issue 6 (23rd May 2017)
- Record Type:
- Journal Article
- Title:
- Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties. Issue 6 (23rd May 2017)
- Main Title:
- Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties
- Authors:
- Nongonierma, A. B.
Hennemann, M.
Paolella, S.
FitzGerald, R. J. - Abstract:
- Abstract : Wheat gluten hydrolysates contain known/potential DPP-IV inhibitory peptides. Abstract : Wheat gluten, a Pro-rich dietary protein, was investigated for its potential to produce dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during enzymatic hydrolysis with Debitrase HYW20. Nine gluten hydrolysates (H1–H9) were generated using a 2 factor × 3 level design of experiments (DOE) including the incubation temperature (40, 50 and 60 °C) and the enzyme: substrate ratio (E : S, 0.5, 1.0 and 1.5% (w/w)). Their DPP-IV half maximal inhibitory concentration (IC50 ) ranged from 0.24 ± 0.02 (H9) to 0.66 ± 0.06 mg mL −1 (H2A and H7) and their degree of hydrolysis (DH) from 31.7 ± 0.9 (H7) to 62.2 ± 3.0% (H6). Gluten and H9, the most potent DPP-IV inhibitory hydrolysate, were subjected to simulated gastrointestinal digestion (SGID), yielding Gluten_CorPP and H9_CorPP, respectively. H9_CorPP had a higher DPP-IV inhibitory potency than Gluten_CorPP ( i.e., DPP-IV IC50 values of 0.33 ± 0.03 vs. 1.45 ± 0.26 mg mL −1, respectively). H9 and H9_CorPP both contained relatively potent DPP-IV inhibitory peptides such as Val-Pro-Leu, Trp-Leu and Trp-Pro which were identified by liquid chromatography tandem mass spectrometry (LC-MS/MS). In addition, several sequences possessing features of DPP-IV inhibitory peptides, mostly consisting of a penultimate or C-terminal Pro, were identified within H9. The presence of Pro-containing peptides within H9 may contribute to its stability toAbstract : Wheat gluten hydrolysates contain known/potential DPP-IV inhibitory peptides. Abstract : Wheat gluten, a Pro-rich dietary protein, was investigated for its potential to produce dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during enzymatic hydrolysis with Debitrase HYW20. Nine gluten hydrolysates (H1–H9) were generated using a 2 factor × 3 level design of experiments (DOE) including the incubation temperature (40, 50 and 60 °C) and the enzyme: substrate ratio (E : S, 0.5, 1.0 and 1.5% (w/w)). Their DPP-IV half maximal inhibitory concentration (IC50 ) ranged from 0.24 ± 0.02 (H9) to 0.66 ± 0.06 mg mL −1 (H2A and H7) and their degree of hydrolysis (DH) from 31.7 ± 0.9 (H7) to 62.2 ± 3.0% (H6). Gluten and H9, the most potent DPP-IV inhibitory hydrolysate, were subjected to simulated gastrointestinal digestion (SGID), yielding Gluten_CorPP and H9_CorPP, respectively. H9_CorPP had a higher DPP-IV inhibitory potency than Gluten_CorPP ( i.e., DPP-IV IC50 values of 0.33 ± 0.03 vs. 1.45 ± 0.26 mg mL −1, respectively). H9 and H9_CorPP both contained relatively potent DPP-IV inhibitory peptides such as Val-Pro-Leu, Trp-Leu and Trp-Pro which were identified by liquid chromatography tandem mass spectrometry (LC-MS/MS). In addition, several sequences possessing features of DPP-IV inhibitory peptides, mostly consisting of a penultimate or C-terminal Pro, were identified within H9. The presence of Pro-containing peptides within H9 may contribute to its stability to digestive enzymes. Gluten hydrolysates may have antidiabetic potential for humans. … (more)
- Is Part Of:
- Food & function. Volume 8:Issue 6(2017)
- Journal:
- Food & function
- Issue:
- Volume 8:Issue 6(2017)
- Issue Display:
- Volume 8, Issue 6 (2017)
- Year:
- 2017
- Volume:
- 8
- Issue:
- 6
- Issue Sort Value:
- 2017-0008-0006-0000
- Page Start:
- 2249
- Page End:
- 2257
- Publication Date:
- 2017-05-23
- Subjects:
- Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Nutrition -- Periodicals
664.07 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/FO ↗
http://pubs.rsc.org/en/journals/journal/fo ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c7fo00165g ↗
- Languages:
- English
- ISSNs:
- 2042-6496
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.038457
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 1927.xml