PMID- 28534590
OWN - NLM
STAT- MEDLINE
DCOM- 20170901
LR  - 20170901
IS  - 2042-650X (Electronic)
IS  - 2042-6496 (Linking)
VI  - 8
IP  - 6
DP  - 2017 Jun 21
TI  - Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) 
      inhibitory properties.
PG  - 2249-2257
LID - 10.1039/c7fo00165g [doi]
AB  - 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 x 3 level design of experiments (DOE) including the incubation 
      temperature (40, 50 and 60  degrees C) and the enzyme: substrate ratio (E : S, 0.5, 1.0 
      and 1.5% (w/w)). Their DPP-IV half maximal inhibitory concentration (IC(50)) 
      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 IC(50) 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.
FAU - Nongonierma, A B
AU  - Nongonierma AB
AD  - Department of Biological Sciences, University of Limerick, Limerick, Ireland. 
      dick.fitzgerald@ul.ie.
FAU - Hennemann, M
AU  - Hennemann M
FAU - Paolella, S
AU  - Paolella S
FAU - FitzGerald, R J
AU  - FitzGerald RJ
LA  - eng
PT  - Journal Article
PL  - England
TA  - Food Funct
JT  - Food & function
JID - 101549033
RN  - 0 (Dipeptidyl-Peptidase IV Inhibitors)
RN  - 0 (Peptides)
RN  - 8002-80-0 (Glutens)
RN  - EC 3.4.14.5 (Dipeptidyl Peptidase 4)
SB  - IM
MH  - Amino Acid Sequence
MH  - Dipeptidyl Peptidase 4/chemistry
MH  - Dipeptidyl-Peptidase IV Inhibitors/*chemistry
MH  - Glutens/*chemistry
MH  - Humans
MH  - Hydrolysis
MH  - Molecular Sequence Data
MH  - Peptide Mapping
MH  - Peptides/*chemistry
MH  - Tandem Mass Spectrometry
MH  - Triticum/*chemistry
EDAT- 2017/05/24 06:00
MHDA- 2017/09/02 06:00
CRDT- 2017/05/24 06:00
PHST- 2017/05/24 06:00 [pubmed]
PHST- 2017/09/02 06:00 [medline]
PHST- 2017/05/24 06:00 [entrez]
AID - 10.1039/c7fo00165g [doi]
PST - ppublish
SO  - Food Funct. 2017 Jun 21;8(6):2249-2257. doi: 10.1039/c7fo00165g.