PMID- 29218344
OWN - NLM
STAT- MEDLINE
DCOM- 20180706
LR  - 20180706
IS  - 2042-650X (Electronic)
IS  - 2042-6496 (Linking)
VI  - 9
IP  - 1
DP  - 2018 Jan 24
TI  - Generation of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during the 
      enzymatic hydrolysis of tropical banded cricket (Gryllodes sigillatus) proteins.
PG  - 407-416
LID - 10.1039/c7fo01568b [doi]
AB  - Tropical banded crickets (Gryllodes sigillatus) were studied for their ability to 
      yield hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties. A 
      cricket protein isolate (CPI) was prepared following extraction of the water 
      soluble proteins from G. sigillatus powder (CP). The extraction yield and purity 
      were 20.90 +/- 0.35% and 57.0 +/- 2.23%, respectively. Endogenous proteinase 
      activities were detected in the CP, which were linked to the significant protein 
      breakdown seen in this sample. Fifteen CPI hydrolysates (H1-H15) were generated 
      with Protamex using a design of experiments (DOE) approach combining three 
      parameters, temperature (40, 50 and 60  degrees C), enzyme to substrate ratio (E : S, 
      0.50, 1.25 and 2.00% (w/w)) and hydrolysis time (60, 150 and 240 min). The DPP-IV 
      half maximal inhibitory concentrations (IC(50)) of the CPI hydrolysates ranged 
      from 0.40 +/- 0.03/0.40 +/- 0.02 (H2/H3) to 1.01 +/- 0.07 mg mL(-1) (H7). Following 
      simulated gastrointestinal digestion (SGID), the DPP-IV IC(50) of CPI decreased 
      (>3.57 vs. 0.78 +/- 0.04 mg mL(-1)) while that of H5 increased (0.47 +/- 0.03 vs. 
      0.71 +/- 0.06 mg mL(-1)). This study has demonstrated for the first time that G. 
      sigillatus protein hydrolysates are able to inhibit DPP-IV. The study of these 
      hydrolysates in vivo is needed to evaluate their potential role in glycaemic 
      management.
FAU - Nongonierma, Alice B
AU  - Nongonierma AB
AD  - Department of Biological Sciences, University of Limerick, Limerick, Ireland. 
      dick.fitzgerald@ul.ie.
FAU - Lamoureux, Candice
AU  - Lamoureux C
FAU - FitzGerald, Richard 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 (Insect Proteins)
RN  - 0 (Peptides)
RN  - 0 (Protein Hydrolysates)
RN  - EC 3.4.- (Peptide Hydrolases)
RN  - EC 3.4.14.5 (Dipeptidyl Peptidase 4)
SB  - IM
MH  - Animals
MH  - Dipeptidyl Peptidase 4/chemistry
MH  - Dipeptidyl-Peptidase IV Inhibitors/*chemistry
MH  - Gryllidae/*chemistry/enzymology
MH  - Hydrolysis
MH  - Insect Proteins/*chemistry
MH  - Peptide Hydrolases/*chemistry
MH  - Peptides/*chemistry
MH  - Protein Hydrolysates/chemistry
EDAT- 2017/12/09 06:00
MHDA- 2018/07/07 06:00
CRDT- 2017/12/09 06:00
PHST- 2017/12/09 06:00 [pubmed]
PHST- 2018/07/07 06:00 [medline]
PHST- 2017/12/09 06:00 [entrez]
AID - 10.1039/c7fo01568b [doi]
PST - ppublish
SO  - Food Funct. 2018 Jan 24;9(1):407-416. doi: 10.1039/c7fo01568b.