TY - JOUR
T1 - Generation of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during the enzymatic hydrolysis of tropical banded cricket (: Gryllodes sigillatus) proteins
AU - Nongonierma, Alice B.
AU - Lamoureux, Candice
AU - FitzGerald, Richard J.
N1 - Publisher Copyright:
© 2018 The Royal Society of Chemistry.
PY - 2018/1
Y1 - 2018/1
N2 - 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 °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 (IC50) 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 IC50 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.
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 °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 (IC50) 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 IC50 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.
UR - http://www.scopus.com/inward/record.url?scp=85041228745&partnerID=8YFLogxK
U2 - 10.1039/c7fo01568b
DO - 10.1039/c7fo01568b
M3 - Article
C2 - 29218344
AN - SCOPUS:85041228745
SN - 2042-6496
VL - 9
SP - 407
EP - 416
JO - Food and Function
JF - Food and Function
IS - 1
ER -