TY - JOUR
T1 - Milk protein isolate (MPI) as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides
AU - Nongonierma, Alice B.
AU - Lalmahomed, Mehdeeyah
AU - Paolella, Sara
AU - FitzGerald, Richard J.
N1 - Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2017/9/15
Y1 - 2017/9/15
N2 - A multifactorial [temperature (40, 50 and 60 °C), hydrolysis time (60, 150 and 240 min) and enzyme to substrate ratio (E:S; 1.0, 1.5 and 2.0%)] design of experiments (DOE) was used to optimise the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during hydrolysis of bovine milk protein isolate (MPI) with Neutrase 0.8L™, yielding 15 hydrolysates (H1-H15). Variation in temperature and time had a significant effect on DPP-IV inhibitory properties (p < 0.05) in contrast with E:S (p > 0.05). The DPP-IV half maximal inhibitory concentration (IC50) of H4, a potent sample, was maintained following simulated gastrointestinal digestion (SGID, DPP-IV IC50 = 0.60 ± 0.06 vs. 0.58 ± 0.09 mg ml−1, p > 0.05). Several peptides with DPP-IV inhibitory features or known activity were identified by liquid chromatography-tandem mass spectrometry (LC–MS/MS) within the hydrolysates. MPI hydrolysates may have potential for use as dietary ingredients with serum glucose lowering activity in humans.
AB - A multifactorial [temperature (40, 50 and 60 °C), hydrolysis time (60, 150 and 240 min) and enzyme to substrate ratio (E:S; 1.0, 1.5 and 2.0%)] design of experiments (DOE) was used to optimise the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during hydrolysis of bovine milk protein isolate (MPI) with Neutrase 0.8L™, yielding 15 hydrolysates (H1-H15). Variation in temperature and time had a significant effect on DPP-IV inhibitory properties (p < 0.05) in contrast with E:S (p > 0.05). The DPP-IV half maximal inhibitory concentration (IC50) of H4, a potent sample, was maintained following simulated gastrointestinal digestion (SGID, DPP-IV IC50 = 0.60 ± 0.06 vs. 0.58 ± 0.09 mg ml−1, p > 0.05). Several peptides with DPP-IV inhibitory features or known activity were identified by liquid chromatography-tandem mass spectrometry (LC–MS/MS) within the hydrolysates. MPI hydrolysates may have potential for use as dietary ingredients with serum glucose lowering activity in humans.
KW - Bioactive peptides
KW - Dipeptidyl peptidase IV inhibition
KW - Milk protein isolate
KW - Response surface methodology
UR - http://www.scopus.com/inward/record.url?scp=85016389741&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2017.03.123
DO - 10.1016/j.foodchem.2017.03.123
M3 - Article
C2 - 28449998
AN - SCOPUS:85016389741
SN - 0308-8146
VL - 231
SP - 202
EP - 211
JO - Food Chemistry
JF - Food Chemistry
ER -