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Milk protein isolate (MPI) as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides
Nongonierma, Alice B.; Lalmahomed, Mehdeeyah; Paolella, Sara; Fitzgerald, Richard J.
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. ACCEPTED peer-reviewed
Keyword(s): dipeptidyl peptidase IV inhibition; milk protein isolate; bioactive peptides; response surface methodology
Publication Date:
2017
Type: Journal article
Peer-Reviewed: Yes
Language(s): English
Institution: University of Limerick
Funder(s): Enterprise Ireland; Science Foundation Ireland
Citation(s): Food Chemistry;231, pp. 202-211
http://dx.doi.org/10.1016/j.foodchem.2017.03.123
TC2013-0001
Publisher(s): Elsevier
First Indexed: 2017-04-20 05:27:59 Last Updated: 2018-04-09 06:32:45