posted on 2017-04-27, 10:55authored byAlice B. Nongonierma, Richard J. Fitzgerald
An in silico approach was developed to predict the potential of 72 dietary proteins to act as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides. The model takes 68 DPP- IV inhibitory peptides (having an IC50 value < 2000 μM) and the specific contribution of their amino acids into account. Bovine α-lactalbumin (α-La) and κ-casein (CN) displayed the highest protein coverage (PC, 43.9 %) and potency index (PI, 17.9 10-6 μM-1 g-1), respectively for DPP-IV inhibitory peptides. Sequence alignment of 39 DPP-IV inhibitory peptides having IC50’s < 200 μM revealed the frequent occurrence of Trp at the N-terminus and Pro at position 2. Canola, chicken egg, oat and wheat were identified as potential sources of DPP-IV inhibitory peptides. In silico approaches may assist in the selection of food proteins for the enzymatic release of DPP-IV inhibitory peptides. The results are relevant to the generation of biofunctional ingredients for glycaemic management.
History
Publication
Food Chemistry;165, pp. 489-498
Publisher
Elsevier
Note
peer-reviewed
Other Funding information
EI
Rights
This is the author’s version of a work that was accepted for publication in Food Chemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Food Chemistry, 2014, 165, pp. 489-498,http://doi.org/10.1016/j.foodchem.2014.05.090