Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7596118 | Food Chemistry | 2014 | 43 Pages |
Abstract
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 10â6 μMâ1 gâ1), 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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Alice B. Nongonierma, Richard J. FitzGerald,