Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel milk protein hydrolysates

Alice B. Nongonierma, Sara Paolella, Priti Mudgil, Sajid Maqsood, Richard J. FitzGerald

Research output: Contribution to journalArticlepeer-review

Abstract

Nine novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (FLQY, FQLGASPY, ILDKEGIDY, ILELA, LLQLEAIR, LPVP, LQALHQGQIV, MPVQA and SPVVPF) were identified in camel milk proteins hydrolysed with trypsin. This was achieved using a sequential approach combining liquid chromatography tandem mass spectrometry (LC-MS/MS), qualitative/quantitative structure activity relationship (QSAR) and confirmatory studies with synthetic peptides. The most potent camel milk protein-derived DPP-IV inhibitory peptides, LPVP and MPVQA, had DPP-IV half maximal inhibitory concentrations (IC50) of 87.0 ± 3.2 and 93.3 ± 8.0 µM, respectively. DPP-IV inhibitory peptide sequences identified within camel and bovine milk protein hydrolysates generated under the same hydrolysis conditions differ. This was linked to differences in enzyme selectivity for peptide bond cleavage of camel and bovine milk proteins as well as dissimilarities in their amino acid sequences. Camel milk proteins contain novel DPP-IV inhibitory peptides which may play a role in the regulation of glycaemia in humans.

Original languageEnglish
Pages (from-to)340-348
Number of pages9
JournalFood Chemistry
Volume244
DOIs
Publication statusPublished - 1 Apr 2018

Keywords

  • Bioactive peptides
  • Camel milk proteins
  • Dipeptidyl peptidase IV inhibition
  • Homologous peptides
  • Quantitative structure activity relationship (QSAR)
  • Trypsin

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