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

    90 Citations (Scopus)

    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 - Apr 1 2018

    Keywords

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

    ASJC Scopus subject areas

    • Analytical Chemistry
    • Food Science

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