Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of a camel whey protein enriched hydrolysate preparation

Alice B. Nongonierma, Cloé Cadamuro, Aurélien Le Gouic, Priti Mudgil, Sajid Maqsood, Richard J. FitzGerald

    Research output: Contribution to journalArticlepeer-review

    53 Citations (Scopus)

    Abstract

    Camel milk proteins contain dipeptidyl peptidase IV (DPP-IV) inhibitory peptides. A camel whey protein concentrate (WPC, 44.7 ± 3.4% (w/w) protein) was prepared and subsequently hydrolysed with trypsin at different temperatures, enzyme to substrate (E:S) ratios and hydrolysis times yielding fifteen hydrolysates (H1–H15). Their DPP-IV half maximal inhibitory concentrations (IC50) ranged from 0.55 ± 0.05 to 1.52 ± 0.16 mg L−1 for H8 and H6, respectively. E:S was the only factor having a significant effect on the DPP-IV IC50 value (p < 0.05). Relatively potent α-lactalbumin-derived DPP-IV inhibitory peptides (LAHKPL and ILDKEGIDY) were detected in selected hydrolysates. Additionally, three potent β-CN-derived peptides, VPV, YPI and VPF having DPP-IV IC50 values of 6.6 ± 0.5, 35.0 ± 2.0 and 55.1 ± 5.8 µM, respectively, were identified. After IPI, VPV is the second most potent DPP-IV inhibitory peptide identified to date, which supports the role of camel milk as an antidiabetic agent.

    Original languageEnglish
    Pages (from-to)70-79
    Number of pages10
    JournalFood Chemistry
    Volume279
    DOIs
    Publication statusPublished - May 1 2019

    Keywords

    • Bioactive peptides
    • Camel milk
    • Dipeptidyl peptidase IV inhibition
    • Liquid chromatography tandem mass spectrometry (LC–MS/MS)
    • Trypsin
    • Whey proteins

    ASJC Scopus subject areas

    • Analytical Chemistry
    • Food Science

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