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    Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate

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    Author
    Le Maux, Solene
    Nongoniermaa, Alice B.
    Murray, Brian
    Kelly, Philip M.
    Fitzgerald, Richard J.
    Keyword
    Bioactive peptides
    Mass spectrometry
    Short peptides
    Retention time
    Dipeptidyl peptidase IV inhibition
    Date
    2015-09-16
    
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    URI
    http://hdl.handle.net/11019/912; http://dx.doi.org/10.1016/j.foodres.2015.09.012
    Citation
    Le Maux, S., Nongonierma, A.B., Murray, B., Kelly, P.M.& FitzGerald, R.J., Identification of short peptide sequences in the nanofiltration permeateof a bioactive whey protein hydrolysate, Food Research International (2015), 77(3), 534-539, doi:10.1016/j.foodres.2015.09.012
    Abstract
    Short peptides in food protein hydrolysates are of significant interest as they may be highly bioactive whilst also being bioavailable. A dipeptidyl peptidase IV (DPP-IV) inhibitory whey protein hydrolysate (WPH) was fractionated using nanofiltration (NF) with a 200 Da MWCO membrane. The DPP-IV half maximal inhibitory concentration of the NF permeate (IC50 = 0.66 ± 0.08 mg protein equivalent mL− 1) was significantly more potent (P > 0.05) than that of the starting WPH (IC50 = 0.94 ± 0.24 mg protein equivalent mL− 1) and associated retentate (IC50 = 0.82 ± 0.13 mg protein equivalent mL− 1). This confirmed the contribution of short peptides within the NF permeate to the overall DPP-IV inhibitory activity. An hydrophilic interaction liquid chromatography (HILIC-) and reverse-phase (RP-) liquid chromatography tandem mass spectrometry (LC–MS/MS) strategy, based on two retention time models, allowed detection of eight free amino acids and eight di- to tetrapeptides in the NF permeate. The potential sequences of the peptides within the NF permeate were then ranked on the basis of their highest probability of occurrence. A confirmatory study with synthetic peptides showed that valine–alanine (VA), valine–leucine (VL), tryptophan–leucine (WL) and tryptophan–isoleucine (WI) displayed DPP-IV IC50 values < 170 μM. The NF and LC–MS strategies employed herein represent a new approach for the targeted identification of short peptides within bioactive food protein hydrolysates.
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