Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate
dc.contributor.author | Le Maux, Solene | * |
dc.contributor.author | Nongonierma, Alice B. | * |
dc.contributor.author | Murray, Brian A. | * |
dc.contributor.author | Kelly, Philip | * |
dc.contributor.author | Fitzgerald, Richard J. | * |
dc.date.accessioned | 2015-11-30T15:03:34Z | |
dc.date.available | 2016-10-01T16:00:07Z | |
dc.date.issued | 16/09/2015 | |
dc.identifier.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 | en_GB |
dc.identifier.issn | 0963-9969 | |
dc.identifier.uri | http://hdl.handle.net/11019/912 | |
dc.description | The work described herein was supported by Enterprise Ireland under Grant Number TC2013-0001. The research was part funded by the Science Foundation Ireland Research Infrastructure Fund. | |
dc.description | peer-reviewed | en_GB |
dc.description.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. | en_GB |
dc.description.sponsorship | Enterprise Ireland Grant Number TC2013-0001. | en_GB |
dc.language.iso | en | en_GB |
dc.publisher | Elsevier | en_GB |
dc.relation.ispartofseries | Food Research International;vol 77 | |
dc.subject | Bioactive peptides | en_GB |
dc.subject | Mass spectrometry | en_GB |
dc.subject | Short peptides | en_GB |
dc.subject | Retention time | en_GB |
dc.subject | Dipeptidyl peptidase IV inhibition | en_GB |
dc.title | Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate | en_GB |
dc.type | Article | en_GB |
dc.embargo.terms | 16/09/2016 | en_GB |
dc.identifier.rmis | 5940 | |
dc.identifier.doi | http://dx.doi.org/10.1016/j.foodres.2015.09.012 | |
dc.contributor.sponsor | Enterprise Ireland | |
dc.contributor.sponsorGrantNumber | TC2013-0001 | |
refterms.dateFOA | 2018-01-12T08:27:48Z |
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Food Biosciences [567]
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Food Biosciences [567]