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dc.contributor.authorLe Maux, Solene*
dc.contributor.authorNongoniermaa, Alice B.*
dc.contributor.authorMurray, Brian*
dc.contributor.authorKelly, Philip M.*
dc.contributor.authorFitzgerald, Richard J.*
dc.date.accessioned2015-11-30T15:03:34Z
dc.date.available2016-10-01T16:00:07Z
dc.date.issued16/09/2015
dc.identifier.citationLe 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.2015.09.012en_GB
dc.identifier.issn0963-9969
dc.identifier.urihttp://hdl.handle.net/11019/912
dc.descriptionThe 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.descriptionpeer-revieweden_GB
dc.description.abstractShort 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.sponsorshipEnterprise Ireland Grant Number TC2013-0001.en_GB
dc.language.isoenen_GB
dc.publisherElsevieren_GB
dc.relation.ispartofseriesFood Research International;vol 77
dc.subjectBioactive peptidesen_GB
dc.subjectMass spectrometryen_GB
dc.subjectShort peptidesen_GB
dc.subjectRetention timeen_GB
dc.subjectDipeptidyl peptidase IV inhibitionen_GB
dc.titleIdentification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysateen_GB
dc.typeArticleen_GB
dc.embargo.terms16/09/2016en_GB
dc.identifier.rmis5940
dc.identifier.doihttp://dx.doi.org/10.1016/j.foodres.2015.09.012
dc.contributor.sponsorEnterprise Ireland
dc.contributor.sponsorGrantNumberTC2013-0001
refterms.dateFOA2018-01-12T08:27:48Z


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