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dc.contributor.authorO'Loughlin, Ian B.
dc.contributor.authorMurray, Brian A.
dc.contributor.authorBrodkorb, Andre
dc.contributor.authorFitzgerald, Richard J.
dc.contributor.authorRobinson, A. A.
dc.contributor.authorHolton, T. A.
dc.contributor.authorKelly, Tom A.
dc.date.accessioned2013-12-09T17:09:07Z
dc.date.available2014-06-01T16:00:04Z
dc.date.issued24/05/2013
dc.identifier.citationI.B. O’Loughlin, B.A. Murray, A. Brodkorb, R.J. FitzGerald, A.A. Robinson, T.A. Holton, P.M. Kelly. Whey protein isolate polydispersity affects enzymatic hydrolysis outcomes. Food Chemistry, 2013, 141(3), 2334-2342. DOI: 10.1016/j.foodchem.2013.05.056en_GB
dc.identifier.issn0308-8146
dc.identifier.urihttp://hdl.handle.net/11019/473
dc.descriptionpeer-revieweden_GB
dc.description.abstractThe effects of heat-induced denaturation of whey protein isolate (WPI) on the enzymatic breakdown of α-La, caseinomacropeptide (CMP), β-Lg A and β-Lg B were observed as hydrolysis proceeded to a 5% degree of hydrolysis (DH) in both unheated and heat-treated (80 °C, 10 min) WPI dispersions (100 g L−1). Hydrolysis of denatured WPI favoured the generation of higher levels of free essential amino acids; lysine, phenylalanine and arginine compared to the unheated substrate. LC–MS/MS identified 23 distinct peptides which were identified in the denatured WPI hydrolysate – the majority of which were derived from β-Lg. The mapping of the detected regions in α-La, β-Lg, and CMP enabled specific cleavage points to be associated with certain serine endo-protease activities. The outcomes of the study emphasise how a combined approach of substrate heat pre-treatment and enzymology may be used to influence proteolysis with attendant opportunities for targeting unique peptide production and amino acid releaseen_GB
dc.description.sponsorshipThe work herein was funded by Enterprise Ireland (EI) as part of the Food for Health Ireland project. I. B. O’Loughlin is a Teagasc Walsh Fellow supported by EI grant number CC/2008/0001/A.
dc.language.isoenen_GB
dc.publisherElsevieren_GB
dc.relation.ispartofseriesFood Chemistry;vol 141(3)
dc.subjectHeat-treatmenten_GB
dc.subjectWhey protein isolateen_GB
dc.subjectEnzynatic hydrolysisen_GB
dc.subjectPeptide analysisen_GB
dc.subjectEssential amino acidsen_GB
dc.titleWhey protein isolate polydispersity affects enzymatic hydrolosis outcomesen_GB
dc.typeArticleen_GB
dc.embargo.terms24/05/2014en_GB
dc.identifier.rmisMDDT-0106-5940
dc.identifier.doihttp://dx.doi.org/10.1016/j.foodchem.2013.05.056
dc.contributor.sponsorTeagasc Walsh Fellowship Programme
dc.contributor.sponsorEnterprise Ireland
dc.contributor.sponsorGrantNumberCC/2008/0001/A.


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