Whey protein isolate polydispersity affects enzymatic hydrolosis outcomes
dc.contributor.author | O'Loughlin, Ian B. | * |
dc.contributor.author | Murray, Brian A. | * |
dc.contributor.author | Brodkorb, Andre | * |
dc.contributor.author | Fitzgerald, Richard J. | * |
dc.contributor.author | Robinson, A. A. | * |
dc.contributor.author | Holton, T. A. | * |
dc.contributor.author | Kelly, Tom A. | * |
dc.date.accessioned | 2013-12-09T17:09:07Z | |
dc.date.available | 2014-06-01T16:00:04Z | |
dc.date.issued | 24/05/2013 | |
dc.identifier.citation | I.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.2013.05.056 | en_GB |
dc.identifier.issn | 0308-8146 | |
dc.identifier.uri | http://hdl.handle.net/11019/473 | |
dc.description | peer-reviewed | en_GB |
dc.description.abstract | The 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 release | en_GB |
dc.description.sponsorship | The 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.iso | en | en_GB |
dc.publisher | Elsevier | en_GB |
dc.relation.ispartofseries | Food Chemistry;vol 141(3) | |
dc.subject | Heat-treatment | en_GB |
dc.subject | Whey protein isolate | en_GB |
dc.subject | Enzynatic hydrolysis | en_GB |
dc.subject | Peptide analysis | en_GB |
dc.subject | Essential amino acids | en_GB |
dc.title | Whey protein isolate polydispersity affects enzymatic hydrolosis outcomes | en_GB |
dc.type | Article | en_GB |
dc.embargo.terms | 24/05/2014 | en_GB |
dc.identifier.rmis | MDDT-0106-5940 | |
dc.identifier.doi | http://dx.doi.org/10.1016/j.foodchem.2013.05.056 | |
dc.contributor.sponsor | Teagasc Walsh Fellowship Programme | |
dc.contributor.sponsor | Enterprise Ireland | |
dc.contributor.sponsorGrantNumber | CC/2008/0001/A. | |
refterms.dateFOA | 2019-06-14T07:10:26Z |