Digestive diversity and kinetic intrigue among heated and unheated β-lactoglobulin species.

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dc.citation.issue11
dc.citation.volume5
dc.contributor.authorLoveday SM
dc.contributor.authorPeram MR
dc.contributor.authorSingh H
dc.contributor.authorYe A
dc.contributor.authorJameson GB
dc.date.available2014-11-01
dc.date.issued2014-11
dc.description.abstractFood processing often alters the structure of proteins, and proteins are deliberately denatured and aggregated to improve technological functionality in many cases. However, the digestive consequences of processing-induced alterations to protein structure have only recently been studied. Here we explored the process-structure-digestibility relationship in the context of heat-processing effects on the structure and gastric digestibility of the bovine whey protein β-lactoglobulin (β-lg). Heating β-lg produces an array of non-native monomers, dimers and aggregates, and we have characterised these with reverse-phase high performance liquid chromatography (RP-HPLC) as a complement to our earlier work using polyacrylamide gel electrophoresis (PAGE) techniques. Using a combination of SDS-PAGE and RP-HPLC we have identified pepsin-resistant dimers and peptides that appear early in digestion. In an unexpected finding, native β-lg underwent complete hydrolysis during prolonged incubation (48 h) with pepsin. Two phases of hydrolysis were identified, and the transition between phases appears to result from alterations to the secondary structure of β-lg at 3-4 h, as measured with circular dichroism spectroscopy, and/or the binding and release of a pepsin inhibitor peptide. This work has unpacked some of the complexities of the processing-structure-digestibility relationship in a highly simplified system; further work is needed to explore the implications of these findings for food processors, regulatory authorities and consumers.
dc.description.publication-statusPublished
dc.format.extent2783 - 2791 (9)
dc.identifierhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000344320600011&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=c5bb3b2499afac691c2e3c1a83ef6fef
dc.identifier.citationFOOD & FUNCTION, 2014, 5 (11), pp. 2783 - 2791 (9)
dc.identifier.doi10.1039/c4fo00362d
dc.identifier.elements-id218371
dc.identifier.harvestedMassey_Dark
dc.identifier.issn2042-6496
dc.languageEnglish
dc.publisherROYAL SOC CHEMISTRY
dc.relation.isPartOfFOOD & FUNCTION
dc.relation.replaceshttp://hdl.handle.net/123456789/224
dc.relation.replaces123456789/224
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectBiochemistry & Molecular Biology
dc.subjectFood Science & Technology
dc.subjectIN-VITRO DIGESTION
dc.subjectFOOD PROTEINS
dc.subjectPEPSIN
dc.subjectPROTEOLYSIS
dc.subjectDENATURATION
dc.subjectHYDROLYSIS
dc.subjectRESISTANCE
dc.subjectCOMPLEXES
dc.subjectAPPETITE
dc.subjectSTOMACH
dc.subject.anzsrc0908 Food Sciences
dc.titleDigestive diversity and kinetic intrigue among heated and unheated β-lactoglobulin species.
dc.typeJournal article
pubs.notesNot known
pubs.organisational-group/Massey University
pubs.organisational-group/Massey University/College of Sciences
pubs.organisational-group/Massey University/College of Sciences/School of Fundamental Sciences
pubs.organisational-group/Massey University/Other
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