Characterization and functional properties of pH- and heated time-induced aggregates from red lentil protein

Simple item page
dc.check.date28/07/2024en
dc.check.infoAccess to this article is restricted until 12 months after publication by request of the publisheren
dc.contributor.authorDu, Hanen
dc.contributor.authorLin, Yichenen
dc.contributor.authorStanton, Catherineen
dc.contributor.authorDaniloski, Davoren
dc.contributor.authorZannini, Emanueleen
dc.contributor.authorRoss, R. Paulen
dc.contributor.authorMiao, Songen
dc.contributor.funderTeagascen
dc.contributor.funderHorizon 2020en
dc.date.accessioned2023-12-01T10:08:22Z
dc.date.available2023-12-01T10:08:22Z
dc.date.issued2023-07-28en
dc.description.abstractIn this study, red lentil isolate protein (RLPI, 3 %, w/v) was treated at pH 2 and 7 at 85 °C for a period of 0–24 h. The TEM and SDS-PAGE results indicated that the molecular weight of RLPI was steadily reduced and hydrolyzed into peptides over the prolonged heating time, eventually forming fibrillar and particulate aggregates at pH 2 and 7, respectively. The FTIR results showed an increased level of the proteins’ random coil motifs due to the excessive heating. According to the results of emulsifying properties, the emulsifying capabilities of fibrillar proteins were higher than those of the particle proteins at the same protein concentration due to the proteins’ structure and their surface charge. Notably, the fibrillar aggregates formed a gel network structure and stronger interactions in fibrillar aggregates compared to the particulate aggregates at pH 2. This study provides references for the processing and utilization of plant proteins in beverages and dietary supplements.en
dc.description.sponsorshipTeagasc-The Irish Agriculture and Food Development Authority (Teagasc Walsh Fellow Scheme (reference number 2019241))en
dc.description.statusPeer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid100342en
dc.identifier.citationDu, H., Lin, Y., Stanton, C., Daniloski, D., Zannini, E., Ross, R.P. and Miao, S. (2023) ‘Characterization and functional properties of pH- and heated time-induced aggregates from red lentil protein’, Food Structure, 37, 100342 (12 pp). https://doi.org/10.1016/j.foostr.2023.100342.en
dc.identifier.doi10.1016/j.foostr.2023.100342en
dc.identifier.endpage12en
dc.identifier.issn2213-3291en
dc.identifier.journaltitleFood Structureen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/15284
dc.identifier.volume37en
dc.language.isoenen
dc.publisherElsevieren
dc.relation.ispartofFood Structureen
dc.relation.projectinfo:eu-repo/grantAgreement/EC/H2020::IA/862957/EU/Smart Protein for a Changing World. Future-proof alternative terrestrial protein sources for human nutrition encouraging environment regeneration, processing feasibility and consumer trust and accepta/SMART PROTEINen
dc.rights© 2023 Published by Elsevier Ltd. © This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.subjectPlant proteinen
dc.subjectFibrillaren
dc.subjectParticulateen
dc.subjectAggregationen
dc.subjectStructureen
dc.titleCharacterization and functional properties of pH- and heated time-induced aggregates from red lentil proteinen
dc.typeArticle (peer-reviewed)en
oaire.citation.volume37en
Files
Original bundle
Now showing 1 - 2 of 2
Thumbnail Image
Name:
1-s2.0-S2213329123000357-main.pdf
Size:
4.78 MB
Format:
Adobe Portable Document Format
Description:
Accepted version
Download
Thumbnail Image
Name:
1-s2.0-S2213329123000357-mmc1.docx
Size:
924.44 KB
Format:
Microsoft Word XML
Description:
Appendix
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
2.71 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Food and Nutritional Sciences - Journal Articles