dc.contributor.author | Madsen, Mikkel | |
dc.contributor.author | Khan, Sanaullah | |
dc.contributor.author | Kunstmann, Sonja | |
dc.contributor.author | Aachmann, Finn Lillelund | |
dc.contributor.author | Ipsen, Richard | |
dc.contributor.author | Westh, Peter | |
dc.contributor.author | Emanuelsson, Cecilia | |
dc.contributor.author | Svensson, Birte | |
dc.date.accessioned | 2023-04-26T05:48:39Z | |
dc.date.available | 2023-04-26T05:48:39Z | |
dc.date.created | 2022-11-16T12:26:15Z | |
dc.date.issued | 2022 | |
dc.identifier.citation | Food Chemistry: Molecular Sciences. 2022, 5 . | en_US |
dc.identifier.issn | 2666-5662 | |
dc.identifier.uri | https://hdl.handle.net/11250/3065018 | |
dc.description.abstract | There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO3, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t1/2 = 3 h, while the polymerization occurred with t1/2 = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/deed.no | * |
dc.title | Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles | en_US |
dc.title.alternative | Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles | en_US |
dc.type | Peer reviewed | en_US |
dc.type | Journal article | en_US |
dc.description.version | publishedVersion | en_US |
dc.source.pagenumber | 11 | en_US |
dc.source.volume | 5 | en_US |
dc.source.journal | Food Chemistry: Molecular Sciences | en_US |
dc.identifier.doi | 10.1016/j.fochms.2022.100137 | |
dc.identifier.cristin | 2074795 | |
dc.source.articlenumber | 100137 | en_US |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |