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Molecular structure-affinity relationship of selected phenolic compounds for lupin seed γ-conglutin

cris.virtual.author-orcid0000-0001-8799-1748
cris.virtual.author-orcid0000-0002-1438-1217
cris.virtualsource.author-orcide45381b5-f3f6-460d-9d8e-5fca34e39285
cris.virtualsource.author-orcid1c802429-36ee-40e7-b72f-32f16b32d8de
dc.abstract.enThe molecular basis underlying the interaction between proteins and phenolic compounds are still not fully understood. The specific structural properties of proteins, as well as phenolics, strongly determine the complex formation. In this work, the interactions between γ-conglutin, a unique lupin seed protein, and twenty-one different phenolic compounds representing six different classes of phenolics that differ in their structures were investigated. The interactions were studied based on a fluorescence quenching experiment, and the determined binding constant (Ka) ranged from 6.88 × 102 (protocatechuic acid) to 5.06 × 106 (hesperidin), while the number of binding sites of phenolic compound molecules to the protein (n) was on average 1.14 ± 0.16. Within the analysed compounds, phenolic acids interacted the weakest with the protein, while flavonoids showed considerable higher affinity strength to γ-conglutin. Notably, flavanones and flavones were the phenolics that formed the complex with markedly higher values of Ka (1-3 orders of magnitude) and n. Additionally, principal component analysis allowed to formulate the general regularities of phenolic compounds preferences for γ-conglutin. Finally, the obtained results also indicate that phenolic compounds' binding preferences for γ-conglutin can result from their native occurrence in lupin seeds
dc.affiliationWydział Nauk o Żywności i Żywieniu
dc.affiliation.instituteKatedra Biochemii i Analizy Żywności
dc.contributor.authorCzubiński, Jarosław
dc.contributor.authorDwiecki, Krzysztof
dc.date.accessioned2025-09-16T09:26:26Z
dc.date.available2025-09-16T09:26:26Z
dc.date.issued2022
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if10,7
dc.description.numberJuly 2022
dc.description.points140
dc.description.volume128
dc.identifier.doi10.1016/j.foodhyd.2022.107561
dc.identifier.eissn1873-7137
dc.identifier.issn0268-005X
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/4812
dc.languageen
dc.relation.ispartofFood Hydrocolloids
dc.relation.pagesart. 107561
dc.rightsClosedAccess
dc.sciencecloudnosend
dc.subject.enprotein-phenolic compounds interaction
dc.subject.enγ-conglutin
dc.subject.enphenolic acids
dc.subject.enflavonoids
dc.subject.enfluorescence quenching
dc.titleMolecular structure-affinity relationship of selected phenolic compounds for lupin seed γ-conglutin
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.volume128