Effect of different oligomerization assemblies of γ-conglutin on its interaction behavior with vitexin
| cris.virtual.author-orcid | 0000-0001-8799-1748 | |
| cris.virtual.author-orcid | 0000-0002-1438-1217 | |
| cris.virtualsource.author-orcid | e45381b5-f3f6-460d-9d8e-5fca34e39285 | |
| cris.virtualsource.author-orcid | 1c802429-36ee-40e7-b72f-32f16b32d8de | |
| dc.abstract.en | BACKGROUND Several different factors underlie the molecular mechanisms of phenolic compound-protein interactions. They include the environmental conditions. In the case of γ-conglutin, pH conditions translate directly into the adoption of two distinct oligomeric assemblies, i.e. hexameric (pH 7.5) or monomeric (pH 4.5). This paper reports research on the pH-dependent oligomerization of γ-conglutin in terms of its ability to form complexes with a model flavonoid (vitexin). RESULTS Fluorescence-quenching thermodynamic measurements indicate that hydrogen bonds, electrostatic forces, and van der Waals interactions are the main driving forces involved in the complex formation. The interaction turned out to be a spontaneous and exothermic process. Assessment of structural composition (secondary structure changes and arrangement/dynamics of aromatic amino acids), molecular size, and the thermal stability of the different oligomeric forms showed that γ-conglutin in a monomeric state was less affected by vitexin during the interaction. CONCLUSION The data show precisely how environmental conditions might influence phenolic compound-protein complex formation directly. This knowledge is essential for the preparation of food products containing γ-conglutin. The results can contribute to a better understanding of the detailed fate of this unique health-promoting lupin seed protein after its intake. © 2023 Society of Chemical Industry. | |
| dc.abstract.pl | - | |
| dc.affiliation | Wydział Nauk o Żywności i Żywieniu | |
| dc.affiliation.institute | Katedra Biochemii i Analizy Żywności | |
| dc.contributor.author | Czubiński, Jarosław Edward | |
| dc.contributor.author | Dwiecki, Krzysztof | |
| dc.date.accessioned | 2025-03-05T07:56:41Z | |
| dc.date.available | 2025-03-05T07:56:41Z | |
| dc.date.issued | 2024 | |
| dc.description.abstract | <jats:title>Abstract</jats:title><jats:sec><jats:title>BACKGROUND</jats:title><jats:p>Several different factors underlie the molecular mechanisms of phenolic compound‐protein interactions. They include the environmental conditions. In the case of <jats:italic>γ</jats:italic>‐conglutin, pH conditions translate directly into the adoption of two distinct oligomeric assemblies, i.e. hexameric (pH 7.5) or monomeric (pH 4.5). This paper reports research on the pH‐dependent oligomerization of <jats:italic>γ</jats:italic>‐conglutin in terms of its ability to form complexes with a model flavonoid (vitexin).</jats:p></jats:sec><jats:sec><jats:title>RESULTS</jats:title><jats:p>Fluorescence‐quenching thermodynamic measurements indicate that hydrogen bonds, electrostatic forces, and van der Waals interactions are the main driving forces involved in the complex formation. The interaction turned out to be a spontaneous and exothermic process. Assessment of structural composition (secondary structure changes and arrangement/dynamics of aromatic amino acids), molecular size, and the thermal stability of the different oligomeric forms showed that <jats:italic>γ</jats:italic>‐conglutin in a monomeric state was less affected by vitexin during the interaction.</jats:p></jats:sec><jats:sec><jats:title>CONCLUSION</jats:title><jats:p>The data show precisely how environmental conditions might influence phenolic compound‐protein complex formation directly. This knowledge is essential for the preparation of food products containing <jats:italic>γ</jats:italic>‐conglutin. The results can contribute to a better understanding of the detailed fate of this unique health‐promoting lupin seed protein after its intake. © 2023 Society of Chemical Industry.</jats:p></jats:sec> | |
| dc.description.bibliography | il., bibliogr. | |
| dc.description.finance | publication_nocost | |
| dc.description.financecost | 0,00 | |
| dc.description.if | 3,3 | |
| dc.description.number | 6 | |
| dc.description.points | 100 | |
| dc.description.volume | 104 | |
| dc.identifier.doi | 10.1002/jsfa.13223 | |
| dc.identifier.eissn | 1097-0010 | |
| dc.identifier.issn | 0022-5142 | |
| dc.identifier.uri | https://sciencerep.up.poznan.pl/handle/item/2541 | |
| dc.language | en | |
| dc.pbn.affiliation | food and nutrition technology | |
| dc.relation.ispartof | Journal of the Science of Food and Agriculture | |
| dc.relation.pages | 3381-3391 | |
| dc.relation.project | National Science Centre, Poland (Project No. 2015/19/D/NZ9/00065) | |
| dc.rights | ClosedAccess | |
| dc.sciencecloud | send | |
| dc.subject.en | phenolic compound-protein interactions | |
| dc.subject.en | γ-conglutin | |
| dc.subject.en | lupin seed | |
| dc.subject.en | vitexin | |
| dc.subject.en | thermodynamics | |
| dc.subject.en | fluorescence quenching | |
| dc.title | Effect of different oligomerization assemblies of γ-conglutin on its interaction behavior with vitexin | |
| dc.type | JournalArticle | |
| dspace.entity.type | Publication | |
| oaire.citation.issue | 6 | |
| oaire.citation.volume | 104 | |
| project.funder.name | National Science Centre, Poland (Project No. 2015/19/D/NZ9/00065). |