Effect of different oligomerisation assemblies of γ‐conglutin on its interaction behaviour with vitexin

Background

Several different factors underline molecular mechanisms of phenolic compound‐protein interactions, one of which is environmental conditions. In the case of γ‐conglutin, pH conditions directly translate into the adaptation of two distinct oligomeric assemblies, i.e. hexameric (pH 7.5) or monomeric (pH 4.5). Herein, the pH‐dependent oligomerisation of γ‐conglutin in terms of its ability to form complexes with model flavonoid (vitexin) was studied.

Results

Fluorescence quenching thermodynamic measurements indicate that hydrogen bonds, electrostatic forces and van der Waals interactions were the main driving forces involved in the complex formation. The interaction turns 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 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 obtained data show precisely how the environmental conditions might directly influence the phenolic compounds‐proteins complex formation. This knowledge is essential for the preparation of food products containing γ‐conglutin. We also believes that the described results will contribute to a better understanding of the detailed fate of this unique health‐promoting lupin seed protein after its intake.

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