Skip to Main content Skip to Navigation
Journal articles

Unraveling the molecular mechanisms underlying interactions between caseins and lutein

Abstract : Understanding the food protein binding to bioactive compounds is of utmost importance for the development of efficient protein-based delivery systems. The binding of lutein to sodium caseinate (NaCas) or native casein micelle (PPCN) was investigated at pH 7 to evaluate the effect of casein supramolecular structures on the interaction. Fluorescence quenching, UV-vis spectroscopy, and dynamic light scattering were carried out. Under the medium conditions of interaction analysis (DMSO-water and ethanol-water), lutein exists as H-type aggregates. The investigation of lutein/casein interaction showed a predominantly static mechanism of fluorescence quenching and the presence of two fluorophore populations on NaCas and PPCN, but only one accessible to lutein. Moreover, the Scatchard plot indicated that lutein interacted with both caseins in one binding site. The interaction of lutein with caseins occurred with binding constant K b of 10 5 M − 1 , regardless of casein supramo-lecular structure.
Document type :
Journal articles
Complete list of metadatas

Cited literature [32 references]  Display  Hide  Download

https://hal.inrae.fr/hal-02977863
Contributor : Anne Giboulot <>
Submitted on : Monday, October 26, 2020 - 10:17:10 AM
Last modification on : Wednesday, October 28, 2020 - 2:57:50 PM

File

1-s2.0-S0963996920308061-main....
Files produced by the author(s)

Licence


Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives 4.0 International License

Identifiers

Citation

Raphaela Mantovani, Pascaline Hamon, Florence Rousseau, Guilherme Tavares, Adriana Zerlotti Mercadante, et al.. Unraveling the molecular mechanisms underlying interactions between caseins and lutein. Food Research International, Elsevier, 2020, 138, pp.109781. ⟨10.1016/j.foodres.2020.109781⟩. ⟨hal-02977863⟩

Share

Metrics

Record views

46

Files downloads

23