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Curcumin-micellar casein multisite interactions elucidated by surface plasmon resonance.
- Source :
-
International Journal of Biological Macromolecules . Jul2019, Vol. 133, p860-866. 7p. - Publication Year :
- 2019
-
Abstract
- Determine the thermodynamic and kinetic parameters of interaction between micellar casein (MC) and curcumin (CUR) is useful for the application of MC-CUR systems in food products. We used surface plasmon resonance (SPR) and ultraviolet-visible spectrophotometry (UV–vis) to study the complex formation between MC obtained from skimmed milk and CUR, MC carrying capacity, and thermal protection for CUR at a pH of 6.6. An MC could carry about 18,000 molecules of CUR. SPR suggested an enthalpy-driven process (∆H° = −64.63 kJ∙mol−1 and T∆S° ranging from −42.45 to −44.46 kJ∙mol−1). Temperature increased reduced the rate of MC-CUR complex formation and increased its dissociation rate. The activation energy for the formation of MC-CUR activated complexes was negative for association of free MC and CUR molecules (−62.8 kJ mol−1) and positive for dissociation of the thermodynamically stable complexes (1.80 kJ mol−1). MC protected the CUR against its thermal degradation when it was subjected to different temperatures (30, 40, 50, and 60 °C for 5.5 h). This study shows the importance of characterizing MC-small molecules interactions for better application of MC as a nanocarrier. • Micellar casein (MC) of 180 nm can carry about 18,000 molecules of curcumin (CUR). • SPR measurements showed that the MC-CUR complex formation was exothermic. • Temperature increasing reduced MC-CUR association but increased its dissociation rate. • MC exhibited thermal protection for CUR. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01418130
- Volume :
- 133
- Database :
- Academic Search Index
- Journal :
- International Journal of Biological Macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 136743603
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2019.04.166