Structure and gelation properties of casein micelles doped with curcumin under acidic conditions. Issue 12 (30th September 2015)
- Record Type:
- Journal Article
- Title:
- Structure and gelation properties of casein micelles doped with curcumin under acidic conditions. Issue 12 (30th September 2015)
- Main Title:
- Structure and gelation properties of casein micelles doped with curcumin under acidic conditions
- Authors:
- Khanji, Aya N.
Michaux, Florentin
Jasniewski, Jordane
Petit, Jeremy
Lahimer, Emna
Cherif, Mohamed
Salameh, Dominique
Rizk, Toufic
Banon, Sylvie - Abstract:
- Abstract : In this study, the ability of micellar casein (MC) to interact with curcumin during acidification and to produce acid gel was investigated. Abstract : In this study, the ability of micellar casein (MC) to interact with curcumin during acidification and to produce acid gel was investigated. Steady-state fluorescence spectroscopy of curcumin variation and fluorescence quenching of caseins upon binding with curcumin molecules were evidenced. Increasing the temperature from 20 to 35 °C enhanced MC–curcumin interactions as reflected by the increase in the binding constant from 0.6 ± 0.3 × 10 4 to 6.6 ± 0.6 × 10 4 M −1 . From changes in entropy, enthalpy and Gibbs free energy, hydrophobic interactions were proposed as major binding forces. Static fluorescence MC quenching was demonstrated for the MC–curcumin complex during acidification. From pH 7.4 to pH 5.0, the binding site numbers varied in the range from 1.25 ± 0.05 to 1.49 ± 0.05 and the binding constant k b varied from 3.9 ± 0.4 × 10 4 to 7.5 ± 0.7 × 10 4 M −1 . Small angle X-ray scattering profiles demonstrated that the MC internal structure was unchanged upon curcumin binding. The ζ-potential value of curcumin-doped MC indicated that curcumin did not modify the global charge of MC particles. Acid gelation studied by oscillation rheology and static multiple light scattering at 20 and 35 °C led to a similar behavior for native and curcumin-doped MC suspensions. For the first time, it was demonstrated that theAbstract : In this study, the ability of micellar casein (MC) to interact with curcumin during acidification and to produce acid gel was investigated. Abstract : In this study, the ability of micellar casein (MC) to interact with curcumin during acidification and to produce acid gel was investigated. Steady-state fluorescence spectroscopy of curcumin variation and fluorescence quenching of caseins upon binding with curcumin molecules were evidenced. Increasing the temperature from 20 to 35 °C enhanced MC–curcumin interactions as reflected by the increase in the binding constant from 0.6 ± 0.3 × 10 4 to 6.6 ± 0.6 × 10 4 M −1 . From changes in entropy, enthalpy and Gibbs free energy, hydrophobic interactions were proposed as major binding forces. Static fluorescence MC quenching was demonstrated for the MC–curcumin complex during acidification. From pH 7.4 to pH 5.0, the binding site numbers varied in the range from 1.25 ± 0.05 to 1.49 ± 0.05 and the binding constant k b varied from 3.9 ± 0.4 × 10 4 to 7.5 ± 0.7 × 10 4 M −1 . Small angle X-ray scattering profiles demonstrated that the MC internal structure was unchanged upon curcumin binding. The ζ-potential value of curcumin-doped MC indicated that curcumin did not modify the global charge of MC particles. Acid gelation studied by oscillation rheology and static multiple light scattering at 20 and 35 °C led to a similar behavior for native and curcumin-doped MC suspensions. For the first time, it was demonstrated that the colloidal and functional properties of MC were unchanged when doped with curcumin during acidification. … (more)
- Is Part Of:
- Food & function. Volume 6:Issue 12(2015)
- Journal:
- Food & function
- Issue:
- Volume 6:Issue 12(2015)
- Issue Display:
- Volume 6, Issue 12 (2015)
- Year:
- 2015
- Volume:
- 6
- Issue:
- 12
- Issue Sort Value:
- 2015-0006-0012-0000
- Page Start:
- 3624
- Page End:
- 3633
- Publication Date:
- 2015-09-30
- Subjects:
- Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Nutrition -- Periodicals
664.07 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/FO ↗
http://pubs.rsc.org/en/journals/journal/fo ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c5fo00829h ↗
- Languages:
- English
- ISSNs:
- 2042-6496
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.038457
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 28.xml