2013
DOI: 10.1016/j.foodchem.2012.12.017
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Interaction of curcumin with phosphocasein micelles processed or not by dynamic high-pressure

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Cited by 53 publications
(24 citation statements)
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“…The gel strength increased with increasing high-pressure treatment (Johnston et al 1992;Desobry-Banon et al 1994) and a syneresis resistance was observed. Highpressure treatments appear as an interesting tool to entrap different ligands like curcumin, vitamin D 2 , and α-tocopherol (Benzaria et al 2013;Menéndez-Aguirre et al 2011;Chevalier-Lucia et al 2011). It increases the binding constant of these compounds to casein micelles.…”
Section: High Pressurementioning
confidence: 99%
“…The gel strength increased with increasing high-pressure treatment (Johnston et al 1992;Desobry-Banon et al 1994) and a syneresis resistance was observed. Highpressure treatments appear as an interesting tool to entrap different ligands like curcumin, vitamin D 2 , and α-tocopherol (Benzaria et al 2013;Menéndez-Aguirre et al 2011;Chevalier-Lucia et al 2011). It increases the binding constant of these compounds to casein micelles.…”
Section: High Pressurementioning
confidence: 99%
“…8), only < 7% of the total amount of RIT being found free in UCF-supernatants. This is according to Benzaria et al (20), who in a study on the effect of dynamic high-pressure on the interaction of curcumin with phosphocasein micelles (PC), observed that digestibility of PC–curcumin complexes were quite resistant to in vitro pepsin treatment. Such results indicate that casein proteins strongly retain RIT in conditions simulating the stomach environment, which might be attributed to that under acidic conditions of gastric solution casein proteins precipitate along with RIT, preventing its release.…”
Section: Resultsmentioning
confidence: 89%
“…The exposure of hydrophobic residues of the individual casein proteins during homogenization at ca. 300 MPa and micellar reassociation has shown to be an efficient method for the binding of hydrophobic compounds such as curcumin (20), triclosan (21), and α-tocopherol acetate (7). However, to the best of our knowledge, no studies on the effect of homogenization pressures higher than 400 MPa on the loading capacity of casein micelles were reported.…”
Section: Introductionmentioning
confidence: 99%
“…In their native state, caseins usually exist as molecular clusters ("casein micelles") that are typically between about 50 and 250 nm in diameter and are partly held together by mineral ions (such as calcium phosphate). Casein micelles may be useful for the development of delivery systems because they can encapsulate lipophilic bioactives in their non-polar interiors, such as carotenoids, curcumin, and oil-soluble vitamins [83][84][85][86]. Caseins are amphiphilic molecules that have good surface-activity and can therefore be used as emulsifiers to stabilize lipid droplets.…”
Section: Caseinmentioning
confidence: 99%