2013
DOI: 10.1016/j.foodhyd.2013.01.007
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Effect of phospholipid molecular structure on its interaction with whey proteins in aqueous solution

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Cited by 39 publications
(14 citation statements)
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“…As suggested above (cf. Section 3.2), this phenomenon could also take place when the oil phase is organized into liposomes (Kasinos, Sabatino, Vanloo, Gevaert, Martins, & Van der Meeren, 2013), explaining the additional protective effect provided by the protein matrix, despite being water-dispersible. These results are in agreement with those recently reported by Frenzel and co-workers (M. Frenzel, Krolak, Wagner, & Steffen-Heins, 2015), who showed that whey protein coatings increased the physical stability of soy phospholipids-based liposomes and reduced their bilayer semi-permeability.…”
Section: Insert Figure About Herementioning
confidence: 98%
See 1 more Smart Citation
“…As suggested above (cf. Section 3.2), this phenomenon could also take place when the oil phase is organized into liposomes (Kasinos, Sabatino, Vanloo, Gevaert, Martins, & Van der Meeren, 2013), explaining the additional protective effect provided by the protein matrix, despite being water-dispersible. These results are in agreement with those recently reported by Frenzel and co-workers (M. Frenzel, Krolak, Wagner, & Steffen-Heins, 2015), who showed that whey protein coatings increased the physical stability of soy phospholipids-based liposomes and reduced their bilayer semi-permeability.…”
Section: Insert Figure About Herementioning
confidence: 98%
“…A similar phenomenon could take place in the prepared liposome dispersions, where the liposomes would act as self-organized oil droplets, which would interact with the exposed non-polar residues of the protein. Previous works have already suggested that phospholipids can modify the secondary structure of whey proteins due to hydrophobic interactions (Kasinos, Sabatino, Vanloo, Gevaert, Martins, & Van der Meeren, 2013), allowing even the insertion of whey proteins into the liposomal membrane (Monika .…”
Section: Hybrid Electrosprayed Capsulesmentioning
confidence: 99%
“…Although the incorporation of curcumin within the zein fibers did not modify their thermal stability, most probably due to the low curcumin to zein ratio employed, the degradation of the gelatin fibers occurred at a slightly lower temperature when they were loaded with curcumin. In this latter case, the bioactive compound was incorporated in the form of liposomal curcumin, and phospholipids have been previously described to interact with proteins through hydrophobic interactions, altering their secondary structure (Kasinos et al, 2013). gests that effect on the gelatin fibers, which also had an impact on their release and stabilization properties (cf.…”
Section: Ft-ir Spectroscopy Analysismentioning
confidence: 99%
“…The α-helix configuration presents an intense and positive band at 190 nm and negative peaks at 208 and 220 nm, while β-sheet configuration presents a negative dichroic peak with a minimum in the 215 nm region. Random coil structures generally have a positive CD peak near 215 nm and a negative one near to 200 nm (Barreto et al, 2003;Kasinos et al, 2013). Unheated lactoferrin presented an ellipticity minimum near 210 nm (Fig.…”
Section: Ansmentioning
confidence: 93%