2011
DOI: 10.1016/j.ifset.2011.07.007
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Processing of phosphocasein dispersions by dynamic high pressure: Effects on the dispersion physico-chemical characteristics and the binding of α-tocopherol acetate to casein micelles

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Cited by 46 publications
(23 citation statements)
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References 51 publications
(76 reference statements)
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“…Lower viscosity was measured in UHPH treated samples of phospho-casein compared with samples without UHPH treatment by Chevalier-Lucia et al (2011), which agree with our results.…”
Section: Rheological Measurementssupporting
confidence: 92%
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“…Lower viscosity was measured in UHPH treated samples of phospho-casein compared with samples without UHPH treatment by Chevalier-Lucia et al (2011), which agree with our results.…”
Section: Rheological Measurementssupporting
confidence: 92%
“…It also contained larger casein micelles (Chevalier-Lucia et al, 2011) and can be expected to have thicker electrical double layers surrounding the casein micelles due to higher ionic strength in the solution (Walstra, 2003). The subsequent rearrangement following UHPH treatment and the resulting microstructure formation will thus be different for the two samples and in samples with low mineral content probably a more diffuse network with more water protein interaction sites will be observed, hence the decreased relaxation time.…”
Section: Low Field Nuclear Magnetic Resonancementioning
confidence: 99%
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“…Among these, considerable interest in recent years has been shown in the use of carrier systems based on food proteins because they are comparatively inexpensive, widely available, non-toxic (Generally Recognized As Safe, GRAS), biodegradable, and have nutritional value and good sensory properties (7). Commonly used natural food proteins include albumin and gelatin (8); however, although this topic has recently retained attention, there is limited research regarding the use of milk proteins (e.g., whey protein and caseins).…”
Section: Introductionmentioning
confidence: 99%
“…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%