2006
DOI: 10.1016/j.idairyj.2005.10.010
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Casein phosphopeptides released by simulated gastrointestinal digestion of infant formulas and their potential role in mineral binding

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Cited by 43 publications
(22 citation statements)
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“…This could at least partially explain the lowest solubility percentage in sample FbFeZn, though in the present study the molar ratio of zinc to iron was 0.5 : 1. Such negative interaction seems to be countered by the presence of milk‐derived caseinophosphopeptides formed during the gastrointestinal digestion of native milk casein (Miquel et al. , 2006).…”
Section: Resultsmentioning
confidence: 99%
“…This could at least partially explain the lowest solubility percentage in sample FbFeZn, though in the present study the molar ratio of zinc to iron was 0.5 : 1. Such negative interaction seems to be countered by the presence of milk‐derived caseinophosphopeptides formed during the gastrointestinal digestion of native milk casein (Miquel et al. , 2006).…”
Section: Resultsmentioning
confidence: 99%
“…The use of sequential hydrolysis with pepsin and pancreatin has been shown to release phosphorylated sequences previously reported in vivo, also in infant formula employing suitable conditions (Miquel et al, 2005). Moreover, isolation of the CPP fraction by selective precipitation or TiO2 chromatography allowed to identify several sequences containing the phosphorylated cluster (Miquel et al, 2006;Picariello et al, 2010). Adt et al compared the number of sites of phosphorylation of CPPs in non-digested and digested Beaufort cheese samples, and found a decrease in the number of polyphosphorylated peptides (Adt et al, 2011).…”
Section: Comparison Of Bioactive Sequences Found In Vitro and In Vivomentioning
confidence: 97%
“…The difference is likely due to the chemical structure of peptides, as the authors found that inhibition of the intestinal phosphatase significantly increased the uptake and the absorption of β-CPPs-iron, but had no effect on α S1 -CPPs-iron. CPPs are commercially available for use in milk-based formula as dietary carriers of calcium and other divalent minerals due to the presence of a unique cluster of three phosphorylated serine residues and two glutamate residues [ 60 ]. Egg yolk also contains phosphorylated protein, like phosvitin, which was used to produce phosphopeptides with a binding capacity towards calcium and improve bioavailability [ 61 ].…”
Section: Hydrolyzed Food Proteins and Peptides That Chelate Or Enhmentioning
confidence: 99%