Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of β-casein

Pérès, Jean Michel; Bouhallab, Saı̈d; Petit, Christelle; Bureau, F.; Maubois, J.L.; Arhan, Pierre; Bouglé, Dominique

doi:10.1051/rnd:19980410

Cited by 44 publications

(12 citation statements)

References 27 publications

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“…The effect was attributed to the presence of calcium and partly also casein, which behaved as inhibitors, and the absence of iron enhancers in the product (Toxqui et al, 2013). Zinc in excess has also been reported to reduce iron absorption, and vice versa, an interaction that may be particularly relevant in pregnancy and infancy (Iyengar, Pullakhandam, & Nair, 2010;Pérès et al, 1998).…”

Section: Inhibitorsmentioning

confidence: 99%

Iron bioavailability from food fortification to precision nutrition. A review

Blanco-Rojo

Vaquero

2019

Innovative Food Science & Emerging Technologies

125

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Iron deficiency anaemia is a Worldwide Public Health problem and the fortification of food with iron is the most cost-effective prevention strategy. The correct combination of iron form and food vehicle is crucial, as well as the dietary context of consumption.Combinations of iron with an enhancer of its bioavailability and avoidance of interaction with iron inhibitors are recommended. New iron fortificants, innovative complexes, coatings and nanoparticulates, and biofortification are the main research lines. Ultimately, human assays are necessary before industrial production. In this regard, precision nutrition helps to identify the vulnerable groups that, according to genotype, dietary habits, physical activity and, most recently, metagenomic profile, may benefit from a specific iron-fortified food. This review addresses the modifiers of iron bioavailability and the main aspects to take into account in the development of iron-fortified food to prevent iron deficiency.

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Section: Inhibitorsmentioning

confidence: 99%

Iron bioavailability from food fortification to precision nutrition. A review

Blanco-Rojo

Vaquero

2019

Innovative Food Science & Emerging Technologies

125

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“…Among bovine caseins, the second most abundant is ␤-CN, which contains the unique cluster sequence SpSpSpEE near C-terminal extreme (residues 17-21) and the fragment ␤-CN(1-25)4P. Several in vitro assays with tumour cells HT-29 (Ferraretto et al, 2001;Ferraretto et al, 2003) and in vivo studies in rats (Aït-Oukhatar et al, 1997;Aït-Oukhatar et al, 2002;Bouhallab et al, 2002;Pérès et al, 1998Pérès et al, , 1999 have demonstrated that this fragment enhances calcium, iron and zinc absorption.…”

Section: Introductionmentioning

confidence: 99%

Identification of Casein Phosphopeptides in β-casein and Commercial Hydrolysed Casein by Mass Spectrometry

Miquel

Gómez

Alegrı́a

et al. 2006

Food sci. technol. int.

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Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in ␤-CN (␤-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH ϭ 2, 37 ºC 2 h) and intestinal stage (pancreatic-bile extract, pH ϭ 5.2, 37 ºC 2 h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation tandem mass spectrometry (RP-HPLC-ESI-MS/MS). In ␤-CN digest five peptides that contained four to five phosphate groups and the cluster sequence SpSpSpEE (residues 17-21) were identified. All CPPs with one exception ␤-CN(1-24)4P, had the protein fragment ␤-CN(1-25)4P, which is one of the main CPPs produced in vivo digestion of casein and the results of in vitro studies showed that this fragment enhanced calcium, iron and zinc absorption. In commercial hydrolysed casein CE90CPP 13 peptides were identified, only one of them, ␣ s2 -CN (1-13)3P, contained the cluster sequence SpSpSpEE but all the peptides have one or two phosphoserine residues with mineral binding capacity. These CPPs were shorter (527-2061 Da vs 2966-6512 Da) and less phosphorylated (1-3 P vs 4-5 P) than those released after simulated gastrointestinal digestion of ␤-CN. In both samples, the potential mineral chelating properties of these peptides in relation to their amino acid sequences and the presence of the phosphorylated cluster are discussed.

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“…Fe complexed CPP prevents the formation of poorly absorbed high molecular weight ferric hydroxides. Zinc absorption can also be enhanced by the formation of Zn complexed to CCP, in particular to -CN (f1-25)4P [51]. Some portion of the mineral complexed CPP formed in the small intestine was resistant to the digestive and enteric bacteria enzymes and found in the feces of rats fed a casein-based diet [52].…”

Section: Bioactive Peptides Released In Vitro By the Hydrolysis Of MImentioning

confidence: 99%

Bioactive Casein Phosphopeptides in Dairy Products as Nutraceuticals for Functional Foods

Pinto¹,

Caira²,

Cuollo³

et al. 2012

Milk Protein

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Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of β-casein

Abstract: -Binding zinc (Zn)

Cited by 44 publications

References 27 publications

Iron bioavailability from food fortification to precision nutrition. A review

Iron bioavailability from food fortification to precision nutrition. A review

Identification of Casein Phosphopeptides in β-casein and Commercial Hydrolysed Casein by Mass Spectrometry

Bioactive Casein Phosphopeptides in Dairy Products as Nutraceuticals for Functional Foods

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