Caseinphosphopeptides (CPP) in Feces and Contents in Digestive Tract of Rats Fed Casein and CPP Preparations

Kasai, Takanori; Iwasaki, Ryo; Tanaka, Miyuki; Kiriyama, Shuhachi

doi:10.1271/bbb.59.26

Cited by 31 publications

(24 citation statements)

References 8 publications

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“…The observation by Kasai et al (1995) of a similar content of CPP in the ileum of rats fed either casein or CPP does not take into account the kinetics of protein hydrolysis that yields digestion products throughout the upper part of the digestive tract, whereas Fe absorption can occur only in the duodenum and proximal jejunum (Beard, 1996); therefore, it appears useful that Fe reaches the upper part of the bowel yet bound to low molecular weight ligands which could favor its absorption.…”

Section: Discussionmentioning

confidence: 99%

Iron Tissue Storage and Hemoglobin Levels of Deficient Rats Repleted with Iron Bound to the Caseinophosphopeptide 1−25 of β-Casein

Aît-Oukhatar

Bouhallab

Arhan

et al. 1999

J. Agric. Food Chem.

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Caseinophosphopeptides (CPP) issued from enzyme digestion of caseins bind cations and keep them soluble in the digestive tract. They could be used as ligands to improve iron (Fe) bioavailability. Fe-deficient young rats were repleted with Fe (40 or 200 mg/kg of diet) bound either to the β-CN (1−25) of β-casein or to whole β-casein or as FeSO4. A control pair-fed group was given 200 mg of Fe (FeSO4)/kg of diet for 6 weeks. After repletion, hemoglobin concentration of the control group was reached only by the β-CN (1−25) animals fed 200 mg of Fe/kg; β-CN (1−25) bound Fe (40 and 200 mg) produced higher Fe liver and spleen stores than FeSO4. Binding Fe to the whole, nonhydrolyzed β-casein gave results intermediate between the other experimental groups. Binding Fe to phosphoserine residues of low molecular weight CPP improved its ability to cure anemia and to restore iron tissue stores, as compared to Fe bound to the whole casein and to inorganic salts. Keywords: Iron; bioavailability; tissue storage; hemoglobin; casein phosphopeptide; milk proteins; rat

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Section: Discussionmentioning

confidence: 99%

Iron Tissue Storage and Hemoglobin Levels of Deficient Rats Repleted with Iron Bound to the Caseinophosphopeptide 1−25 of β-Casein

Aît-Oukhatar

Bouhallab

Arhan

et al. 1999

J. Agric. Food Chem.

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“…The high concentration of negative charges of phosphate peptides makes them resistant to further proteolysis (Clare & Swaisgood, 2000;Reynolds, Riley, & Adamson, 1994;Meisel & Schlimme, 1990;Hirayama, Toyota, Yamaguchi, Hidaka, & Naito, 1992;Kasai, Honda, & Kiriyama, 1992;Kasai, Iwasaki, Tanaka, & Kiriyama, 1995;FitzGerald, 1998).…”

Section: Article In Pressmentioning

confidence: 99%

Caseins as source of bioactive peptides

Silva

Malcata

2005

International Dairy Journal

382

211

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Biologically active peptides are of particular interest in food science and nutrition because they have been shown to play physiological roles, including opioid-like features, as well as immunostimulating and anti-hypertensive activities, and ability to enhance calcium absorption. Hidden or inactive in the amino-acid sequence of dairy proteins, they can be released or activated in vivo during gastrointestinal digestion, or upstream during food processing via specific, enzyme-mediated proteolysis. Caseins, in either milk or dairy products (e.g. cheese), are important sources of those peptides; their biological significance, their impact on human health and the manufacture of novel functional food ingredients therefrom have been subject to intensive research, which will be briefly presented and critically discussed in this review. r

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“…L'hydrolyse des caséines par les enzymes digestives libère physiologiquement des phosphopeptides (CPP) solubles et partiellement résistants à une hydrolyse enzymatique ultérieure (Bouhallab et al, 1991 ;Brommage et al, 1991) qui sont donc retrouvés dans la lumière intestinale aux diffé-rents niveaux du tractus digestif (Naito et al, 1972 ;Brommage et al, 1991) et dans les selles (Kasai et al, 1995). L'absorption du fer pourrait bénéficier de la présence d'un ligand susceptible de le maintenir à l'état soluble jusqu'au contact de l'entérocyte, à l'intérieur duquel son devenir dépend de l'homéostasie de l'organisme (Conrad, 1993 ;Bothwell, 1995).…”

Section: Rats Carencés En Fer Gluc Feunclassified

Absorption digestive du fer lié au caséinophosphopeptide 1-25 de la β-caséine

Pérès¹,

Bouhallab²,

Bureau³

et al. 1997

Lait

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Summary -Digestive absorption of iron bound to the 1-25 caseinophosphopeptide of~-casein. We investigated the digestive absorption of iron using an isolated, perfused rat intestinalloop. Iron bound to the 1-25 caseinophosphopeptide of~-casein (~-CN (1-25» was compared to iron gluconate. Half of the animals were bled to induce an acute iron deficiency, which enhances iron absorption; the protective effect of~-CN (1-25) against the calcium inhibition of iron absorption was tested as weIl. In the control or anemie groups, iron disappearance from digestive lumen was higher in thẽ -CN (1-25) than in the gluconate group. In control animaIs the amount of iron stored was lower iñ -CN (1-25) animaIs than in animaIs perfused with gluconate, while both groups of anemie animaIs also displayed lower enterocyte retenti on than control animaIs. As a result, the net iron absorption was higher in animaIs perfused with~-CN (1-25) than with gluconate, whether the animaIs were iron depleted or not. Addition of calcium to the perfused solution decreased iron absorption, however, this decrease was significantly reduced in~-CN (1-25) groups. The increased solubility of iron bound to~-CN (1-25) could explain these results, in association with enhancement of the mucosal transfer of iron taken up by the enterocyte.Résumé -L'absorption digestive du fer lié au 1-25 caséinophosphopeptide issu de la~-caséine (~-CN [1-25]) a été comparée à celle du gluconate de fer par le modèle d'intestin perfusé isolé, vascularisé de rat, à l'état basal et dans deux conditions connues pour augmenter l'absorption du fer (saignée) ou l'inhiber (présence de calcium). Chez l'animal normal ou après saignée, la disparition du fer de la lumière intestinale du groupe~-CN (1-25) est supérieure à celle du groupe gluconate. Chez l'animal normal, la rétention entérocytaire du fer est plus faible dans le groupe~-CN (1-25) que * Correspondence and reprints 434 lM Peres et al dans le groupe gluconate. Après saignée, elle est semblable dans les deux groupes et est significativement inférieure à celle des animaux normaux. En conséquence, chez les animaux normaux ou anémiques, l'absorption nette est plus élevée dans les groupes~-CN (1-25) que dans les groupes perfusés avec du gluconate. La fixation du fer au~-CN (1-25) limite significativement l'effet inhibiteur du calcium sur son absorption, chez l'animal contrôle et anémique. Ces résultats semblent dus à la protection intraluminale apportée au fer par sa liaison au~-CN (1-25) soluble, associée à une modification du transport entérocytaire du fer capté.fer / absorption digestive / caséinophosphopeptide~-CN

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Caseinphosphopeptides (CPP) in Feces and Contents in Digestive Tract of Rats Fed Casein and CPP Preparations

Cited by 31 publications

References 8 publications

Iron Tissue Storage and Hemoglobin Levels of Deficient Rats Repleted with Iron Bound to the Caseinophosphopeptide 1−25 of β-Casein

Iron Tissue Storage and Hemoglobin Levels of Deficient Rats Repleted with Iron Bound to the Caseinophosphopeptide 1−25 of β-Casein

Caseins as source of bioactive peptides

Absorption digestive du fer lié au caséinophosphopeptide 1-25 de la β-caséine

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