The reaction of α<sub>s1</sub>- and β-casein with ferrous ions in the presence of oxygen

Manson, William; Cannon, J H

doi:10.1017/s0022029900016204

Cited by 23 publications

(11 citation statements)

References 12 publications

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“…The observation that casein is antioxidative is in agreement with other reports on the antioxidant activity of casein (Tannenbaum et al 1969;Manson & Cannon, 1978;Laakso, 1984;Truby et al 1987). Taylor & Richardson (19806) reported that the PI decreased when casein (pH 6-7) was heated at 130 °C for 30 min.…”

Section: Antioxidant Activity Of Caseinsupporting

confidence: 92%

Antioxidant activity of casein and Maillard reaction products from casein-sugar mixtures

Mcgookin

Augustin

1991

Journal of Dairy Research

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The antioxidant activity of casein and Maillard reaction products obtained by reaction of casein with glucose or lactose was studied. Antioxidant activity was evaluated in a model system containing methyl linoleate with haemoglobin as a pro-oxidant. Casein was antioxidative and heating casein in the presence of glucose or lactose resulted in enhancement of antioxidant activity. The development of antioxidant activity in reacted casein-sugar mixtures was determined as a function of initial casein and sugar concentration. The observed antioxidant activity of reacted casein-sugar mixtures was due to casein itself and Maillard reaction products resulting from reacting casein with sugar.

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Section: Antioxidant Activity Of Caseinsupporting

confidence: 92%

Antioxidant activity of casein and Maillard reaction products from casein-sugar mixtures

Mcgookin

Augustin

1991

Journal of Dairy Research

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“…Caseins may also act as antioxidants because they have the ability to bind prooxidant metals to their phosphoserine residues [6,11], which inhibits the catalytic effect of the metals [1]. The present study showed that iron added as ferrous sulphate was bound completely to the casein molecules in sodium caseinate at added iron concentrations up to 4 mmol·L −1 (Fig.…”

Section: Discussionmentioning

confidence: 53%

“…The formation of casein-iron complexes induces the oxidation of iron from the ferrous state to the ferric state [11]. The characteristics of different iron complexes as donors to caseins were investigated by Hegenauer et al [6].…”

Section: Introductionmentioning

confidence: 99%

Milk protein-iron complexes: Inhibition of lipid oxidation in an emulsion

Sugiarto

Taylor

et al. 2009

Dairy Sci. Technol.

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-Fortification of foods with iron is a common vehicle for delivering iron in required quantities to the consumer. However, many technological problems occur when food products are fortified with minerals, due mainly to the many reactions of minerals with other food components, e.g. fat oxidation. In the present study, the binding of iron (ferrous sulphate) to common milk protein products, sodium caseinate, whey protein isolate (WPI) and milk protein concentrate (MPC), to form protein-iron complexes was characterized by the amount of iron binding and the turbidity as functions of the iron concentration. In an emulsion containing linoleic acid, the oxidation activity of these protein-iron complexes was compared with that of the iron in its free state. The affinities of caseinate and MPC to bind iron were higher than that of WPI. These differences were attributed to the presence of clusters of phosphoserine residues in casein molecules, that are known to bind divalent cations strongly. Lipid oxidation experiments showed that the ability of iron to catalyse lipid oxidation was reduced significantly when iron was bound to protein compared with when it was in its free form. This suggests that the formation of milk protein-iron complexes could be a novel way of incorporating iron into food products with high bioavailability, good flavour and no solubility problems. sodium caseinate / whey protein isolate / milk protein concentrate / protein-iron complex / emulsion oxidationRésumé -Complexes protéines laitières-fer : inhibition de l'oxydation des lipides dans une émulsion. La fortification en fer des aliments est utilisée couramment pour apporter aux consommateurs les quantités nécessaires en fer. Cependant, beaucoup de problèmes technologiques surviennent quand les produits alimentaires sont fortifiés avec des minéraux, principalement en raison de nombreuses réactions des minéraux avec les autres composants des aliments, par exemple Article published by EDP Sciences l'oxydation de la matière grasse. Dans la présente étude, la liaison du fer (sulfate de fer) à des produits protéiques laitiers courants, caséinate de sodium, isolat de protéines de lactosérum et concentré de protéines laitières, pour former des complexes protéines-fer a été caractérisée par la quantité de fer lié et la turbidité en fonction de la concentration en fer. Dans une émulsion contenant de l'acide linoléique, l'activité oxydante de ces complexes protéines-fer a été comparée avec l'activité oxydante du fer à l'état libre. Les affinités du caséinate et du concentré de protéines laitières pour lier le fer étaient plus élevées que celle de l'isolat de protéines de lactosérum. Ces différences ont été attribuées à la présence dans les molécules de caséine d'amas de résidus phosphosérine qui sont connus pour lier fortement les cations divalents. Les essais d'oxydation des lipides ont montré que la capacité du fer à catalyser l'oxydation des lipides était significativement réduite quand le fer était lié aux protéines par rapport à celle obtenue q...

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“…Casein phosphopeptides have interesting physicochemical properties such as the formation of soluble complexes with bi-or trivalent metals (Oesterberg, 1966;Manson & Cannon, 1978), or the stabilization of Ca phosphate solutions against precipitation of tricalcium phosphate (Reeves & Latour, 1958). This latter property led to speculation that phosphopeptides might favourably influence intestinal Ca solubility (Naito el al.…”

mentioning

confidence: 99%

Tryptic phosphopeptides from whole casein. I. Preparation and analysis by fast protein liquid chromatography

Juillerat

Baechler

Berrocal

et al. 1989

Journal of Dairy Research

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SUMMARY. Tryptic phosphopeptides were obtained from whole bovine casein by chromatography on the anion exchange resin QAE-Sephadex A 25. Salt gradient clution of the column allowed separation of non-phosphorylated peptidcs from phosphorylated species. The preparations obtained contained at least seven distinct phosphopeptides of which the following casein fragments were identified: a sl (43-58):2P, a sl (59-79): 5P, a s2 (46-70): 4P, /?(1-28):4P, /?(2-28):4P, and /?(33-48): IP. Fast protein liquid chromatography (FPLC) on Mono Q HR 5/5 resin showed that the phosphopeptides were eluted in the same order as from the QAESephadex resin. However, on the analytical column HR 5/5 the fragments a sl (59-79): 5P and /?(2-28): 4P, having the same net charge under the conditions of chromatography, co-eluted, whereas they were at least partly separated on the preparative column HR 16/10. Following enzymic dephosphorylation, the peptides eluted at lower salt strength in the gradient. FPLC on Mono Q resin thus permitted dephosphorylation to be monitored and intermediates between the parent species and the fully dephosphorylated peptide to be identified.

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The reaction of α_s1- and β-casein with ferrous ions in the presence of oxygen

Cited by 23 publications

References 12 publications

Antioxidant activity of casein and Maillard reaction products from casein-sugar mixtures

Antioxidant activity of casein and Maillard reaction products from casein-sugar mixtures

Milk protein-iron complexes: Inhibition of lipid oxidation in an emulsion

Tryptic phosphopeptides from whole casein. I. Preparation and analysis by fast protein liquid chromatography

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The reaction of αs1- and β-casein with ferrous ions in the presence of oxygen

Cited by 23 publications

References 12 publications

Antioxidant activity of casein and Maillard reaction products from casein-sugar mixtures

Antioxidant activity of casein and Maillard reaction products from casein-sugar mixtures

Milk protein-iron complexes: Inhibition of lipid oxidation in an emulsion

Tryptic phosphopeptides from whole casein. I. Preparation and analysis by fast protein liquid chromatography

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The reaction of α_s1- and β-casein with ferrous ions in the presence of oxygen