Caseins and Casein Hydrolysates. 2. Antioxidative Properties and Relevance to Lipoxygenase Inhibition

Rival, Sandrine; Boeriu, Carmen G.; Wichers, Harry J.

doi:10.1021/jf0003911

Cited by 305 publications

(208 citation statements)

References 44 publications

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“…Several studies reported antioxidant effects of both casein and whey hydrolysates produced by different enzymes (80,81) . Many tripeptides (other than LTP, for example, Xaa -Xaa-Trp/Tyr, Tyr-His-Tyr) that show high scavenging activity and strong synergistic effects with phenolic antioxidants have been identified in milk (82) .…”

Section: Putative Mechanisms Underlying the Impact Of Milk Peptides Omentioning

confidence: 99%

The impact of milk proteins and peptides on blood pressure and vascular function: a review of evidence from human intervention studies

2013

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CVD are the leading cause of death worldwide. Hypertension, a major controllable risk factor of CVD, is intimately associated with vascular dysfunction, a defect which is also now recognised to be a major, modifiable risk factor for the development of CVD. The purpose of the present review was to critically evaluate the evidence for the effects of milk proteins and their associated peptides on blood pressure (BP) and vascular dysfunction. After a detailed literature search, the number of human trials evaluating the antihypertensive effects of caseinderived peptides (excluding isoleucine-proline-proline and valine-proline-proline) was found to be limited; the studies were preliminary with substantial methodological limitations. Likewise, the data from human trials that examined the effects of whey protein and peptides were also scarce and inconsistent. To date, only one study has conducted a comparative investigation on the relative effects of the two main intact milk proteins on BP and vascular function. While both milk proteins were shown to reduce BP, only whey protein improved measures of arterial stiffness. In contrast, a growing number of human trials have produced evidence to support beneficial effects of both milk proteins and peptides on vascular health. However, comparison of the relative outcomes from these trials is difficult owing to variation in the forms of assessment and measures of vascular function. In conclusion, there is an accumulating body of evidence to support positive effects of milk proteins in improving and/or maintaining cardiovascular health. However, the variable quality of the studies that produced this evidence, and the lack of robust, randomised controlled intervention trials, undermines the formulation of firm conclusions on the potential benefits of milk proteins and peptides on vascular health.

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Section: Putative Mechanisms Underlying the Impact Of Milk Peptides Omentioning

confidence: 99%

The impact of milk proteins and peptides on blood pressure and vascular function: a review of evidence from human intervention studies

2013

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“…Much physiological damage may be directly imputable to the hydroxyl radical, because it is highly reactive, and so many hydroxyl radicals produced in vivo react at or close to their site of formation. The biochemical literature is full of claims that reactive species are involved in different diseases (Southorn & Powis, 1988).Many proteins have been reported to have antioxidant activities against the peroxidation of lipids or fatty acids upon hydrolysis (Rival et al, 2001, Suetsuna, 2000Chen et al, 1998;Hattori et al, 1998;Bishov & Henick, 1972). Gluten has a unique amino acid composition, with Glu/Gln and Pro accounting for more than 50% of the amino acid residues.…”

mentioning

confidence: 99%

Isolation and Characterization of Peptides with Antioxidant Activity Derived from Wheat Gluten.

Suetsuna

Chen²

2002

FSTR

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Peptides having potent antioxidant activity were separated from the hydrolysate of wheat gluten by ion-exchange and gel filtration chromatography. Peptides obtained by SP Sephadex C-25 chromatography of the most active fraction (WP-3) were further separated using reversed-phase high performance liquid chromatography. The amino acid sequences of these peptides were Leu-Gln-Pro-Gly-Gln-Gly-Gln-Gln-Gly and Ala-Gln-Ile-Pro-Gln-Gln.Keywords: wheat gluten, hydrolysate, peptide, antioxidant activityThe disease-preventing potential of naturally occurring substances in the diet is a main area of scientific interest. Antioxidants have attracted great attention for disease preventive effects because of lipid peroxidation which can lead to destabilization and disintegration of cell membranes, to many age-related diseases, to aging, and to cancer (Mcbrien & Slater, 1982). Recently, the involvement of free radicals and other oxidants in aging and in several diseases has been investigated in detail. Much physiological damage may be directly imputable to the hydroxyl radical, because it is highly reactive, and so many hydroxyl radicals produced in vivo react at or close to their site of formation. The biochemical literature is full of claims that reactive species are involved in different diseases (Southorn & Powis, 1988).Many proteins have been reported to have antioxidant activities against the peroxidation of lipids or fatty acids upon hydrolysis (Rival et al., 2001, Suetsuna, 2000Chen et al., 1998;Hattori et al., 1998;Bishov & Henick, 1972). Gluten has a unique amino acid composition, with Glu/Gln and Pro accounting for more than 50% of the amino acid residues. About 30% of gluten's amino acid residues are hydrophobic, and the residues contribute greatly to its ability to form protein aggregates by hydrophobic interactions and to bind nonpolar substances (Fennema, 1996). Since wheat gluten had strong affinity for oil and other nonpolar substances, we speculated that gluten's hydrolysate would have some protective effect on the degradation of fatty acid. In this study, we examined the antioxidant effects of peptic hydrolysate of wheat gluten, and the amino acid sequences of antioxidant peptides were determined. Materials and methodsMaterials Wheat gluten was purchased from Oriental Yeast (Tokyo). Pepsin (from porcine gastric mucosa, EC 3.4.23.1) was obtained from Merck (Darmstadt, Germany).Linoleic acid (~99%) and d-␣-tocopherol from Sigma Chemical (St. Louis, MO) were used as received. All other reagents were of analytical grade from Nacalai Tesque (Kyoto).Purification of peptides from wheat gluten Ten grams of wheat gluten was put in 100 ml of deionized water overnight and homogenized in 1 l of deionized water. The pH value of the homogenate was adjusted to 2.0 with 2 N HCl, and 0.3 g of pepsin was added. After 20 h of digestion at 37ºC, the hydrolysate was filtered to remove the residue and centrifuged at 20,000¥g for 20 min at 4ºC. The supernatant was applied to a Dowex 50W column (4.5¥20 cm, 50-100 mesh, H + form). The ...

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“…This could result from the binding of iron to the phosphopeptide, limiting both initiation of the reaction and breakage of the hydroperoxides. Free radical scavenging by the peptides, or reactions of peroxidizing lipids with amino groups of the protein hydrolysate, causing losses in reacting amino acids, cannot be excluded [23,52]. Loss of methionine during storage of casein and of lysyl, tryptophanyl and histidyl residues of whey proteins were observed previously in the presence of oxidizing methyl linoleate [7,45,55].…”

Section: Discussionmentioning

confidence: 94%

“…The antioxidant activity of milk proteins such as lactoferrin, transferrin and caseins has been demonstrated in various systems [2,25,46,49,54,56]. Casein hydrolysates and caseinderived peptides have been shown to inhibit enzymatic and non-enzymatic lipid peroxidation [52]; caseinophosphopeptides were demonstrated to exhibit antioxidant properties in oil-in-water emulsions [14]. Iron chelation, scavenging of free radicals, and reactions of some side-chains of amino acids with hydroperoxides or secondary oxidation products, such as malonaldehyde and other aldehydes, are the main mechanisms involved in the antioxidant activity of amino acids, peptides and proteins [12,23,24,26,33,34,44,45].…”

Section: Introductionmentioning

confidence: 99%

?-Caseinophosphopeptide (f1-25) confers on ?-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes

Kansci

Génot²,

Meynier³

et al. 2004

Lait

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-Protein ingredients such as hydrolysates of milk proteins may improve the nutritive value of functional foods. For instance, β-casein tryptic hydrolysate could simultaneously increase iron absorption and prevent lipid oxidation in foods containing high contents of polyunsaturated fatty acids (PUFA). The aim of this study was to determine the antioxidant activity of β-casein tryptic hydrolysate and of its β-caseinophosphopeptide (f1-25) on Fe(III)/ascorbate-induced oxidation of muscle phospholipids in a liposome system. Oxygen consumption, conjugated dienes (CD), thiobarbituric acid reactive substances (TBARS) and volatile compounds were measured during oxidation at 25 °C of the liposomes in the presence of either the β-casein tryptic hydrolysate (0.24-2.4 mg·mL -1 ) or of its phosphopeptide (0.1-0.31 mg·mL -1 ). Oxygen consumption was significantly enhanced in the presence of β-casein tryptic hydrolysate or of the phosphopeptide (f1-25) and staircase curves were observed for the highest concentrations, showing complex oxidative interactions between iron, β-casein tryptic hydrolysate or phosphopeptide and the phospholipids. In contrast, on an hourly scale, formation of CD, TBARS and total volatile compounds were inhibited. The inhibition of CD and TBARS reached 50% after 20 h of oxidation in the presence of 1.2 mg·mL -1 β-casein tryptic hydrolysate or 0.16 mg·mL -1 phosphopeptide (f1-25). Amounts of total volatile compounds produced after 24 h decreased by about 60% in the presence of the hydrolysate (1.2 mg·mL -1 ) and 50% with the phosphopeptide (f1-25) (0.31 mg·mL -1 ) due to drastic decrease or even disappearance of alkanals and 2-alkenals. Several alcohols such as pentanol and hexanol were produced in higher amounts. Thus β-casein tryptic hydrolysate can protect rich-in-PUFA phospholipid liposomes against long-term iron-induced oxidation, mainly due to iron chelation by β-caseinophosphopeptide (f1-25). This antioxidant activity could benefit specific food products.

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Caseins and Casein Hydrolysates. 2. Antioxidative Properties and Relevance to Lipoxygenase Inhibition

Cited by 305 publications

References 44 publications

The impact of milk proteins and peptides on blood pressure and vascular function: a review of evidence from human intervention studies

The impact of milk proteins and peptides on blood pressure and vascular function: a review of evidence from human intervention studies

Isolation and Characterization of Peptides with Antioxidant Activity Derived from Wheat Gluten.

?-Caseinophosphopeptide (f1-25) confers on ?-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes

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