Iron Binding by Wheat Gluten, Soy Isolate, Zein, Albumen and Casein

Nelson, Kathleen J.; Potter, Norman N.

doi:10.1111/j.1365-2621.1979.tb10017.x

Cited by 22 publications

(6 citation statements)

References 6 publications

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“…Many proteins have been shown to have antioxidant activity against the preoxidation of lipids or fatty acids, and the mechanisms have been suggested to be an increase in the surface area of linoleic acid due to the adsorption by protein molecules which might cause the catalytic effect (Nelson & Potter, 1979). The antioxidant activities of both amino acids and peptides have been investigated to gain insight into the antioxidant mechanism of protein hydrolysates.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

confidence: 99%

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

Suetsuna

Chen²

2002

FSTR

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“…The iron-binding capacities of major dietary fiber components (Camire and Clydesdale, 1981), and of pinto bean suspensions (Kojima et al, 1981) have also illustrated the importance of pH in determining the chemical form of iron. However, in addition to pH, the percent iron binding by soy protein has also been influenced by the iron source added, and the temperature and time of incubation (Nelson and Potter, 1979; Four hundred ml of double distilled deionized water at 37°C were blended with 30g of soy protein isolate in a 500 ml erlenmeyer flask to produce a slurry. A Teflon-coated stirring bar was added to evaluate elemental iron and the temperature of the sample slurry was maintained at 37 f l°C for the entire time of each experiment.…”

Section: Introductionmentioning

confidence: 99%

“…The iron-binding capacities of major dietary fiber components (Camire and Clydesdale, 1981), and of pinto bean suspensions (Kojima et al, 1981) have also illustrated the importance of pH in determining the chemical form of iron. However, in addition to pH, the percent iron binding by soy protein has also been influenced by the iron source added, and the temperature and time of incubation (Nelson and Potter, 1979;. It was the intent of this research to correlate the chemical changes of iron in the soy protein isolate with the bioavailabilities observed in man.…”

Section: Introductionmentioning

confidence: 99%

Effect of Iron Sources and Ascorbic Acid on the Chemical Profile of Iron in a Soy Protein Isolate

Rizk

Clydesdale

1983

Journal of Food Science

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The chemical changes in the iron profile of a commercial soy protein isolate resulting from ascorbic acid and iron fortification were examined. An in vitro method was devised to simulate gastrointestinal pH and an "enhancing factor" developed as a potential in vitro indicator of iron bioavailability. Ascorbic acid supplementation of soy protein produced substantial increases in soluble iron at pH 4 and 6. The solubilizing effect of ascorbic acid on iron was concentration and pH-dependent and contingent upon the exogenous iron source present. The exogenous iron entered a different chemical pool than the endogenous iron, thus raising questions about the concept of a nonheme pool at high levels of exogenous iron.

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“…or binding of the hexaammine staining reagent to protein but not the binding of iron to phytate since phytate is not present. Several papers (Champagne et al, 1985;Nelson and Potter, 1979) have reported that proteins can bind to iron when placed in iron solution. This suggests that the technique involving precipitation of ferric phytate in protein, with ferric chloride solution, on polyacrylamide gels might not represent phytate-iron interaction only but could also be the result of nonspecific protein-iron interaction.…”

Section: Resultsmentioning

confidence: 99%

Identification of phytate in proteins using polyacrylamide disc gel electrophoresis

DiLollo¹,

Alli²,

Kermasha³

1991

J. Agric. Food Chem.

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Iron Binding by Wheat Gluten, Soy Isolate, Zein, Albumen and Casein

Cited by 22 publications

References 6 publications

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

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

Effect of Iron Sources and Ascorbic Acid on the Chemical Profile of Iron in a Soy Protein Isolate

Identification of phytate in proteins using polyacrylamide disc gel electrophoresis

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