ANTIOXIDANT EFFECT OF PROTEIN HYDROLYZATES IN FREEZE‐DRIED MODEL SYSTEMS Synergistic Action with a Series of Phenolic Antioxidants

Bishov, S. J.; Henick, A. S.

doi:10.1111/j.1365-2621.1975.tb02198.x

Cited by 56 publications

(21 citation statements)

References 5 publications

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“…The other peptide contained tyrosine residue, which is a potent hydrogen donor. Previously, many proteins have been reported to have strong antioxidative activity against the peroxidation of lipid or fatty acids systems (27,28). Three antioxidative peptides previously isolated from egg white albumin contained histidine residues at the second residue in their sequences (29), and all of the six antioxidative peptides isolated from β-conglycinin contained a proline residue in their sequences.…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin‐free egg yolk

Park

Jung

Nam

et al. 2001

J Americ Oil Chem Soc

316

183

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The protein extracted from lecithin-free egg yolk, normally discarded by lecithin processing plants, was hydrolyzed with the aid of Alcalase, a commercial enzyme. The hydrolysate was separated through a series of ultrafiltration membranes with molecular weight cutoffs of 10, 5, and 1 kDa; and three types of permeates including 10 K (permeate from 10 kDa), 5 K (permeate from 5 kDa), and 1 K (permeate from 1 kDa) were obtained. The antioxidative efficacy of hydrolysates so obtained was investigated and compared with α-tocopherol. Furthermore, two different peptides showing strong antioxidative activity were isolated from the hydrolysates by using consecutive chromatographic methods including ion exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-25 column, and high-performance liquid chromatography on an octadecylsilane column. The purity of the peptides was identified using capillary electrophoresis. The isolated peptides were composed of 10 and 15 amino acid residues, and both contained a leucine residue at their Nterminal positions.Paper no. J9748 in JAOCS 78, 651-656 (June 2001).

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin‐free egg yolk

Park

Jung

Nam

et al. 2001

J Americ Oil Chem Soc

316

183

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“…The protein hydrolysates were synergistic with BHA, BHT, and tocopherols in the system. Bishov and Henick (1975).…”

Section: Protein Hydrolysates and Amino Acidsmentioning

confidence: 95%

“…Rosemary and sage were the most effective in this study of the commonly used spices. Bishov and Henick (1976) compared unpublished studies on antioxidant activity of spices with those of Chipault (1952) and Cort (1974) in their review on natural antioxidants. Hirahara and Takai (1974) compared several spices at 0.0003% with BHA at 0.02% in soybean, linseed, olive, and Watanabe and Ayano (1974) were comparing the effectiveness in lard of ground spices with the water soluble and ethanol soluble extracts.…”

Section: Spices and Herbsmentioning

confidence: 98%

Natural Antioxidants

Dugan¹

1980

Autoxidation in Food and Biological Systems

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“…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: 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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ANTIOXIDANT EFFECT OF PROTEIN HYDROLYZATES IN FREEZE‐DRIED MODEL SYSTEMS Synergistic Action with a Series of Phenolic Antioxidants

Cited by 56 publications

References 5 publications

Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin‐free egg yolk

Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin‐free egg yolk

Natural Antioxidants

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

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