Changes in Molecular Size and Chemical Properties of Gelatin Caused by the Reaction with Oxidizing Methyl Linoleate

Matoba, Teruyoshi; Kurita, Osamu

doi:10.1080/00021369.1984.10866574

Cited by 3 publications

(2 citation statements)

References 6 publications

(5 reference statements)

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“…4). This agrees with small differences reported in mixtures of ethyl linoleate and gelatin heated to 50 "C [40]. Products resistant to acid hydrolysis were formed only in advanced reaction stages (Tab.…”

Section: Discussionsupporting

confidence: 91%

Interactions of oxidized lipids with protein Part XVI. Interactions of oxidized ethyl linoleate with collagen

Pokorný

Davı́dek

Chocholatá

et al. 1990

Nahrung

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The reaction of ethyl linoleate with collagen proceeded at 60 degrees C following the first order kinetics but during the hydroperoxide decomposition the rate constant of the first order decomposition was substantially lower than that of the second order decomposition. Contrary to cellulose, collagen catalyzed the hydroperoxide decomposition. The amount of total oxidation products rose rapidly at the stage of rapid hydroperoxide formation, and slowly afterwards. The browning reaction was fasted in the stage of maximum hydroperoxide content, and both ether-insoluble and ether-soluble pigments were formed, the latter low in nitrogen. The amount of lipid oligomers increased mainly in the reaction stage following the hydroperoxide maximum. Soluble collagen was converted into insoluble forms by the reaction with oxidized lipids. Basic amino acids were blocked by reaction with oxidized lipids but the bonds formed became resistant to acid hydrolysis only in the stage following the hydroperoxide maximum. Changes of sensory profiles could be explained by reactions of flavour-active carbonylic oxidation products with protein.

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Section: Discussionsupporting

confidence: 91%

Interactions of oxidized lipids with protein Part XVI. Interactions of oxidized ethyl linoleate with collagen

Pokorný

Davı́dek

Chocholatá

et al. 1990

Nahrung

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“…Electrophoretic patterns of the apple samples were characterized by a band smearing, also observed in chickpea legumin, that increased with the oxidation of the proteins (Wall et al, 1996). Other changes caused by oxidized lipids on protein structure are the fragmentation of proteins (Matoba et al, 1984;Castilho et al, 1996) and the cross-linking of protein chains caused by hydroperoxides (Kawasaki and Ooizumi, 1996) or by secondary products from lipid oxidation (Chio and Tappel, 1969). The SDS-PAGE patterns of the control and legumin incubated with linoleic acid were identical (data not shown), suggesting that there is no breakage of peptidic bonds, although breakage of disulfide bridges or noncovalent bonds is possible.…”

Section: Resultsmentioning

confidence: 95%

Interaction of Chickpea (Cicer arietinum L.) Legumin with Oxidized Linoleic Acid

Sánchez‐Vioque

Vioque

Clemente

et al. 1999

J. Agric. Food Chem.

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Chickpea legumin has been purified and incubated under oxidizing conditions with linoleic acid to investigate the influence of this acid on the structure and nutritional quality of the protein. At the end of the incubation time, >30% of the linoleic acid was oxidized. The oxidized linoleic acid was highly detrimental to legumin, and the electrophoretic pattern of the protein was completely changed after the incubation period. Nevertheless, neither polymerization nor cleavage of the protein was observed as deduced from gel filtration chromatography, suggesting that the changes observed in native electrophoresis were probably due to oxidation of legumin. The incubation of legumin with linoleic acid also produced a diminution of the contents of methionine and histidine, by 81.3 and 24.3%, respectively. Finally, in vitro protein digestibility of chickpea legumin was also seriously affected by the incubation with linoleic acid, decreasing from 84.1 to 69.2%.

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Epoxides: an underestimated lipid oxidation product

Schaich

2023

Free Radical Research

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Changes in Molecular Size and Chemical Properties of Gelatin Caused by the Reaction with Oxidizing Methyl Linoleate

Cited by 3 publications

References 6 publications

Interactions of oxidized lipids with protein Part XVI. Interactions of oxidized ethyl linoleate with collagen

Interactions of oxidized lipids with protein Part XVI. Interactions of oxidized ethyl linoleate with collagen

Interaction of Chickpea (Cicer arietinum L.) Legumin with Oxidized Linoleic Acid

Epoxides: an underestimated lipid oxidation product

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