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

✍ Scribed by Pokorný, J. ;Davídek, J. ;Chocholatá, V. ;Pánek, J. ;Bulantová, H. ;Janitz, W. ;Valentová, H. ;Vierecklová, M.

Book ID
102841429
Publisher
John Wiley and Sons
Year
1990
Tongue
English
Weight
680 KB
Volume
34
Category
Article
ISSN
0027-769X

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✦ Synopsis

The reaction of ethyl linoleate with collagen proceeded at 60 "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 decompositon. 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 fastest 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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