Inhibition of lipid peroxidation by casein. Evidence of molecular encapsulation of 1,4-pentadiene fatty acids.
The capability of cyclodextrins to form molecular inclusion complexes with linoleate appeared in a lipoxygenase-linoleate model reaction as inhibition of oxygenation. The inhibited rates were established instantaneously upon addition of the complexant and maintained until linoleate was exhausted. Total cessation of the reaction was not obtained with cyclodextrins. All these features were reproduced also in casein-inhibited reaction mixtures. Both casein and cyclodextrins protected linoleate also against autoxidation although they did not change free radical generation by xanthine oxidase or Fe2+ reactions. Since neither of the inhibitors affected the enzyme directly, casein may also act by forming linoleate complexes which via a standing equilibrium reduce the oxidizable monomer fatty acids and cause substrate-limited reaction rates. Comparisons at acidic and alkaline pH, in the presence of increasing amounts of the complexants, detergent and hydroperoxides supported this view.
D002364:Caseins / Q000494:pharmacology*; D003505:Cyclodextrins / Q000494:pharmacology; D005296:Ferrous Compounds / Q000494:pharmacology; D005609:Free Radicals; D019787:Linoleic Acid; D008041:Linoleic Acids / Q000378:metabolism; D008054:Lipid Peroxides / Q000378:metabolism*; D008084:Lipoxygenase / Q000378:metabolism; D008956:Models, Chemical; D014969:Xanthine Oxidase / Q000378:metabolism
D002364:Caseins; D003505:Cyclodextrins; D005296:Ferrous Compounds; D005609:Free Radicals; D008041:Linoleic Acids; D008054:Lipid Peroxides; D019787:Linoleic Acid; D008084:Lipoxygenase; D014969:Xanthine Oxidase