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Swedish Institute for Food Preservation Research (SIK), Fack, S-400 21 Göteborg 16, Sweden
ABSTRACT
The enzyme lactoperoxidase might, like other hemoproteins, nonenzymatically catalyze oxidation of unsaturated fatty acids and hence contribute to the development of oxidized flavor. Purified native lactoperoxidase had a catalytic activity on linoleic acid comparable to that of other native hemoproteins but this activity was drastically increased on heat-treatment of the enzyme. Both native and denaturated lactoperoxidase accelerated the development of the expected aldehydes from linoleic acid, which were identified by combined gas chromatography—mass spectrometry. In addition 2-pentyl-furan, propan-1-ol and pentan-1-ol were identified.
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