The enzyme laetoperoxidase might, like other hemoproteins, noneuzymatically 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-l-ol and pentan-l-ol were identified.