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Peroxygenase-catalyzed epoxidation of oleic acid in preparations of cereal seeds was investigated. The 105,OOOg particle fraction of oat (Avena safiva) seed homogenate showed high peroxygenase activity, i.e. 3034 2 288 and 2441 f 168 nmol (10 min)-' mg-' protein in two cultivars, whereas the corresponding fraction obtained from barley (Hordeum vulgare and Hordeum distichum), rye (Secale cereale), and wheat (Trificum aesfivum) showed only weak activity, i.e. dihydroxy-9(Z)-octadecenoic acid, and 12(R),13(S)-epoxy-9(S)-hy-droxy-1 O(€)-octadecenoic acid. lncubation of linoleic acid with the 105,OOOg particle fraction gave a similar, but not identical, pattern of metabolites. Conversion of linoleic acid into 9(S),12(S),13(S)-trihydroxy-1 O(€)-octadecenoic acid, a naturally occurring oxylipin with antifungal properties, took place by a pathway involving sequential catalysis by lipoxygenase, peroxygenase, and epoxide hydrolase.Formation of hydroxyoctadecadienoic acids and epoxyhydroxyoctadecenoic acids upon incubation of linoleic acid with wheat (Triticum aestivum) flour-water suspensions was described by Graveland (1970). In the same year, the presence of a "lipoperoxidase" activity in oat (Avena sntiva) seed was postulated to explain reduction of linoleic acid 9-and 13-hydroperoxides (9-HPOD and 13-HPOD) into the corresponding alcohols (9-and 13-HOD) (Heimann and Schreier, 1970). In a further study, oat seed was reported to '

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