Effects of soybean lipoxygenase-1 on phosphatidylcholines containing furan fatty acids.

Naturally occurring tetraalkylsubstituted furan fatty acids (F-acids) were tested as potential substrates for soybean lipoxygenase-1. For this purpose, F-acid methyl ester and phosphatidylcholines containing F-acids at the sn-2 position of the glycerol residue were incubated with the enzyme. Oxidation of F-acids only occurs in the presence of linoleic acid as co-substrate. Linoleic acid is converted by lipoxygenase to the corresponding hydroperoxide that oxidizes the F-acid, probably in a radical reaction, to form an unstable dioxoene compound. This intermediate then forms, dependent on pH, unsaturated furanoid acids or isomers with cyclopentenolone structure that can be detected by gas chromatography/mass spectrometry (GC/MS). F-acids located at the sn-2 position of a synthetic phosphatidylcholine (PC), containing linoleic acid in the sn-1 position, are co-oxidized to a greater extent by incubation with soybean lipoxygenase-1 than are F-acids bound to PC with myristic acid in the sn-1 position when subjected to the enzyme in the presence of a great excess of linoleic acid. The results suggest that F-acids may play a strategic role in antioxidative processes in plant cells.