An enzymatic formation of 13-oxo-trideca-9,11-dienoic acid from 13-hydroperoxylinolenic acid by a homolytic hydroperoxide lyase in elicitor-treated soybean cotyledons.

An activity of homolytic hydroperoxide lyase (HPLS) catalyzing the specific cleavage of 13-hydroperoxylinolenic acid to form a volatile compound and 13-oxo acid was found in the enzyme extract from soybean cotyledons. 2-Penten-1-ol was characterized as a volatile metabolite by gas chromatography-mass spectrometry analysis. The methyl ester derivatives of reaction products were separated and isolated by a normal-phase high-performance liquid chromatography, and identified to be 13-oxo-trideca-9(Z),11(E)-dienoic acid methyl ester and its geometric isomer possessed 9(E),11(E) moiety by the analyses of high resolution mass spectrometry and nuclear magnetic resonance spectrometry. An activity of homolytic HPLS found in soybean cotyledons was evidently enhanced by elicitation. The products of 13-oxo-tridecadienoic acid with alpha, beta, gamma, delta-unsaturation were shown to be antifungal substances by a chromatographic bioassay. The metabolites via lipoxygenase and HPLS pathways may have physiological roles in the resistant action of host plants.