Abstract
Fatty acids are peroxidized by lipoxygenase and subsequently cleaved by hydroperoxide lyase (HPL), which leads to the formation of short-chain aldehydes. Two different types of HPL, which can use 13- and 9-hydroperoxy derivatives of C18 polyunsaturated fatty acids as substrates, are known. So far, nobody cloned monocotyledonous HPL. In this study, the full-length cDNA from barley seedlings coding for HPL was cloned and expressed in Escherichia coli and characterized. Barley HPL has 50.1% similarity with Arabidopsis HPL in amino acid level. The enzyme was specific 13-hydroperoxy linoleic and linolenic acids and did not use the 9-hydroperoxy isomers as substrates. The expression analysis of barley HPL gene is being carried out under various treatments.
