| Summary: | The biocatalysis of purified soybean lipoxygenase (LOX) (EC 1.13.11.12) using linoleic acid as a substrate model was investigated in selected organic solvent media, including chloroform, dichloromethane, hexane, iso-octane, octane and toluene. The results indicated that there was a 2.6 fold increase in LOX activity in the monophasic iso-octane medium compared to that obtained in the aqueous medium. In addition, the optimum concentration of octane and iso-octane in the biphasic medium containing the organic solvent and Tris-HCl buffer solution, was determined to be 3.5 and 4%, respectively, for LOX activity which resulted in a further increase in LOX activity. The immobilized LOX showed better substrate specificity towards linoleic acid, followed by arachidonic acid. The enzymatically-catalyzed end-products were investigated, and the results indicated that different proportions of the 9- and 13-HPOD isomers were produced by LOX biocatalysis depending on the reaction medium used and the free or immobilized state of the enzyme. (Abstract shortened by UMI.)
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