In this study, Lipoxygenase from potato tuber has been purified by a method involving hydrophobic chromatography and the purified enzyme immobilized by covalent coupling to oxirane acrylic beads. The immobilized lipoxygenase exhibited increased long-term stability without a significant modification of the kinetic parameters. The comparative study on the effects of inhibitors such as dithizone, NDGA, phenidone, and beta-mercaptoethanol on the free and immobilized enzyme highlighted the importance of the lipoxygenase-support interaction, concluding that the immobilization process could cause the protection of the iron atom in the enzyme. The enzymatic specificity was maintained for the immobilized lipoxygenase, and their stability increased as compared to the free enzyme, making it feasible to use the enzyme in a multistep reaction to produce large quantities of leukotriene A(4) or other related compounds of interest in the chemical industry and medicine.