Lipoxygenase-produced oxidized fatty acids may serve as intermediates in chemical and pharmaceutical syntheses. For practical applications the enzyme should be immobilized to prevent its loss at product retrieval and to enable a continuous process. In this study the immobilization of soybean lipoxygenase on various neutral and charged supports was investigated. The best results were obtained using cellulose-based anion exchangers. The activity of the immobilized lipoxygenase was lower than the activity of the free enzyme, which was possibly caused by diffusion limitation of the fatty acids to or from the support beads.