Lipoxygenase from soybean has been immobilized in polyacrylamide gel derivatized with glutaraldehyde as a means to facilitate obtaining hydroperoxy derivatives of linoleic acid. We have found that 10% acrylamide, 6% glutaraldehyde, and pH 8.0 are the best conditions for the coupling of enzyme to gel. Although catalytic efficiency is lowered by the coupling process, the stability of the system is maintained at a high level, and lipoxygenase products are not altered by the immobilization process. The use of the system in a reactor revealed that no effect of self-inactivation is produced by long-term reaction, thereby making feasible the use of a lipoxygenase bioreactor for the synthesis of lipoxygenase products.