In this study, lipase from Pseudomonas fluorescens was immobilized on octyl-nanoparticles by hydrophobic interaction, producing the biocatalyst OCTYL-NANO-PSF. In order to stabilize the immobilized enzyme on OCTYL-NANO, an additional step was conducted, which is the reticulation with different concentrations of glutaraldehyde (GA), producing OCTYL-NANO-PSF-GA preparations. The concentrations of glutaraldehyde were 0.5, 1, 2.5 and 5 % v/v in sodium phosphate buffer, pH 7, 200 mM. The results show that the PSF could be immobilized on octyl-nanoparticles, events at short contact time between enzyme and support (Yield of immobilization about 75 %). The reticulation step was also shown successful, since the biocatalysts remain active (Activity retention above 55 %) and it was much more stable than OCTYL-NANO-PSF preparation. Best results of activity and stability was achieved when 5% was used (OCTYL-NANO-PSF-GA 5 %) for the reticulation. This biocatalyst was 65 fold more stable than adsorbed preparation (OCTYL-NANO-PSF).