The purpose of the present work is improving stability properties of porcine pancreatic lipase (triacylglycerol lipase, E.C.3.1.1.3) by immobilization on chitosan/TiO2 composite beads. The immobilization parameters were initial enzyme concentration (0.5-2 mg/ml), adsorption time (5-25 min), and glutaraldehyde concentration (1-4 % v/v). The optimum temperature (20-60 A degrees C), optimum pH (3.0-10.0), kinetic parameters, thermal stability (4-70 A degrees C), pH stability (4.0-9.0), and reusability (9 times) were investigated for characterization of immobilized lipase system. The optimum temperatures of free and immobilized lipase were 30 A degrees C. The temperature profile of the immobilized lipase was spread over a large area. The optimum pH values for the free lipase and immobilized lipase were found to be 6.5 and 7.5, respectively. The thermal stability of immobilized lipase was evaluated, and it maintained 45 % activity at 70 A degrees C. But, at this temperature, soluble lipase protected only 15 % activity. Also, the structural characterization of chitosan/TiO2 composite beads was analyzed with scanning electron microscope (SEM), X-ray diffraction (XRD), thermal gravimetric analysis (TGA), and attenuated total reflection Fourier transform infrared spectroscopy analysis (ATR-FTIR). The significance of this study is improving of stability properties of lipase for the industrial usage especially production of biodiesel and dairy products.