Lipase catalytic
activity is greatly influenced by immobilization
on nanoparticles. In this study, lipase from
Aspergillus
niger
was immobilized on TiO
2
nanoparticles
with different morphologies: microspheres, nanotubes, and nanosheets.
All TiO
2
samples were prepared by a hydrothermal method.
Lipase/TiO
2
nanocomposites were prepared by a physical
adsorption method through hydrophobic interactions. The prepared composites
were characterized by Fourier transform infrared spectroscopy (FTIR),
X-ray diffraction (XRD), scanning electron microscopy (SEM), and high-resolution
transmission electron microscopy (HRTEM). The catalytic activity of
free and immobilized lipases was tested using sunflower oil in the
presence of methanol to produce biodiesel at 40 °C for 90 min.
The lipase immobilized on TiO
2
microspheres showed the
highest activity compared to the lipase immobilized on TiO
2
nanotubes and nanosheets. To optimize the lipase-to-microsphere
ratio, lipase was immobilized on TiO
2
microspheres in different
microspheres/lipase, w/w, (S/L) ratios of 1:1, 1:0.75, 1:0.5, and
1:0.25. It was noticed that the hydrolytic activity follows the order
1:0.25 > 1:0.5 > 1:75 > 1:1. The immobilization yield activities
were
found to be 113, 123, 125, and 130% for the microspheres/lipase (S/L)
ratios of 1:1, 1:0.75, 1:0.5, and 1:0.25, respectively.