Nanoscale particle-based enzyme immobilization carries a risk of
dissolving or breaking the material when applied. One effective strategy
to improve the stability and functionality of this type of nanomaterial
is compounding with polymers. In this study, Fe3O4 nanoparticles were synthesized and coated with SiO2,
after which magnetic hollow composite beads with nanoscale porous
structures, named, lipase/Fe3O4/PAN (L/FP),
were fabricated by compounding polyacrylonitrile and SiO2-coated Fe3O4 nanoparticles to immobilize Candida
antarctica lipase B (CALB) in one step. Fourier transform infrared
spectroscopy, scanning electron microscopy, the Brunauer–Emmett–Teller
method, vibrating sample magnetometer measurements, and thermogravimetry
analysis were used to analyze the structure of hollow beads. It was
found that composite beads retained nanoscale channels and had a larger
specific surface area (27.2 m2/g), a higher pore volume
(0.09 cm3/g), and better saturation magnetization values
(9.8 emu/g) than PAN hollow beads (6.2 m2/g, 0.03 cm3/g, and 0 emu/g, respectively). After optimizing fabrication
and immobilization conditions, L/FP showed a high lipase capacity
(50 mg protein/g support) at 2 mg/mL lipase, and the immobilized yield
was up to 98.4% when the mass ratio of the starting lipase and support
was 1.3 (mg lipase/g support). The immobilized lipase in L/FP showed
greater thermal stability and resistance to alkali than free CALB.
L/FP also had good stability in most organic solvents. In all tested
cycles, it also had better reusability (78.4, 47.2, and 23.8% retained
activity after 10, 20, and 30 cycles, respectively) in ester hydrolysis
than CALB-immobilized Fe3O4 nanoparticles or
PAN beads and had higher activity than the commercial immobilized
lipase (Novo 435).