Nuclear chemistry

Catalysis

Candida antarctica

Engineering

Glutaraldehyde

Nanoparticle

Biology

Materials science

Chromatography

Chitosan

Biochemistry

Chemical engineering

Nanotechnology

Organic chemistry

Biocatalysis

Microbiology

Enzyme

Composite material

Chemistry

Scanning electron microscope

Ionic liquid

Covalent bond

Fourier transform infrared spectroscopy

Lipase

Magnetic nanoparticles

Immobilized enzyme

International Journal of Molecular Sciences

In this communication, lipase A from Candida antarctica (CALA) was immobilized by covalent bonding on magnetic nanoparticles coated with chitosan and activated with glutaraldehyde, labelled CALA-MNP, (immobilization parameters: 84.1% ± 1.0 for immobilization yield and 208.0 ± 3.0 U/g ± 1.1 for derivative activity). CALA-MNP biocatalyst was characterized by X-ray Powder Diffraction (XRPD), Fourier Transform Infrared (FTIR) spectroscopy, Thermogravimetry (TG) and Scanning Electron Microscope (SEM), proving the incorporation of magnetite and the immobilization of CALA in the chitosan matrix. Besides, the immobilized biocatalyst showed a half-life 8-11 times higher than that of the soluble enzyme at pH 5-9. CALA showed the highest activity at pH 7, while CALA-MNP presented the highest activity at pH 10. The immobilized enzyme was more active than the free enzyme at all studied pH values, except pH 7.

Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles