Activity of Candida rugosa Lipase Immobilized on γ-Fe2O3 Magnetic Nanoparticles

Abstract
We report the stability and enzymatic activity of Candida rugosa Lipase (E.C.3.1.1.3) immobilized on γ-Fe2O3 magnetic nanoparticles. The immobilization strategies were either reacting the enzyme amine group with a nanoparticle surface acetyl, or amine groups. In the former, the enzyme was attached through a CN bond, while in the latter it was connected using glutaraldehyde. AFM images show an average particle size of 20 ± 10 nm after deconvolution. The enzymatic activity of the immobilized lipase was determined by following the ester cleavage of p-nitrophenol butyrate. The covalently immobilized enzyme was stabile and reactive over 30 days.