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Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles
Ansil Dyal1, Katja Loos, Mayumi Noto
1Department of Chemical Engineering, Chemistry and Material Science, Polytechnic University, 6 Metrotech Center, Brooklyn, New York 11201, USA.
Abstract:
We report the stability and enzymatic activity of Candida rugosa Lipase (E.C.3.1.1.3) immobilized on gamma-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 C=N 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.
