Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles.
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.
Dyal
Ansil
A
Department of Chemical Engineering, Chemistry and Material Science, Polytechnic University, 6 Metrotech Center, Brooklyn, New York 11201, USA.
Loos
Katja
K
Noto
Mayumi
M
Chang
Seung W
SW
Spagnoli
Chiara
C
Shafi
Kurikka V P M
KV
Ulman
Abraham
A
Cowman
Mary
M
Gross
Richard A
RA
D002175:Candida / Q000201:enzymology; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D005290:Ferric Compounds / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008280:Magnetics; D036103:Nanotechnology / Q000379:methods
D004800:Enzymes, Immobilized; D005290:Ferric Compounds; C000499:ferric oxide; D008049:Lipase