title: Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles.
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.
authors.affiliation: Department of Chemical Engineering, Chemistry and Material Science, Polytechnic University, 6 Metrotech Center, Brooklyn, New York 11201, USA.
authors.forename: Ansil
authors.initials: A
authors.lastname: Dyal
authors.forename: Katja
authors.initials: K
authors.lastname: Loos
authors.forename: Mayumi
authors.initials: M
authors.lastname: Noto
authors.forename: Seung W
authors.initials: SW
authors.lastname: Chang
authors.forename: Chiara
authors.initials: C
authors.lastname: Spagnoli
authors.forename: Kurikka V P M
authors.initials: KV
authors.lastname: Shafi
authors.forename: Abraham
authors.initials: A
authors.lastname: Ulman
authors.forename: Mary
authors.initials: M
authors.lastname: Cowman
authors.forename: Richard A
authors.initials: RA
authors.lastname: Gross
mesh_terms: 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
chemical_list: D004800:Enzymes, Immobilized; D005290:Ferric Compounds; C000499:ferric oxide; D008049:Lipase