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.
Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles. Publishing Authors By Initials
Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles. Journal Published:
PUBLICATION TYPE: Research Support, U.S. Gov't,
Journal: Journal of the American Chemical Society
VOLUME: 125
Page Numbers: 1684-5
Journal Abbreviation: J. Am. Chem. Soc.
ISSN: 0002-7863
DAY: 19
MONTH: Feb
YEAR: 2003
Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 7503056
Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles. Keywords Mesh Terms:
KEYWORDS: Nanotechnology
MESH TERMS: methods
Chemical & Substance for Abstract: Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles. Information
Substance Name: Lipase
Registry Number: EC 3.1.1.3
Grant and Affiliation Information for Activity of Candida rugosa lipase immobilized on gamma-Fe2O3 magnetic nanoparticles.
AFFILIATION: Department of Chemical Engineering, Chemistry and Material Science, Polytechnic University, 6 Metrotech Center, Brooklyn, New York 11201, USA.
Country: United States
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MEDLINETA: J Am Chem Soc
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