| Literature DB >> 12580578 |
Ansil Dyal1, Katja Loos, Mayumi Noto, Seung W Chang, Chiara Spagnoli, Kurikka V P M Shafi, Abraham Ulman, Mary Cowman, Richard A Gross.
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.Entities:
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Year: 2003 PMID： 12580578 DOI： 10.1021/ja021223n
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419