Activity of Candida rugosa lipase immobilized on γ-Fe2O3 magnetic nanoparticles

Ansil Dyal, Katja Loos, Mayumi Noto, Seung W. Chang, Chiara Spagnoli, Kurikka V.P.M. Shafi, Abraham Ulman, Mary Cowman, Richard A. Gross

Research output: Contribution to journalArticle

Abstract

We report the stability and enzymatic activity of Candida rugosa Lipase (E.C.3.1.1.3) immobilized on γ-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.

Original languageEnglish (US)
Pages (from-to)1684-1685
Number of pages2
JournalJournal of the American Chemical Society
Volume125
Issue number7
DOIs
StatePublished - Feb 15 2003

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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    Dyal, A., Loos, K., Noto, M., Chang, S. W., Spagnoli, C., Shafi, K. V. P. M., Ulman, A., Cowman, M., & Gross, R. A. (2003). Activity of Candida rugosa lipase immobilized on γ-Fe2O3 magnetic nanoparticles. Journal of the American Chemical Society, 125(7), 1684-1685. https://doi.org/10.1021/ja021223n