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 journalArticlepeer-review


We report the stability and enzymatic activity of Candida rugosa Lipase (E.C. 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
Issue number7
StatePublished - Feb 15 2003

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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