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

doi:10.1021/ja021223n

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 journal › Article › peer-review

565 Scopus citations

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 language	English
Pages (from-to)	1684-1685
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	125
Issue number	7
DOIs	https://doi.org/10.1021/ja021223n
State	Published - 19 Feb 2003
Externally published	Yes

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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.",

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T1 - Activity of Candida rugosa lipase immobilized on γ-Fe2O3 magnetic nanoparticles

AU - Dyal, Ansil

AU - Loos, Katja

AU - Noto, Mayumi

AU - Chang, Seung W.

AU - Spagnoli, Chiara

AU - Shafi, Kurikka V.P.M.

AU - Ulman, Abraham

AU - Cowman, Mary

AU - Gross, Richard A.

PY - 2003/2/19

Y1 - 2003/2/19

N2 - 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.

AB - 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.

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

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