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Activity of Candida rugosa Lipase Immobilized on γ-Fe2O3 Magnetic Nanoparticles

Dyal, Ansil, Loos, Katja, Noto, Mayumi, Chang, Seung W., Spagnoli, Chiara, Shafi, Kurikka V. P. M., Ulman, Abraham, Cowman, Mary, Gross, Richard A.·2003·Journal of the American Chemical Society

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.

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Metadata

Authors
Dyal, A., Loos, K., Noto, M., Chang, S. W., Spagnoli, C., Shafi, K. V. P. M., Ulman, A., Cowman, M., & Gross, R. A.
Venue
Journal of the American Chemical Society
Published
2003-01-28
Volume
125
Issue
7
Pages
1684-1685
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W2254901956
Cited by
554
References
0
FWCI
8.79
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Activity of Candida rugosa Lipase Immobilized on γ-Fe2O3 Magnetic Nanoparticles. https://app.cochat.ai/papers/10.1021/ja021223n
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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. https://doi.org/10.1021/ja021223n

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.