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

被引：510

作者：

Dyal, A ^{[1
]}

Loos, K ^{[1
]}

Noto, M ^{[1
]}

Chang, SW ^{[1
]}

Spagnoli, C ^{[1
]}

Shafi, KVPM ^{[1
]}

Ulman, A ^{[1
]}

Cowman, M ^{[1
]}

Gross, RA ^{[1
]}

机构：

[1] Polytech Univ, Dept Chem Engn Chem & Mat Sci, Metrotech Ctr 6, Brooklyn, NY 11201 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2003年 / 125卷 / 07期

关键词：

D O I：

10.1021/ja021223n

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Copyright © 2003 American Chemical Society.

引用

页码：1684 / 1685

页数：2

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