Magnetic nanoparticles supported ionic liquids for lipase immobilization: Enzyme activity in catalyzing esterification

被引：231

作者：

Jiang, Yangyang ^{[1
]}

Guo, Chen ^{[1
]}

Xia, Hansong ^{[1
]}

Mahmood, Iram ^{[1
]}

Liu, Chunzhao ^{[1
]}

Liu, Huizhou ^{[1
]}

机构：

[1] Chinese Acad Sci, Inst Proc Engn, Lab Separat Sci & Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2009年 / 58卷 / 1-4期

基金：

中国国家自然科学基金; 国家高技术研究发展计划(863计划);

关键词：

Esterification; Ionic liquids; Lipase immobilization; Magnetic nanoparticle; CANDIDA-RUGOSA; BIOCATALYST; HYDROLYSIS; ADSORPTION; CATALYSIS;

D O I：

10.1016/j.molcatb.2008.12.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Candida rugosa lipase was immobilized on magnetic nanoparticles supported ionic liquids having different cation chain length (C-1, C-4 and C-8) and anions (Cl-, BF4- and PF6-). Magnetic nanoparticles Supported ionic liquids were obtained by covalent bonding of ionic liquids-silane on magnetic silica nanoparticles. The particles are superparamagnetic with diameter of about 55 nm. Large amount of lipase (63.89 mg/(100 mg carrier)) was loaded on the support through ionic adsorption. Activity of the immobilized lipase was examined by the catalysis of esterification between oleic acid and butanol. The activity of bound lipase was 118.3% compared to that of the native lipase. Immobilized lipase maintained 60% of its initial activity even when the temperature was LIP to 80 degrees C. In addition, immobilized lipase retained 60% of its initial activity after 8 repeated batches reaction, while no activity was detected after 6 cycles for the free enzyme. (C) 2008 Elsevier B.V. All rights reserved.

引用

页码：103 / 109

页数：7

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