Optimum conditions for lipase immobilization on chitosan-coated Fe3O4 nanoparticles

被引：187

作者：

Kuo, Chia-Hung ^{[1
]}

Liu, Yung-Chuan ^{[2
]}

Chang, Chieh-Ming J. ^{[2
]}

Chen, Jiann-Hwa ^{[3
]}

Chang, Cheng ^{[1
]}

Shieh, Chwen-Jen ^{[1
]}

机构：

[1] Natl Chung Hsing Univ, Ctr Biotechnol, Taichung 402, Taiwan

[2] Natl Chung Hsing Univ, Dept Chem Engn, Taichung 402, Taiwan

[3] Natl Chung Hsing Univ, Grad Inst Mol Biol, Taichung 402, Taiwan

来源：

CARBOHYDRATE POLYMERS | 2012年 / 87卷 / 04期

关键词：

Lipase; Magnetic Fe3O4; Chitosan; Immobilization; Response surface methodology (RSM); MAGNETIC-FIELD; ALPHA-AMYLASE;

D O I：

10.1016/j.carbpol.2011.11.026

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Magnetic Fe3O4-chitosan nanoparticles are prepared by the coagulation of an aqueous solution of chitosan with Fe3O4 nanoparticles. The characterization of Fe3O4-chitosan is analyzed by FTIR, FESEM, and SQUID magnetometry. The Fe3O4-chitosan nanoparticles are used for the covalent immobilization of lipase from Candida rugosa using N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide (EDC) and N-hydroxysuccinimide (NHS) as coupling agents. The response surface methodology (RSM) was employed to search the optimal immobilization conditions and understand the significance of the factors affecting the immobilized lipase activity. Based on the ridge max analysis, the optimum immobilization conditions were immobilization time 2.14h, pH 6.37, and enzyme/support ratio 0.73 (w/w); the highest activity obtained was 20 U/g Fe3O4-chitosan. After twenty repeated uses, the immobilized lipase retains over 83% of its original activity. The immobilized lipase shows better operational stability, including wider thermal and pH ranges, and remains stable after 13 days of storage at 25 degrees C. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：2538 / 2545

页数：8

共 26 条

[1]

[Anonymous], [No title captured]

[2] Optimization of immobilization conditions of Thermomyces lanuginosus lipase on styrene-divinylbenzene copolymer using response surface methodology [J].

Aybastier, Oender ;

Demir, Cevdet .

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2010, 63 (3-4) :170-178

[3] Preparation and characterization of epoxy-functionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes [J].

Bayramoglu, Gulay ;

Yilmaz, Meltem ;

Arica, M. Yakup .

BIOPROCESS AND BIOSYSTEMS ENGINEERING, 2010, 33 (04) :439-448

[4] Esterification activity and stability of Talaromyces thermophilus lipase immobilized onto chitosan [J].

Belhaj-Ben Romdhane, Ines ;

Ben Romdhane, Zamen ;

Gargouri, Ali ;

Belghith, Hafedh .

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2011, 68 (3-4) :230-239

[5] Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups [J].

Chiou, SH ;

Wu, WT .

BIOMATERIALS, 2004, 25 (02) :197-204

[6] Lipase from Thermomyces lanuginosus: Uses and prospects as an industrial biocatalyst [J].

Fernandez-Lafuente, Roberto .

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2010, 62 (3-4) :197-212

[7] Magnetite Nanoparticle-Linked Immunosorbent Assay [J].

Gao, Lizeng ;

Wu, Jiamin ;

Lyle, Sarah ;

Zehr, Keith ;

Cao, Liangliang ;

Gao, Di .

JOURNAL OF PHYSICAL CHEMISTRY C, 2008, 112 (44) :17357-17361

[8] Lipase-catalyzed synthesis of partial acylglycerols of acetoacetate [J].

Haas, Michael J. ;

Fox, Pamela S. ;

Foglia, Thomas A. .

EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY, 2011, 113 (02) :168-179

[9] Covalent binding of α-chymotrypsin on the magnetic nanogels covered by amino groups [J].

Hong, Jun ;

Xu, Dongmei ;

Gong, Peijun ;

Sun, Hanwen ;

Dong, Li ;

Yao, Side .

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2007, 45 (3-4) :84-90

[10] Analysis of freeze-gelation and cross-linking processes for preparing porous chitosan scaffolds [J].

Hsieh, Chien-Yang ;

Tsai, Sung-Pei ;

Ho, Ming-Hwa ;

Wang, Da-Ming ;

Liu, Chung-En ;

Hsieh, Cheng-Hsuan ;

Tseng, Hsien-Chung ;

Hsieh, Hsyue-Jen .

CARBOHYDRATE POLYMERS, 2007, 67 (01) :124-132

← 1 2 3 →