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High catalytic activity of immobilized laccase on core-shell magnetic nanoparticles by dopamine self-polymerization
Alternative TitleJ. Mol. Catal. B-Enzym.
Deng, Manfeng1,2; Zhao, He2; Zhang, Songping3; Tian, Chunyong3; Zhang, Di2; Du, Penghui2; Liu, Chenming2; Cao, Hongbin2,4; Li, Heping1
2015-02-01
Source PublicationJOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN1381-1177
Volume112Issue:FEBPages:15-24
Abstract

A facile and efficient method is developed for enzyme immobilization on silica-coated magnetic nanoparticles (Fe3O4@SiO2 NPs) via dopamine (DA) self-polymerization process. The scanning electron microscope images indicate that Fe3O4@SiO2 NPs have a spherical and uniform size distribution, and the high saturation magnetization (14.68 emu g(-1)) makes it easily to be separated from the reaction system under an extra magnetic field. Fourier-transform infrared spectroscopy and thermogravimetric analysis reveal that polydopamine (PDA) has been successfully coated on Fe3O4@SiO2 NPs surface. During in situ polymerization of DA, laccase is also firmly immobilized on Fe3O4@SiO2 NPs, and the total activity recovery can reach to 43.28%. However, the laccase immobilized by glutaraldehyde (GA) crosslinking method only keeps 3.33% of the total activity recovery under the optimized condition. Compared with free laccase and laccase immobilized by GA, the laccase immobilized by DA exhibits superior resistance to a broader pH value and obviously enhanced stability. After 10 times reusing cycles, the activity of laccase immobilized by DA still retains 65% of its initial activity, whereas the laccase immobilized by GA has 35% of its original activity. After 70 days of storage at 4 degrees C, the laccase immobilized by DA keeps about 80% of its initial activity, but the free laccase and the laccase immobilized by GA only remained 7.8% and 37%, respectively. Thus, this work provides a method for laccase immobilization with advantages of environmentally friendly, low cost and high catalytic activity. (C) 2014 Elsevier B.V. All rights reserved.

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A facile and efficient method is developed for enzyme immobilization on silica-coated magnetic nanoparticles (Fe3O4@SiO2 NPs) via dopamine (DA) self-polymerization process. The scanning electron microscope images indicate that Fe3O4@SiO2 NPs have a spherical and uniform size distribution, and the high saturation magnetization (14.68 emu g(-1)) makes it easily to be separated from the reaction system under an extra magnetic field. Fourier-transform infrared spectroscopy and thermogravimetric analysis reveal that polydopamine (PDA) has been successfully coated on Fe3O4@SiO2 NPs surface. During in situ polymerization of DA, laccase is also firmly immobilized on Fe3O4@SiO2 NPs, and the total activity recovery can reach to 43.28%. However, the laccase immobilized by glutaraldehyde (GA) crosslinking method only keeps 3.33% of the total activity recovery under the optimized condition. Compared with free laccase and laccase immobilized by GA, the laccase immobilized by DA exhibits superior resistance to a broader pH value and obviously enhanced stability. After 10 times reusing cycles, the activity of laccase immobilized by DA still retains 65% of its initial activity, whereas the laccase immobilized by GA has 35% of its original activity. After 70 days of storage at 4 degrees C, the laccase immobilized by DA keeps about 80% of its initial activity, but the free laccase and the laccase immobilized by GA only remained 7.8% and 37%, respectively. Thus, this work provides a method for laccase immobilization with advantages of environmentally friendly, low cost and high catalytic activity. (C) 2014 Elsevier B.V. All rights reserved.

KeywordMagnetic Nanoparticle Laccase Dopamine Immobilization Glutaraldehyde
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.molcatb.2014.11.012
URL查看原文
Indexed BySCI
Language英语
WOS KeywordNANOFIBROUS MEMBRANE ; TRAMETES-VERSICOLOR ; GOLD NANOPARTICLES ; POLYDOPAMINE ; SURFACE ; SEPARATION ; WATER ; DEGRADATION ; ENRICHMENT ; CHEMISTRY
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Physical
WOS IDWOS:000349592700003
Citation statistics
Cited Times:26[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/11723
Collection研究所(批量导入)
Affiliation1.Changsha Univ Sci & Technol, Hunan Prov Key Lab Mat Protect Elect Power & Tran, Key Lab Rd Struct & Mat, Minist Transport Changsha, Changsha 410114, Hunan, Peoples R China
2.Beijing Engn Res Ctr Proc Pollut Control, Beijing 100190, Peoples R China
3.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
4.Chinese Acad Sci, Inst Proc Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Deng, Manfeng,Zhao, He,Zhang, Songping,et al. High catalytic activity of immobilized laccase on core-shell magnetic nanoparticles by dopamine self-polymerization[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2015,112(FEB):15-24.
APA Deng, Manfeng.,Zhao, He.,Zhang, Songping.,Tian, Chunyong.,Zhang, Di.,...&Li, Heping.(2015).High catalytic activity of immobilized laccase on core-shell magnetic nanoparticles by dopamine self-polymerization.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,112(FEB),15-24.
MLA Deng, Manfeng,et al."High catalytic activity of immobilized laccase on core-shell magnetic nanoparticles by dopamine self-polymerization".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 112.FEB(2015):15-24.
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