High catalytic activity of immobilized laccase on core-shell magnetic nanoparticles by dopamine self-polymerization | |
Deng, Manfeng1,2; Zhao, He2; Zhang, Songping3; Tian, Chunyong3; Zhang, Di2; Du, Penghui2; Liu, Chenming2; Cao, Hongbin2,4; Li, Heping1 | |
刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC |
2015-02-01 | |
卷号 | 112期号:FEB页码:15-24 |
关键词 | Magnetic nanoparticle Laccase Dopamine Immobilization Glutaraldehyde |
ISSN号 | 1381-1177 |
其他题名 | J. Mol. Catal. B-Enzym. |
中文摘要 | 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. |
英文摘要 | 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. |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
类目[WOS] | Biochemistry & Molecular Biology ; Chemistry, Physical |
研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
关键词[WOS] | NANOFIBROUS MEMBRANE ; TRAMETES-VERSICOLOR ; GOLD NANOPARTICLES ; POLYDOPAMINE ; SURFACE ; SEPARATION ; WATER ; DEGRADATION ; ENRICHMENT ; CHEMISTRY |
收录类别 | SCI |
原文出处 | |
语种 | 英语 |
WOS记录号 | WOS:000349592700003 |
公开日期 | 2015-04-01 |
内容类型 | 期刊论文 |
源URL | [http://ir.ipe.ac.cn/handle/122111/11723] |
专题 | 过程工程研究所_研究所(批量导入) |
作者单位 | 1.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 |
推荐引用方式 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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