详细信息

Spacer arm-facilitated tethering of laccase on magnetic polydopamine nanoparticles for efficient biocatalytic water treatment  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Spacer arm-facilitated tethering of laccase on magnetic polydopamine nanoparticles for efficient biocatalytic water treatment

作者:Chen, Chao[1];Sun, Wen[1];Lv, Hangya[1];Li, Hui[2];Wang, Yibing[1];Wang, Ping[1,3]

机构:[1]East China Univ Sci & Technol, Sch Biotechnol, Shanghai Collaborat Innovat Ctr Biomfg, State Key Lab Bioreactor Engn,Biomed Nanotechnol, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, State Environm Protect Key Lab Environm Risk Asse, State Key Lab Bioreactor Engn, Sch Resources & Environm Engn, Shanghai 200237, Peoples R China;[3]Univ Minnesota, Dept Bioprod & Biosyst Engn, St Paul, MN 55108 USA

年份:2018

卷号:350

起止页码:949

外文期刊名:CHEMICAL ENGINEERING JOURNAL

收录:;EI(收录号:20182505322050);WOS:【SCI-EXPANDED(收录号:WOS:000437093000095)】;

基金:This work was supported by the National Natural Science Foundation of China (31471659, 21636003 and 21303050). Authors thank the support from Jiangsu National Synergetic Innovation Center for Advanced Materials (SICAM).

语种:英文

外文关键词:Magnetic nanoparticles; Polydopamine (PDA); dialdehyde starch (DAS); Enzyme immobilization; Laccase

摘要:Development of high performance biocatalysts generally seeks enhanced specific enzyme activities under intensified reaction conditions. This work reports a novel polydopamine fabricated Fe3O4 nanoparticles for incorporation with enzymes through the formation of flexible spacer arms using dialdehyde starch (DAS). It appeared that the biocompatible microenvironment and flexible tethering at the particle interface could effectively improve performance of the immobilized enzyme. In a test with laccase, such fabricated nanoparticles could reach enzyme loadings as high as 242 mg/g, while retained 69% specific enzyme activity. At the same time, the spacer arm-facilitated immobilization reduced the conformation changes with the control of interfacial action between enzyme and nanoparticles. Furthermore, the immobilized enzyme showed much improved stability against pH and thermal inactivation compared to free laccase. As a result, the immobilized laccase exhibited high degradation efficiency and reusability when tested for removal of 2,4-dichlorophenol and more contaminants from water. The results demonstrated a new strategy in fabricating nanomaterials using bio-based polymers for preparation of high performance biocatalysts.

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