Role of Organic Solvents in Immobilizing Fungus Laccase on Single Walled Carbon Nanotubes for Improved Current Response in Direct Bioelectrocatalysis

被引:78
作者
Wu, Fei [1 ,2 ]
Su, Lei. [1 ]
Yu, Ping [1 ,2 ]
Mao, Lanqun [1 ,2 ]
机构
[1] Chinese Acad Sci, Beijing Natl Lab Mol Sci, Key Lab Analyt Chem Living Biosyst, Inst Chem, Beijing 100190, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
基金
中国国家自然科学基金; 中国博士后科学基金;
关键词
DIRECT ELECTRON-TRANSFER; PROTEIN SECONDARY STRUCTURE; ELECTROCATALYTIC OXYGEN REDUCTION; TRAMETES-HIRSUTA LACCASE; MULTI-COPPER OXIDASES; DIRECT ELECTROCHEMISTRY; GOLD NANOPARTICLES; ENZYME IMMOBILIZATION; ADSORPTION; O-2;
D O I
10.1021/jacs.6b11469
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Improving bioelectrocatalytic current response of redox enzymes on electrodes has been a focus in the development of enzymatic biosensors and biofuel cells. Herein a mediatorless electroreduction of oxygen is effectively improved in terms of a remarkable enhancement by ca. 600% in maximum reductive current by simply adding 20% ethanol into laccase solution during its immobilization onto single-walled carbon nanotubes (SWCNTs). Conformation analysis by circular dichroism and attenuated total reflectance infrared spectroscopy demonstrate promoted laccase-SWCNTs contact by ethanol, thus leading to favorable enzyme orientation on SWCNTs. Extended investigation on acetone-, acetonitrile-, N,N-dimethylformamide (DMF)-, or dimethyl sulfoxide (DMSO)-treated laccase-SWCNTs electrodes shows a 400% and 350% current enhancement at maxima upon acetone and acetonitrile treatment, respectively, and a complete diminish of reductive current by DMF and DMSO. These results together reveal the important role of organic solvents in regulating laccase immobilization for direct bioelectrocatalysis by balancing surface wetting and protein denaturing.
引用
收藏
页码:1565 / 1574
页数:10
相关论文
共 90 条
[1]  
[Anonymous], CELL MOL LIFE SCI, DOI DOI 10.1007/s00018-014-1828-4
[2]   The infrared absorption of amino acid side chains [J].
Barth, A .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 2000, 74 (3-5) :141-173
[3]  
BEREZIN IV, 1978, DOKL AKAD NAUK SSSR+, V240, P615
[4]   A chloride resistant high potential oxygen reducing biocathode based on a fungal laccase incorporated into an optimized Os-complex modified redox hydrogel [J].
Beyl, Yvonne ;
Guschin, Dmitrii A. ;
Shleev, Sergey ;
Schuhmann, Wolfgang .
ELECTROCHEMISTRY COMMUNICATIONS, 2011, 13 (05) :474-476
[5]   Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase, laccase, directly attached to chemically modified carbons [J].
Blanford, Christopher F. ;
Foster, Carina E. ;
Heath, Rachel S. ;
Armstrong, Fraser A. .
FARADAY DISCUSSIONS, 2008, 140 :319-335
[6]   A stable electrode for high-potential, electrocatalytic O2 reduction based on rational attachment of a blue copper oxidase to a graphite surface [J].
Blanford, Christopher F. ;
Heath, Rachel S. ;
Armstrong, Fraser A. .
CHEMICAL COMMUNICATIONS, 2007, (17) :1710-1712
[7]   Peculiarities of direct bioelectrocatalysis by laccase in aqueous-nonaqueous mixtures [J].
Bogdanovskaya, VA ;
Tarasevich, MR ;
Kuznetsova, LN ;
Reznik, MF ;
Kasatkin, EV .
BIOSENSORS & BIOELECTRONICS, 2002, 17 (11-12) :945-951
[8]  
BOGDANOVSKAYA VA, 1986, SOV ELECTROCHEM+, V22, P697
[9]   PEI-coated gold nanoparticles decorated with laccase: A new platform for direct electrochemistry of enzymes and biosensing applications [J].
Brondani, Daniela ;
de Souza, Bernardo ;
Souza, Bruno S. ;
Neves, Ademir ;
Vieira, Iolanda C. .
BIOSENSORS & BIOELECTRONICS, 2013, 42 :242-247
[10]   Adsorption of polar and nonpolar organic chemicals to carbon nanotubes [J].
Chen, Wei ;
Duan, Lin ;
Zhu, Dongqiang .
ENVIRONMENTAL SCIENCE & TECHNOLOGY, 2007, 41 (24) :8295-8300