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Enzyme immobilization is one of the key factors in constructing high-performance enzyme biosensors and biofuel cells (BFCs). Herein, we propose a new protocol for efficient immobilization of a glycoprotein enzyme based on the interaction of the 1, 2- or 1, 3-diols in the glycoprotein with a boronic acid functionalized monomer. Briefly, casting a mixture of glucose oxidase (GOx) and anilineboronic acid (ABA) followed by a NaAuCl(4) solution to an Au-plated Au electrode surface yielded a GOx-poly(ABA) (PABA)-gold nanoparticle (Au(nano)) bionanocomposite, and chitosan (CS) was then cast and air-dried. In the present protocol, the small-sized Au(nano) or Au subnanostructures can form near/on the enzyme molecule, which greatly promotes the electron transfer of enzymatic reaction and enhances the amperometric responses. The thus-prepared CS/GOx-PABA-Au(nano)/Au-plated Au electrode worked well in the first-/second generation biosensing modes and as a bioanode in a monopolar biofuel cell, with analytical or cell-power performance superior to those of most analogues hitherto reported. Copyright © 2011 Elsevier B.V. All rights reserved.


Yi Huang, Xiaoli Qin, Zou Li, Yingchun Fu, Cong Qin, Feng Wu, Zhaohong Su, Ming Ma, Qingji Xie, Shouzhuo Yao, Jiming Hu. Fabrication of a chitosan/glucose oxidase-poly(anilineboronic acid)-Au(nano)/Au-plated Au electrode for biosensor and biofuel cell. Biosensors & bioelectronics. 2012 Jan 15;31(1):357-62

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PMID: 22099959

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