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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.

Citation

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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