Amperometric phenol biosensor based on covalent immobilization of tyrosinase onto an electrochemically prepared novel copolymer poly (N-3-aminopropyl pyrrole-co-pyrrole) film

被引:86
作者
Rajesh [1 ]
Takashima, W [1 ]
Kaneto, K [1 ]
机构
[1] Kyushu Inst Technol, Grad Sch Life Sci & Syst Engn, Wakamatsu Ku, Kitakyushu, Fukuoka 8080196, Japan
基金
日本学术振兴会;
关键词
enzyme; polymer; biosensor; covalent immobilization; peptide linkage;
D O I
10.1016/j.snb.2004.04.028
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
An amperometric biosensor has been developed for the quantitative estimation of phenols in aqueous solution. The enzyme, tyrosinase, also called as poly phenol oxidase (PPO), was covalently immobilized on a novel copolymer poly (N-3-aminopropyl pyrrole-co-pyrrole) (PAPCP) film, electrochemically prepared onto an indium-tin-oxide (ITO) coated glass plate. The covalent linkage of enzyme and porous morphology of the polymer film lead to high enzyme loading and an increased lifetime stability of the enzyme electrode. Amperometric response was measured as a function of concentration of phenol, at fixed bias voltage of -0.2 V versus Ag/AgCl in a phosphate buffer (pH 7.2). The electrode gives a wide linear response range of 1.35-222.3, 1.6-118.8, 1.9-257.8 muM, for phenol, catechol and p-cresol, respectively. The response time is <10 s reaching to a 95% steady state current value, and 80% of the enzyme activity is retained for 4 months. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:271 / 277
页数:7
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