A new tyrosinase biosensor based on covalent immobilization of enzyme on N-(3-aminopropyl) pyrrole polymer film
A new tyrosinase biosensor based on covalent immobilization of enzyme on N-(3-aminopropyl) pyrrole polymer film
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DOI：
10.1016/j.cap.2004.06.001
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发表时间：
2005-02-01
影响因子：
2.4
通讯作者：
Kaneto, K
中科院分区：
文献类型：
--
作者：
Rajesh;Kaneto, K
以酪氨酸酶（PPO）为例，制备了一种n -氨基取代吡咯单体导电聚合物膜，用于生物传感酶的共价固定化。酪氨酸酶通过共价键固定在n取代吡咯聚合物薄膜上，保持其生物活性。用紫外可见光谱和红外光谱对酶电极进行了表征。在-0.2 V和Ag/AgCl下，通过直接电化学还原酶解醌类化合物来定量估计酚类化合物。在酶电极上进行的电流响应测量结果表明，对苯酚、儿茶酚和对甲酚的灵敏度分别为57.6、71.4和45.8 mA M-1 cm(-2)，线性响应范围分别为1.8 ~ 170.2、1.3 ~ 110.1和2.1 ~ 168 mA。该生物传感器对苯酚、儿茶酚和对甲酚的最低检出限分别为0.9、0.7和1.1 ma，在4-5℃下的稳定灵敏度为3个月。(C) 2004 Elsevier B.V.版权所有
A conducting polymer film of N-amino substituted pyrrole monomer has been prepared for covalent immobilization of enzyme for biosensing applications, illustrated by tyrosinase (PPO). The tyrosinase enzyme retains its bioactivity when being immobilized on N-substituted pyrrole polymer film by covalent bonding. The enzyme electrode was characterized by UV - Vis and infrared spectroscopy. Phenolic compounds were quantitatively estimated by the direct electrochemical reduction of enzymatically liberated quinone species at -0.2 V vs. Ag/AgCl. The results of amperometric response measurements conducted on enzyme electrode show sensitivity of 57.6, 71.4 and 45.8 mA M-1 cm(-2) and a linear response range of 1.8-170.2, 1.3-110.1 and 2.1-168 muM for phenol, catechol and p-cresol, respectively. The biosensor exhibits a lowest detection limit of 0.9, 0.7 and 1.1 muM, for phenol, catechol and p-cresol, respectively and a period of stable sensitivity of 3 months at 4-5degreesC. (C) 2004 Elsevier B.V. All rights reserved.