The kinetic and analytical behaviours of an L-lysine amperometric biosensor based on lysine oxidase immobilised onto a platinum electrode by co-crosslinking

被引:31
作者
Guerrieri, Antonio [1 ]
Cataldi, Tornmaso R. I. [1 ]
Ciriello, Rosanna [1 ]
机构
[1] Univ Basilicata, Dipartimento Chim, I-85100 Potenza, Italy
关键词
enzyme immobilization; enzyme co-crosslinking; lysine oxidase lysine; biosensor; drug analysis;
D O I
10.1016/j.snb.2007.03.025
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
An improved L-lysine amperometric biosensor based on lysine oxidase immobilised onto a platinum electrode by glutaraldehyde co-crosslinking with bovine serum albumin is described. A thoroughly optimization of the enzyme immobilization procedure permitted the fabrication of a fast-response biosensor with high sensitivity and improved stability. Moreover, the relevant electrochemical study showed the possibility to tune the overall kinetic control of biosensor from merely diffusive to enzymatic or mixed by switching the pH from weakly alkaline to weakly acid values, respectively, as well as by controlling its hydrodynamic behaviour. The response time, t(0.95), evaluated in batch addition experiments, was lower than 6 s. Linear lysine responses up to 0.6 M were observed with a sensitivity of 4.4 mu A mM(-1), while detection limit at S/N = 3 was 1 mu M. The sensor has been tested for lysine determination of a pharmaceutical sample obtaining a good agreement with the expected values. (C) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:424 / 430
页数:7
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