Electron transfer properties and electrocatalytic behavior of tyrosinase on ZnO nanorod
Electron transfer properties and electrocatalytic behavior of tyrosinase on ZnO nanorod
复制标题
ZnO纳米棒上酪氨酸酶的电子传递特性及电催化行为
DOI：
10.1016/j.jelechem.2008.01.009
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发表时间：
2008-06-01
影响因子：
4.5
通讯作者：
Xu, Chunxiang
中科院分区：
文献类型：
--
作者：
Chen, Liyuan;Gu, Baoxiang;Xu, Chunxiang
研究了酪氨酸酶在ZnO纳米棒上的吸附及其电催化行为。在中性溶液中，具有低等电点的蘑菇酪氨酸酶有望通过静电吸引附着在带正电荷的ZnO纳米棒表面。扫描电子显微镜和光谱分析表明酪氨酸酶在ZnO纳米棒上的吸附，吸附后的酪氨酸酶在很大程度上保持了其生物活性。在酪氨酸酶的作用下，得到了形貌大致呈杯状的纳米ZnO薄膜.这种开放的三维枝状结构使Fe（CN）（6）（3-/4-）更容易穿过GCE并与GCE交换电子，从而加速了电活性Fe（CN）（6）（3-/4-）与GCE之间的电子转移。吸附的酪氨酸酶对苯酚和邻苯二酚具有催化氧化作用。苯酚和邻苯二酚的线性浓度范围分别为0.02至0.1 mM和0.01至0.4 mM。表观米氏常数（K-M（app））反映了酶的亲和力，对于苯酚为0.24 mM，对于邻苯二酚为1.75 mM，这表明对酚类化合物具有较大的亲和力。该方法为进一步研究蛋白质在纳米结构材料上的固定化和电化学提供了一条途径。(c)2008 Elsevier B. V.保留所有权利。
In this work, the adsorption of tyrosinase on ZnO nanorods and its electrocatalytic behaviors were investigated. The mushroom tyrosinase with low isoelectrie point was expected to adhere on the positively charged surface of ZnO nanorods by electrostatic attraction in a neutral solution. Scanning electron microscope images and spectroscopic analysis demonstrated the adsorption of tyrosinase on ZnO nanorods and the adsorbed tyrosinase remain its bioactivity to a large extent. In the presence of tyrosmase, a roughly and cyathiform of nanosized ZnO films was obtained. This open, three-dimensioned ramiform, structure made the Fe(CN)(6)(3-/4-) move through and exchange the electron with GCE more easily, and thus accelerating the electron transfer between electroactive Fe(CN)(6)(3-/4-) and GCE. The adsorbed tyrosinase could catalyze the oxidation of phenol and catechol. The linear concentration ranges were from 0.02 to 0.1 mM and 0.01 to 0.4 mM, for phenol and catechol, respectively. The apparent Michaelis-menten constant (K-M(app)), a reflection of the enzymatic affinity, was 0.24 mM for phenol and 1.75 mM for catechol, which suggests a large affinity to phenolic compound. The proposed methods presented a way for further studies of the immobilization and electrochemistry of proteins on nanostructured materials. (c) 2008 Elsevier B.V. All rights reserved.