Yildiz Huseyin Bekir, Sahmetlioglu Ertugrul, Boyukbayram Ayse Elif, Toppare Levent, Yagci Yusuf
Department of Chemistry, Middle East Technical University, 06531 Ankara, Turkey.
Int J Biol Macromol. 2007 Aug 1;41(3):332-7. doi: 10.1016/j.ijbiomac.2007.04.006. Epub 2007 May 5.
Immobilization of tyrosinase and alcohol oxidase is achieved in the copolymer of pyrrole with vinyl alcohol with thiophene side groups (PVATh-co-PPy) which is a newly synthesized conducting polymer. PVATh-co-PPy/alcohol oxidase and PVATh-co-PPy/tyrosinase electrodes are constructed by the entrapment of enzyme in conducting copolymer matrix during electrochemical copolymerization. For tyrosinase and alcohol oxidase enzymes, catechol and ethanol are used as the substrates, respectively. Kinetic parameters: maximum reaction rates (V(max)) and Michaelis-Menten constants (K(m)) are obtained. V(max) and K(m) are found as 2.75 micromol/(minelectrode) and 18 mM, respectively, for PVATh-co-PPy/alcohol oxidase electrode and as 0.0091micromol/(minelectrode) and 40 mM, respectively, for PVATh-co-PPy/tyrosinase electrode. Maximum temperature and pH values are investigated and found that both electrodes have a wide working range with respect to both temperature and pH. Operational and storage stabilities show that although they have limited storage stabilities, the enzyme electrodes are useful with respect to operational stabilities.
酪氨酸酶和乙醇氧化酶固定于吡咯与带有噻吩侧基的乙烯醇的共聚物(PVATh-co-PPy)中,PVATh-co-PPy是一种新合成的导电聚合物。PVATh-co-PPy/乙醇氧化酶电极和PVATh-co-PPy/酪氨酸酶电极是通过在电化学共聚过程中将酶包埋于导电共聚物基质中构建而成。对于酪氨酸酶和乙醇氧化酶,分别使用儿茶酚和乙醇作为底物。获得了动力学参数:最大反应速率(V(max))和米氏常数(K(m))。对于PVATh-co-PPy/乙醇氧化酶电极,V(max)和K(m)分别为2.75微摩尔/(分钟电极)和18毫摩尔;对于PVATh-co-PPy/酪氨酸酶电极,V(max)和K(m)分别为0.0091微摩尔/(分钟电极)和40毫摩尔。研究了最高温度和pH值,发现两种电极在温度和pH方面都有较宽的工作范围。操作稳定性和储存稳定性表明,尽管它们的储存稳定性有限,但酶电极在操作稳定性方面是有用的。