The electrochemical behavior of a FAD dependent glucose dehydrogenase with direct electron transfer subunit by immobilization on self-assembled monolayers

被引:40
作者
Lee, Inyoung [1 ]
Loew, Noya [1 ]
Tsugawa, Wakako [1 ]
Lin, Chi-En [2 ]
Probst, David [2 ]
La Belle, Jeffrey T. [2 ]
Sode, Koji [1 ,3 ,4 ,5 ]
机构
[1] Tokyo Univ Agr & Technol, Grad Sch Engn, Dept Biotechnol & Life Sci, 2-24-16 Naka Cho, Koganei, Tokyo 1848588, Japan
[2] Arizona State Univ, Sch Biol & Hlth Syst Engn, Harrington Program Biomed Engn, Tempe, AZ 85287 USA
[3] Ultizyme Int Ltd, Meguro Ku, 1-13-16 Minami, Tokyo 1520013, Japan
[4] Univ North Carolina Chapel Hill, Joint Dept Biomed Engn, Chapel Hill, NC 27599 USA
[5] North Carolina State Univ, Chapel Hill, NC 27599 USA
关键词
Self-assembled monolayer; Direct electron transfer; FADGDH; Glucose sensor; BURKHOLDERIA-CEPACIA; TEMPERATURE PROPERTIES; CATALYTIC SUBUNIT; ESCHERICHIA-COLI; SENSOR; ACETAMINOPHEN; EXPRESSION; BIOSENSORS; PRINCIPLE; CLONING;
D O I
10.1016/j.bioelechem.2017.12.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Continuous glucose monitoring (CGM) is a vital technology for diabetes patients by providing tight glycemic control. Currently, many commercially available CGM sensors use glucose oxidase (GOD) as sensor element, but this enzyme is not able to transfer electrons directly to the electrode without oxygen or an electronic mediator. We previously reported a mutated FAD dependent glucose dehydrogenase complex (FADGDH) capable of direct electron transfer (DET) via an electron transfer subunit without involving oxygen or a mediator. In this study, we investigated the electrochemical response of DET by controlling the immobilization of DET-FADGDH using 3 types of self-assembled monolayers (SAMs) with varying lengths. With the employment of DET-FADGDH and SAM, high current densities were achieved without being affected by interfering substances such as acetaminophen and ascorbic acid. Additionally, the current generated from DET-FADGDH electrodes decreased with increasing length of SAM, suggesting that the DET ability can be affected by the distance between the enzyme and the electrode. These results indicate the feasibility of controlling the immobilization state of the enzymes on the electrode surface. (C) 2017 Published by Elsevier B.V.
引用
收藏
页码:1 / 6
页数:6
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