Engineered Glucose Oxidase Capable of Quasi-Direct Electron Transfer after a Quick-and-Easy Modification with a Mediator.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
08 Feb 2020
Historique:
received: 03 01 2020
revised: 04 02 2020
accepted: 05 02 2020
entrez: 13 2 2020
pubmed: 13 2 2020
medline: 1 12 2020
Statut: epublish

Résumé

Glucose oxidase (GOx) has been widely utilized for monitoring glycemic levels due to its availability, high activity, and specificity toward glucose. Among the three generations of electrochemical glucose sensor principles, direct electron transfer (DET)-based third-generation sensors are considered the ideal principle since the measurements can be carried out in the absence of a free redox mediator in the solution without the impact of oxygen and at a low enough potential for amperometric measurement to avoid the effect of electrochemically active interferences. However, natural GOx is not capable of DET. Therefore, a simple and rapid strategy to create DET-capable GOx is desired. In this study, we designed engineered GOx, which was made readily available for single-step modification with a redox mediator (phenazine ethosulfate, PES) on its surface via a lysine residue rationally introduced into the enzyme. Thus, PES-modified engineered GOx showed a quasi-DET response upon the addition of glucose. This strategy and the obtained results will contribute to the further development of quasi-DET GOx-based glucose monitoring dedicated to precise and accurate glycemic control for diabetic patient care.

Identifiants

pubmed: 32046321
pii: ijms21031137
doi: 10.3390/ijms21031137
pmc: PMC7036908
pii:
doi:

Substances chimiques

Blood Glucose 0
Fungal Proteins 0
Phenazines 0
5-ethylphenazine 10510-77-7
Glucose Oxidase EC 1.1.3.4
Glucose IY9XDZ35W2

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Déclaration de conflit d'intérêts

The authors declare no conflict of interest.

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Auteurs

Nanami Suzuki (N)

Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan.

Jinhee Lee (J)

Joint Department of Biomedical Engineering, The University of North Carolina at Chapel Hill and North Carolina State University, Chapel Hill, NC 27599, USA.

Noya Loew (N)

Joint Department of Biomedical Engineering, The University of North Carolina at Chapel Hill and North Carolina State University, Chapel Hill, NC 27599, USA.

Yuka Takahashi-Inose (Y)

Ultizyme International Ltd., 3-9-5. Taihei, Sumida, Tokyo 130-0012, Japan.

Junko Okuda-Shimazaki (J)

Joint Department of Biomedical Engineering, The University of North Carolina at Chapel Hill and North Carolina State University, Chapel Hill, NC 27599, USA.

Katsuhiro Kojima (K)

Ultizyme International Ltd., 3-9-5. Taihei, Sumida, Tokyo 130-0012, Japan.

Kazushige Mori (K)

Ultizyme International Ltd., 3-9-5. Taihei, Sumida, Tokyo 130-0012, Japan.

Wakako Tsugawa (W)

Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan.

Koji Sode (K)

Joint Department of Biomedical Engineering, The University of North Carolina at Chapel Hill and North Carolina State University, Chapel Hill, NC 27599, USA.

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Classifications MeSH