Format

Send to

Choose Destination
Biosens Bioelectron. 2019 Feb 1;126:170-177. doi: 10.1016/j.bios.2018.10.013. Epub 2018 Oct 13.

Significant enhancement of direct electric communication across enzyme-electrode interface via nano-patterning of synthetic glucose dehydrogenase on spatially tunable gold nanoparticle (AuNP)-modified electrode.

Author information

1
School of Earth Sciences and Environmental Engineering, Gwangju Institute of Science and Technology (GIST), 261 Cheomdan-gwagiro, Buk-gu, Gwangju 61005, Republic of Korea.
2
School of Electrical Engineering and Computer Science, Gwangju Institute of Science and Technology (GIST), 261 Cheomdan-gwagiro, Buk-gu, Gwangju 61005, Republic of Korea.
3
Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, Republic of Korea.
4
School of Earth Sciences and Environmental Engineering, Gwangju Institute of Science and Technology (GIST), 261 Cheomdan-gwagiro, Buk-gu, Gwangju 61005, Republic of Korea. Electronic address: ischang@gist.ac.kr.

Abstract

In this study, the effect of inter-enzyme steric hindrance that occurs during enzyme immobilization on the electrode, on direct electrical communications of enzyme with electrode was investigated via nano-patterning of enzymes on the electrode. Here, the nano-patterning of enzymes was achieved through the combination of DET-capable enzyme that was produced via fusion of site-specific gold binding peptide (GBP) to catalytic subunit of enzyme and gold nanoparticle (AuNP) array with highly tunable dimensions of AuNPs, resulting in spatially controllable enzyme-electrode. The nano-scale spatial control between immobilized enzymes on the highly tuned AuNPs shows different DET efficiency across the enzyme-electrode interface, showing 18.47% of maximum electron recovery which is 3.2-fold enhanced electron recovery efficiency compared to spatially non-controlled enzymes on the electrode where showed 5.7% of electron recovery. The result affirms that inter-enzyme interaction is a significant parameter that decides the enzyme-electrode performance.

KEYWORDS:

Charge transfer resistance; Direct electron transfer; Enzyme nano-patterning; Immobilization; Protein agglomeration

PMID:
30399519
DOI:
10.1016/j.bios.2018.10.013
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center