Biocathode design with highly-oriented immobilization of multi-copper oxidase from Pyrobaculum aerophilum onto a single-walled carbon nanotube surface via a carbon nanotube-binding peptide.
biocathode
biofuel cell
carbon nanotube
carbon nanotube binding peptide
orientation
Journal
Biotechnology progress
ISSN: 1520-6033
Titre abrégé: Biotechnol Prog
Pays: United States
ID NLM: 8506292
Informations de publication
Date de publication:
01 2021
01 2021
Historique:
received:
19
05
2020
revised:
26
08
2020
accepted:
23
09
2020
pubmed:
6
10
2020
medline:
29
1
2022
entrez:
5
10
2020
Statut:
ppublish
Résumé
Biofuel cells generate electric energy using an enzyme as a catalyst for an electrode but their stability and low battery output pose problems for practical use. To solve these problems, this study aimed to build a long-lasting and high-output biocathode as a catalyst using a highly stable hyperthermophilic archaeal enzyme, multi-copper oxidase, from Pyrobaculum aerophilum (McoP). To increase output, McoP was oriented and immobilized on single-walled carbon nanotubes (SWCNT) with a high specific surface area, and the electrode interface was designed to achieve highly efficient electron transfer between the enzyme and electrode. Type 1 copper (T1Cu), an electron-accepting site in the McoP molecule, is located near the C-terminus. Therefore, McoP was prepared by genetically engineering a CNT-binding peptide with the sequence LLADTTHHRPWT, at the C-terminus of McoP (McoP-CBP). We then constructed an electrode using a complex in which McoP-CBP was aligned and immobilized on SWCNT, and then clarified the effect of CBP. The amounts of immobilized enzymes on McoP-SWCNT and (McoP-CBP)-SWCNT complexes were almost equal. CV measurement of the electrode modified with both complexes showed 5.4 times greater current density in the catalytic reaction of the (McoP-CBP)-SWCNT/GC electrode than in the McoP-SWCNT/GC electrode. This is probably because CBP fusion immobilize the enzyme on SWCNTs in an orientational manner, and T1Cu, the oxidation-reduction site in McoP, is close to the electrode, which improves electron transfer efficiency.
Substances chimiques
Enzymes, Immobilized
0
Nanotubes, Carbon
0
Peptides
0
Oxidoreductases
EC 1.-
copper oxidase
EC 1.16.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3087Informations de copyright
© 2020 American Institute of Chemical Engineers.
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