Skip to main content
Log in

Construction of a biocathode using the multicopper oxidase from the hyperthermophilic archaeon, Pyrobaculum aerophilum: towards a long-life biobattery

  • Original Research Paper
  • Published:
Biotechnology Letters Aims and scope Submit manuscript

Abstract

Objectives

The life of biobatteries remains an issue due to loss of enzyme activity over time. In this study, we sought to develop a biobattery with a long life using a hyperthermophilic enzyme.

Results

We hypothesized that use of such hyperthermophilic enzymes would allow for the biofuel cells to have a long battery life. Using pyrroloquinoline quinone-glucose dehydrogenase and the multicopper oxidase from Pyrobaculum aerophilum, we constructed an anode and cathode. The maximum output was 11 μW at 0.2 V, and the stability of the both electrode was maintained at 70 % after 14 days.

Conclusion

The biofuel cells that use hyperthermophilic enzymes may prolong their life.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4

Similar content being viewed by others

References

  • Fenga PG, Cardoso FP, Neto SA, Andrade ARD (2013) Multiwalled carbon nanotubes to improve ethanol/air biofuel cells. Electrochim Acta 106:109–113

    Article  CAS  Google Scholar 

  • Fernandez-Sanchez C, Tzanov T, Gubitz GM, Cavaco-Paulo A (2002) Voltammetric monitoring of laccase-catalysed mediated reactions. Bioelectrochemistry 58:149–156

    Article  CAS  PubMed  Google Scholar 

  • Karnicka K, Miecznikowski K, Kowalewska B, Skunik M, Opallo M, Rogalski J, Schuhmann W, Kulesza PJ (2008) ABTS-modified multiwalled carbon nanotubes as an effective mediating system for bioelectrocatalytic reduction of O2. Anal Chem 80:7643–7648

    Article  CAS  PubMed  Google Scholar 

  • Kim J, Jia H, Wang P (2006) Challenges in biocatalysis for enzyme-based biofuel cells. Biotech Adv 24:296–308

    Article  CAS  Google Scholar 

  • Koto A, Taniya S, Sakamoto H, Satomura T, Sakuraba H, Ohshima T, Suye S (2014) Efficient direct electron transfer for a highly oriented PQQ-GDH immobilized electrode for bioanode. J Biosens Bioelectron 5:1000148

    Google Scholar 

  • Krzemiński L, Cronin S, Ndamba L, Canters GW, Aartsma TJ, Evans SD, Jeuken LJC (2011) Orientation control over nitrite reductase on modified gold electrode and its effects on the interfacial electrode transfer. J Phys Chem B 115:12607–12614

    Article  PubMed  Google Scholar 

  • Lee JY, Shin HY, Kang SW, Park C, Kim SW (2010) Use of bioelectrode containing DNA-wrapped single-walled carbon nanotubes for enzyme-based biofuel cell. J Power Sources 195:750–755

    Article  CAS  Google Scholar 

  • Olejnik P, Palys B, Kowalczyk A, Nowicka AM (2012) Orientation of laccase and carged surfaces. Mediatorless O2 reduction on amino- and carboxyl-Ended ethylphenyl groups. J Phys Chem C 116:25911–25918

    Article  CAS  Google Scholar 

  • Osman MH, Shah AA, Walsh FC (2011) Recent progress and continuing challenges in bio-fuel cells. Biosens Bioelectron 26:3087–3102

    Article  CAS  PubMed  Google Scholar 

  • Palmore GTR, Kim HH (1999) Electro-enzymatic reduction of dioxygen to water in the cathode compartment of a biofuel cell. J Electroanal Chem 464:110–117

    Article  CAS  Google Scholar 

  • Ramanavicius A, Kausaite A, Ramanaviciene A (2008) Enzymatic biofuel cell based on anode and cathode powered by ethanol. Biosens Bioelectron 24:761–766

    Article  CAS  Google Scholar 

  • Ray S, Chand S, Zhang Y, Nussbaum S, Rajeshwar K (2013) Implications of active site orientation in myoglobin for direct electron transfer and electrocatalysis based on monolayer and multilayer covalent immobilization on gold electrodes. Electrochim Acta 99:85–93

    Article  CAS  Google Scholar 

  • Sakuraba H, Yokono K, Yoneda K, Watanabe A, Asada Y, Satomura T, Yabutani T, Motonaka J, Ohshima T (2010) Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum. Arch Biochem Biophys 502:81–88

    Article  CAS  PubMed  Google Scholar 

  • Sakuraba H, Koga K, Yoneda K, Kashima Y, Ohshima T (2011) Structure of a muticopper oxidase from the hyperthermophilic archaeon Pyrobaculum islandicum. Acta Cryst F67:753–757

    Google Scholar 

Download references

Acknowledgments

This work was supported by the Japan Society for the Promotion of Science (JSPS) KAKENHI (23510127) Grant-in-Aid for Scientific Research (C).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Shin-ichiro Suye.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Sakamoto, H., Uchii, T., Yamaguchi, K. et al. Construction of a biocathode using the multicopper oxidase from the hyperthermophilic archaeon, Pyrobaculum aerophilum: towards a long-life biobattery. Biotechnol Lett 37, 1399–1404 (2015). https://doi.org/10.1007/s10529-015-1819-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10529-015-1819-z

Keywords

Navigation