Biotechnology and Bioprocess Engineering

, Volume 22, Issue 2, pp 195–199 | Cite as

Expression of NADH-oxidases enhances ethylene productivity in Saccharomyces cerevisiae expressing the bacterial EFE

  • Nina Johansson
  • Karl O. Persson
  • Joakim NorbeckEmail author
  • Christer Larsson
Research Paper


Ethylene is a major petrochemical for which biotechnological production methods are an attractive alternative. Here we use a system based on a bacterial ethylene forming enzyme (EFE) expressed in Saccharomyces cerevisiae. Metabolic modelling performed in a previous study identified re-oxidation of NADH as a factor limiting ethylene production in S. cerevisiae. In line with this, we here found that strains with multicopy plasmid expression of the heterologous oxidases nox and Aox1 led to significantly increased specific ethylene productivity, up 12 and 36%, respectively, compared to the control strain with empty plasmid. However the productivity and yield was only improved in the AOX expressing strain compared to that of the control strain. Both oxidase expressing strains also exhibited increased respiration rates compared to the reference strain, with specific oxygen consumption rates being roughly doubled in both strains. The AOX strain furthermore exhibited a significant increase in the EFE substrate 2-oxoglutarate formation compared to the reference strain, linking an improvement in ethylene production to both increased respiratory capacity and increased substrate availability, thereby corroborating our previous finding.


ethylene Saccharomyces cerevisiae in silico metabolic modelling respiration oxidase 2-oxoglutarate 


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Copyright information

© The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg 2017

Authors and Affiliations

  • Nina Johansson
    • 1
  • Karl O. Persson
    • 2
  • Joakim Norbeck
    • 1
    Email author
  • Christer Larsson
    • 1
  1. 1.Department of Biology and Biological EngineeringChalmers University of TechnologyGothenburgSweden
  2. 2.Department of Chemistry and Molecular BiologyGothenburg UniversityGothenburgSweden

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