Unspecific Peroxygenases: A New Frontier in Biocatalysis

Strategic Insights -

Researchers at Ruhr-University Bochum have made significant breakthroughs in the field of biocatalysis, specifically in the use of unspecific peroxygenases (UPOs) for various reactions. Supported by Projekt DEAL, the team demonstrated the potential of a bifunctional biocatalyst, comprised of a formate dehydrogenase and an azoreductase, to fuel the activity of UPOs. This novel approach enables the control of hydrogen peroxide delivery, affecting the enantioselectivity of reactions. The study highlights the importance of optimizing peroxide supply and delivery for efficient and selective biocatalysis.

Key Takeaways:

  • Unspecific peroxygenases (UPOs) have been studied extensively for their potential as biocatalysts, capable of performing C-H oxyfunctionalization reactions with hydrogen peroxide as the sole oxidant.
  • The research team developed a bifunctional biocatalyst consisting of a formate dehydrogenase and an azoreductase linked by a peptide, which can produce hydrogen peroxide in situ and fuel UPOs.
  • The delivery and supply level of hydrogen peroxide significantly impact the enantioselectivity and activity of the UPO, demonstrating the importance of control over peroxide availability.
  • Model substrates, such as ethylbenzene and thioanisole, were used to showcase the efficiency of the bifunctional biocatalyst in achieving enantioselective reactions.
  • The study concluded that controlling hydrogen peroxide delivery is crucial for achieving efficient and selective biocatalysis, contributing to the advancement of biocatalytic reactions.
  • Authors Anna Christina R. Ngo, Beyzanur Cicek, Simon Niklas Hermann Hadewig, and Dirk Tischler from Ruhr-University Bochum contributed to the research.
  • Projekt DEAL provided the necessary financial support for this research.

Statistics:

  • 10-fold increase in hydrogen peroxide production was achieved when free FMN was added to the bifunctional biocatalyst.
  • Coupling the fusion protein with UPOs resulted in improved activities of up to 1 mM H2O2, demonstrating the importance of controlling peroxide availability.
  • The study used model substrates, ethylbenzene and thioanisole, to demonstrate the effectiveness of the bifunctional biocatalyst in achieving enantioselective reactions.

Sources:

  • NewsRx. New Findings from Ruhr-University Bochum Update Understanding of Proteomics (Fuelling Unspecific Peroxygenases With In-situ Generated H2o2 Using Enzyme Fusions). Proteomics Weekly. October 20, 2025; p 2136.
  • Fuelling Unspecific Peroxygenases With In-situ Generated H2o2 Using Enzyme Fusions. ChemCatChem, 2025.
  • Ruhr-University Bochum. Microbial Biotechnol, Univ Str 150, D-44780 Bochum, Germany.
  • Projekt DEAL.