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Identification, heterologous expression, and characterization of a new unspecific peroxygenase from Marasmius fiardii PR-910


Unspecific peroxygenases (UPOs) are glycosylated enzymes that provide an efficient method for oxyfunctionalizing a variety of substrates using only hydrogen peroxide (H2O2) as the oxygen donor. However, their poor heterologous expression has hindered their practical application. In the present study, a novel UPO from Marasmius fiardii PR910 (MfiUPO) was identified and heterologously expressed in Pichia pastoris. By employing a two-copy expression cassette, the protein titer reached 1.18 g /L in a 5-L bioreactor, marking the highest record. With its high expression level, rMfiUPO is a promising candidate as an excellent parental template for enhancing desirable traits such as increased stability and selectivity through directed evolution.


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Bioresources and Bioprocessing (BIOB) is a peer-reviewed open access journal published under the brand SpringerOpen. BIOB aims at providing an international academic platform for exchanging views on and promoting research to support bioresource development, processing and utilization in a sustainable manner. As an application-oriented research journal, BIOB covers not only the application and management of bioresource technology but also the design and development of bioprocesses that will lead to new and sustainable production processes.

BIOB publishes original and review articles on most topics relating to bioresource and bioprocess engineering, including:

  • Biochemical and microbiological engineering
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  • Biosynthesis and metabolic engineering
  • Bioprocess and biosystems engineering
  • Bioenergy and biorefinery
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  • Food, agricultural and marine biotechnology
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