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Magnaporthe oryzae as an expression host for the production of the unspecific peroxygenase AaeUPO from the basidiomycete Agrocybe aegerita
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  • Stefan Jacob,
  • Sebastian Bormann,
  • Michael Becker,
  • Luis Antelo,
  • Dirk Holtmann,
  • Eckhard Thines
Stefan Jacob
Institute of Biotechnology and Drug Research
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Sebastian Bormann
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Michael Becker
Institute of Biotechnology and Drug Research
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Luis Antelo
Institute of Biotechnology and Drug Research
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Dirk Holtmann
Technische Hochschule Mittelhessen
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Eckhard Thines
Johannes Gutenberg University Mainz
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The filamentous fungus Magnaporthe oryzae has the potential to be developed as an alternative platform organism for the heterologous production of industrially important enzymes. M. oryzae is easy to handle, fast-growing and unlike yeast, posttranslational modifications like N-glycosylations are similar to the human organism. Here, we established M. oryzae as a host for the expression of the unspecific peroxygenase from the basidiomycete Agrocybe aegerita (AaeUPO). UPOs are attractive biocatalysts for selective oxyfunctionalization of non-activated carbon-hydrogen bonds. To improve and simplify the isolation of AaeUPO in M. oryzae, we fused a Magnaporthe signal peptide for protein secretion and set it under control of the strong EF1-promotor. The success of the heterologous production of full-length AaeUPO in M. oryzae and the secretion of the functional enzyme was confirmed by a peroxygenase-specific enzyme assay. These results offer the possibility to establish the filamentous ascomycete M. oryzae as a broad applicable alternative expression system. This is in particular valid for proteins that cannot or not in sufficient yields produced in established systems.

Peer review status:IN REVISION

08 Jul 2021Submitted to MicrobiologyOpen
09 Jul 2021Assigned to Editor
09 Jul 2021Submission Checks Completed
15 Jul 2021Reviewer(s) Assigned
21 Jul 2021Review(s) Completed, Editorial Evaluation Pending
22 Jul 2021Editorial Decision: Revise Major
23 Jul 20211st Revision Received