Magnaporthe oryzae as an expression host for the production of the unspecific peroxygenase AaeUPO from the basidiomycete Agrocybe aegerita
| Autor: | Luis Antelo, Sebastian Bormann, Eckhard Thines, Dirk Holtmann, Stefan Jacob, Michael Becker |
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| Přispěvatelé: | Publica |
| Rok vydání: | 2021 |
| Předmět: |
biology
Agrocybe Host (biology) Eukaryotic Initiation Factor-1 heterologous expression food and beverages Magnaporthe oryzae Protein Sorting Signals biology.organism_classification Microbiology QR1-502 Recombinant Proteins Mixed Function Oxygenases AaeUPO oxyfunctionalization Fungal Proteins Magnaporthe unspecific peroxygenases Unspecific peroxygenase Commentary Heterologous expression Promoter Regions Genetic |
| Zdroj: | MicrobiologyOpen, Vol 10, Iss 6, Pp n/a-n/a (2021) MicrobiologyOpen |
| ISSN: | 2045-8827 |
| Popis: | 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). Note, 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 EF1α‐promoter. 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. 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 EF1α‐promoter. |
| Databáze: | OpenAIRE |
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