Magnaporthe oryzae as an expression host for the production of the unspecific peroxygenase AaeUPO from the basidiomycete Agrocybe aegerita

We establishedM. 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 inM. oryzae, we fused aMagnaporthe signal peptide for protein secretion and set it under control of the strong EF1 α-promoter. AbstractThe filamentous fungusMagnaporthe 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 establishedM. oryzae as a host for the expression of the unspecific peroxygenase from the basidiomyceteAgrocybe aegerita (AaeUPO). Note, UPOs are attractive biocatalysts for selective oxyfunctionalization of non-activated carbon-hydrogen bonds. To improve and simplify the isolation ofAaeUPO inM. oryzae, we fused aMagnaporthe signal peptide for protein secretion and set it under control of the strong EF1 α-promoter. The success of the heterologous production of full-lengthAaeUPO inM. 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 ascomyceteM. oryzae as a broad applicable alternative expression system.

Source: MicrobiologyOpen - December 3, 2021 Category: Microbiology Authors: Stefan Jacob, Sebastian Bormann, Michael Becker, Luis Antelo, Dirk Holtmann, Eckhard Thines Tags: COMMENTARY Source Type: research