Open AccessMagnaporthe oryzae as an expression host for the production of the unspecific peroxygenase Aae UPO from the basidiomycete Agrocybe aegerita
Author(s) -
Jacob Stefan,
Bormann Sebastian,
Becker Michael,
Antelo Luis,
Holtmann Dirk,
Thines Eckhard
Publication year - 2021
Publication title -
microbiologyopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.881
H-Index - 36
ISSN - 2045-8827
DOI - 10.1002/mbo3.1229
Subject(s) - heterologous , heterologous expression , aspergillus oryzae , biology , yeast , secretion , enzyme , fungus , microbiology and biotechnology , biochemistry , gene , recombinant dna , botany
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 ( Aae UPO). Note, UPOs are attractive biocatalysts for selective oxyfunctionalization of non‐activated carbon‐hydrogen bonds. To improve and simplify the isolation of Aae UPO 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 Aae UPO 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.