Print Email Facebook Twitter A novel unspecific peroxygenase from Agaricus bisporus var. bisporus for biocatalytic oxyfunctionalisation reactions Title A novel unspecific peroxygenase from Agaricus bisporus var. bisporus for biocatalytic oxyfunctionalisation reactions Author Li, Tiantian (South China University of Technology) Liang, Hongjing (South China University of Technology) Wu, Bin (South China University of Technology) Lan, Dongming (South China University of Technology) Ma, Yunjian (South China University of Technology) Hollmann, F. (TU Delft BT/Biocatalysis) Wang, Yonghua (South China University of Technology) Date 2023 Abstract Unspecific peroxygenases (UPOs) represent an emerging class of catalysts for the selective oxyfunctionalisation of C–H- and C = C groups. Until now, only a few UPOs have been characterised. In this study, we report a new peroxygenase identified from the Unspecific Peroxygenase Database. The UPO from Agaricus bisporus var. bisporus (AbvbUPO) has been heterologously expressed in Aspergillus niger and initially characterised with respect to its basic biochemical features. Furthermore, its catalytic properties were evaluated with enzymatic cascade reactions of choline oxidase (AnChOx) and AbvbUPO, which the AnChOx provided H2O2 necessary via reductive activation of oxygen in situ. Three types of oxyfunctionalizations, such as hydroxylation of ethylbenzene, epoxidations of styrene and cyclohexene, sulfoxidations of methyl phenyl sulfide and phenyl vinyl sulfide, were successfully achieved. We also investigated the activity of AbvbUPO on fatty acids in some more detail. The experimental results show that Under the above conditions, AbvbUPO had the higher activity for cyclohexene epoxidation and sulfonation of sulfide substrates. The concentration of epoxy cyclohexane was 2.91 mM, and the concentration of methyl phenyl sulfoxide was 3.69 mM. The regioselectivity of AbvbUPO was ω-1 bonds position of linear saturated fatty acid. All in all, AbvbUPO exhibits some interesting differences which may put the basis for further understanding of the factors determining peroxygenase selectivity. Subject Agaricus bisporus var. bisporusHeme-thiolate peroxidaseHeterologous expressionOxyfunctionalisationUnspecific peroxygenase To reference this document use: http://resolver.tudelft.nl/uuid:af4301b8-c203-41db-9b9c-04c1c4e85028 DOI https://doi.org/10.1016/j.mcat.2023.113275 ISSN 2468-8231 Source Molecular Catalysis, 546 Part of collection Institutional Repository Document type journal article Rights © 2023 Tiantian Li, Hongjing Liang, Bin Wu, Dongming Lan, Yunjian Ma, F. Hollmann, Yonghua Wang Files PDF 1_s2.0_S2468823123003590_main.pdf 5.68 MB Close viewer /islandora/object/uuid:af4301b8-c203-41db-9b9c-04c1c4e85028/datastream/OBJ/view