From characterization to biocatalytic application of two peroxygenases from Collariella virescens and Daldinia caldariorum

Peroxygenases are promising biocatalysts for selective oxyfunctionalization reactions including hydroxylation, epoxidation, and sulfoxidation. In this study, we explore the activity of two recently reported peroxygenases from Collariella virescens ( Cvi UPO) and Daldinia caldariorum ( Dca UPO) in a range of synthetically relevant transformations. Both enzymes were heterologously expressed in Escherichia coli and tested for various oxidative reactions. Dca UPO generally demonstrated higher activity compared to Cvi UPO across several substrates, showing significant conversions in alcohol and arene oxidations as well as enantioselective epoxidations of styrene derivatives. Notably, the enzymes exhibited complementary selectivities in several reactions including allylic hydroxylation and benzylic oxidation. These results broaden the substrate scope of Cvi UPO and Dca UPO and highlight their potential for industrial applications. However, challenges with enzyme expression in E. coli remain, necessitating future work on alternative expression systems such as Pichia pastoris to improve yields.