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Laboratory tests show unspecific peroxygenase mutants oxidize emerging contaminants in pharmaceuticals, suggesting new biocatalyst applications.
Unspecific peroxygenase (UPO) is versatile fungal enzyme that carries out with high efficiency a plethora of C-H oxyfunctionalizations of organic compounds, simply triggered by H₂O₂. With the goal of making UPO an industrial biocatalyst, it has been subjected over the years to different directed evolution campaigns focused on expression, stability, activity, and selectivity. In this work, we tested the ability of PaDa-I and JaWa, evolved variants of the UPO from Agrocybe aegerita, to catalyze the oxidation of a series of pharmaceutical compounds, considered emerging contaminants (EC), or microcontaminants. Remarkably, these UPO mutants were able to catalyze the oxidation of 9 out of 12 EC, albeit with different efficacy. A detailed analysis of the reaction efficiency and the nontoxic nature of the reaction products point these UPO mutants as promising tools for enzymatic bioremediation schemes.
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Torres‐Aguirre et al. (2026) studied this question.
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