Promiscuous fungal peroxygenase from Chaetomium globosum by directed evolution

Fungal unspecific peroxygenases (UPOs) are appealing enzymes for C–H oxyfunctionalization reactions, and, among them, the short UPO type from Chaetomium globosum ( Cgl UPO) is of special interest due to its diverse substrate scope and selectivity. Despite its significance, Cgl UPO shows low stability and poor heterologous expression which has hitherto impeded its use for practical applications. In this study, Cgl UPO was engineered by directed evolution to produce a highly active and stable secreted variant that performs selective oxidations on a panel of organic molecules, including ethylbenzene, styrene, 1,2,3,4-tetrahydronaphthalene (THN), isophorone, pinene, and limonene. Molecular dynamic simulations demonstrate how mutations F154L and M210V in the heme access channel are responsible for dramatic changes in the enzyme performance, including inverted enantioselectivities and anti-Markovnikov oxidation reactions.

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Publication Details

Journal
iScience
Published
2026-09-18
DOI
https://doi.org/10.1016/j.isci.2026.117534
Primary Topic
Enzyme-mediated dye degradation
Type
article
Field-Weighted Citation Impact
0.00

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article

Promiscuous fungal peroxygenase from Chaetomium globosum by directed evolution

Vicent Moliner, Morgane Valles, Patricia Gómez de Santos, David González-Pérez et al.
iScience
Enzyme-mediated dye degradation
article

Promiscuous fungal peroxygenase from Chaetomium globosum by directed evolution

Vicent Moliner, Morgane Valles, Patricia Gómez de Santos, David González-Pérez, David M. Upp, Martin Hofrichter, Daniel Méndez‐Sánchez, Israel Sánchez‐Moreno, Ivan Mateljak, Katrin Scheibner, Miguel Alcalde, Katarzyna Świderek
article en

Abstract

Fungal unspecific peroxygenases (UPOs) are appealing enzymes for C–H oxyfunctionalization reactions, and, among them, the short UPO type from Chaetomium globosum ( Cgl UPO) is of special interest due to its diverse substrate scope and selectivity. Despite its significance, Cgl UPO shows low stability and poor heterologous expression which has hitherto impeded its use for practical applications. In this study, Cgl UPO was engineered by directed evolution to produce a highly active and stable secreted variant that performs selective oxidations on a panel of organic molecules, including ethylbenzene, styrene, 1,2,3,4-tetrahydronaphthalene (THN), isophorone, pinene, and limonene. Molecular dynamic simulations demonstrate how mutations F154L and M210V in the heme access channel are responsible for dramatic changes in the enzyme performance, including inverted enantioselectivities and anti-Markovnikov oxidation reactions.

iScienceVol. 29(10)
Universitat Jaume I (ES), Instituto de Catálisis y Petroleoquímica (ES), Unidades Centrales Científico-Técnicas (ES), Jena Bioscience (Germany) (DE), International University Institute (IHI) Zittau (DE), Instituto de Química Orgánica General (ES)
Comunidad de Madrid, Ministerio de Ciencia, Innovación y Universidades
Openalex Percentile: Top 13%
Enzyme-mediated dye degradation
DOIOpen Access PDFOpenAlex
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