Details
Original language | English |
---|---|
Article number | 107615 |
Journal | Biotechnology advances |
Volume | 51 |
Early online date | 19 Aug 2020 |
Publication status | Published - 1 Nov 2021 |
Externally published | Yes |
Abstract
Peroxygenases are an emerging new class of enzymes allowing selective oxyfunctionalisation reactions in a cofactor-independent way different from well-known P450 monooxygenases. Herein, we focused on recent developments from organic synthesis, molecular biotechnology and reaction engineering viewpoints that are devoted to bring these enzymes in industrial applications. This covers natural diversity from different sources, protein engineering strategies for expression, substrate scope, activity and selectivity, stabilisation of enzymes via immobilisation, and the use of peroxygenases in low water media. We believe that peroxygenases have much to offer for selective oxyfunctionalisations and we have much to study to explore the full potential of these versatile biocatalysts in organic synthesis.
Keywords
- Fungal enzyme, Oxidation chemistry, Oxyfunctionalisation, Oxygenase, Peroxygenase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Biotechnology advances, Vol. 51, 107615, 01.11.2021.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - Recent developments in the use of peroxygenases – Exploring their high potential in selective oxyfunctionalisations
AU - Hobisch, Markus
AU - Holtmann, Dirk
AU - Gomez de Santos, Patricia
AU - Alcalde, Miguel
AU - Hollmann, Frank
AU - Kara, Selin
N1 - Funding Information: This project has received funding from the European Union's Horizon 2020 research and innovation program under the Marie Sk?odowska-Curie grant agreement No 764920. MA and PGS thank the FPI fellowship BES-2017-080040, the Spanish Government Project PID2019-106166RB-I00-Oxywave, and the Comunidad de Madrid Synergy CAM project Y2018/BIO-4738-EVOCHIMERA-CM. FH gratefully acknowledges support by The Netherlands Organisation for Scientific Research through a VICI grant (no. 724.014.003) and the European Research Commission (ERC consolidator grant No 648026).
PY - 2021/11/1
Y1 - 2021/11/1
N2 - Peroxygenases are an emerging new class of enzymes allowing selective oxyfunctionalisation reactions in a cofactor-independent way different from well-known P450 monooxygenases. Herein, we focused on recent developments from organic synthesis, molecular biotechnology and reaction engineering viewpoints that are devoted to bring these enzymes in industrial applications. This covers natural diversity from different sources, protein engineering strategies for expression, substrate scope, activity and selectivity, stabilisation of enzymes via immobilisation, and the use of peroxygenases in low water media. We believe that peroxygenases have much to offer for selective oxyfunctionalisations and we have much to study to explore the full potential of these versatile biocatalysts in organic synthesis.
AB - Peroxygenases are an emerging new class of enzymes allowing selective oxyfunctionalisation reactions in a cofactor-independent way different from well-known P450 monooxygenases. Herein, we focused on recent developments from organic synthesis, molecular biotechnology and reaction engineering viewpoints that are devoted to bring these enzymes in industrial applications. This covers natural diversity from different sources, protein engineering strategies for expression, substrate scope, activity and selectivity, stabilisation of enzymes via immobilisation, and the use of peroxygenases in low water media. We believe that peroxygenases have much to offer for selective oxyfunctionalisations and we have much to study to explore the full potential of these versatile biocatalysts in organic synthesis.
KW - Fungal enzyme
KW - Oxidation chemistry
KW - Oxyfunctionalisation
KW - Oxygenase
KW - Peroxygenase
UR - http://www.scopus.com/inward/record.url?scp=85089826545&partnerID=8YFLogxK
U2 - 10.1016/j.biotechadv.2020.107615
DO - 10.1016/j.biotechadv.2020.107615
M3 - Review article
C2 - 32827669
AN - SCOPUS:85089826545
VL - 51
JO - Biotechnology advances
JF - Biotechnology advances
SN - 0734-9750
M1 - 107615
ER -