Details
| Original language | English |
|---|---|
| Article number | e202300613 |
| Journal | CHEMSUSCHEM |
| Volume | 16 |
| Issue number | 23 |
| Publication status | Published - 7 Dec 2023 |
Abstract
Unspecific peroxygenases have attracted interest in synthetic chemistry, especially for the oxidative activation of C−H bonds, as they only require hydrogen peroxide (H2O2) instead of a cofactor. Due to their instability in even small amounts of H2O2, different strategies like enzyme immobilization or in situ H2O2 production have been developed to improve the stability of these enzymes. While most strategies have been studied separately, a combination of photocatalysis with immobilized enzymes was only recently reported. To show the advantages and limiting factors of immobilized enzyme in a photobiocatalytic reaction, a comparison is made between free and immobilized enzymes. Adjustment of critical parameters such as (i) enzyme and substrate concentration, (ii) illumination wavelength and (iii) light intensity results in significantly increased enzyme stabilities of the immobilized variant. Moreover, under optimized conditions a turnover number of 334,500 was reached.
Keywords
- biocatalysis, g-CN, immobilized enzyme, peroxygenases, photocatalysis, g-C N
ASJC Scopus subject areas
- Energy(all)
- General Energy
- Chemical Engineering(all)
- General Chemical Engineering
- Materials Science(all)
- General Materials Science
- Environmental Science(all)
- Environmental Chemistry
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In: CHEMSUSCHEM, Vol. 16, No. 23, e202300613, 07.12.2023.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Robust Light Driven Enzymatic Oxyfunctionalization via Immobilization of Unspecific Peroxygenase
AU - De Santis, Piera
AU - Wegstein, Deborah
AU - Burek, Bastien O.
AU - Patzsch, Jacqueline
AU - Alcalde, Miguel
AU - Kroutil, Wolfgang
AU - Bloh, Jonathan Z.
AU - Kara, Selin
N1 - Funding Information: f . S.K. acknowledges Independent Research Fund Denmark (PHOTOX‐ project, grant No 9063‐00031B) for the grant funding in the framework of Sapere Aude DFF Starting Grant. This project has received funding from the European Union's Horizon 2020 research and innovation program under the Marie Skłodowska‐Curie grant agreement No 764920. Deutsche Forschungsgemeinschaft (DFG) under funding code BL 1425/1‐2 is gratefully acknowledged
PY - 2023/12/7
Y1 - 2023/12/7
N2 - Unspecific peroxygenases have attracted interest in synthetic chemistry, especially for the oxidative activation of C−H bonds, as they only require hydrogen peroxide (H2O2) instead of a cofactor. Due to their instability in even small amounts of H2O2, different strategies like enzyme immobilization or in situ H2O2 production have been developed to improve the stability of these enzymes. While most strategies have been studied separately, a combination of photocatalysis with immobilized enzymes was only recently reported. To show the advantages and limiting factors of immobilized enzyme in a photobiocatalytic reaction, a comparison is made between free and immobilized enzymes. Adjustment of critical parameters such as (i) enzyme and substrate concentration, (ii) illumination wavelength and (iii) light intensity results in significantly increased enzyme stabilities of the immobilized variant. Moreover, under optimized conditions a turnover number of 334,500 was reached.
AB - Unspecific peroxygenases have attracted interest in synthetic chemistry, especially for the oxidative activation of C−H bonds, as they only require hydrogen peroxide (H2O2) instead of a cofactor. Due to their instability in even small amounts of H2O2, different strategies like enzyme immobilization or in situ H2O2 production have been developed to improve the stability of these enzymes. While most strategies have been studied separately, a combination of photocatalysis with immobilized enzymes was only recently reported. To show the advantages and limiting factors of immobilized enzyme in a photobiocatalytic reaction, a comparison is made between free and immobilized enzymes. Adjustment of critical parameters such as (i) enzyme and substrate concentration, (ii) illumination wavelength and (iii) light intensity results in significantly increased enzyme stabilities of the immobilized variant. Moreover, under optimized conditions a turnover number of 334,500 was reached.
KW - biocatalysis
KW - g-CN
KW - immobilized enzyme
KW - peroxygenases
KW - photocatalysis
KW - g-C N
UR - http://www.scopus.com/inward/record.url?scp=85168128710&partnerID=8YFLogxK
U2 - 10.1002/cssc.202300613
DO - 10.1002/cssc.202300613
M3 - Article
VL - 16
JO - CHEMSUSCHEM
JF - CHEMSUSCHEM
SN - 1864-5631
IS - 23
M1 - e202300613
ER -