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 -