TY - JOUR

T1 - A holistic carrier-bound immobilization approach for unspecific peroxygenase

AU - De Santis, Piera

AU - Petrovai, Noémi

AU - Meyer, Lars-Erik

AU - Hobisch, Markus

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 Skłodowska-Curie grant agreement No 764920. SK gratefully acknowledges the Independent Research Fund Denmark (PHOTOX-f project, grant No 9063-00031B) for the grant funding in the framework of Sapere Aude DFF-Starting Grant.

PY - 2022/8/30

Y1 - 2022/8/30

N2 - Unspecific peroxygenases (UPOs) are among the most studied enzymes in the last decade and their well-deserved fame owes to the enzyme’s ability of catalyzing the regio- and stereospecific hydroxylation of non-activated C–H bonds at the only expense of H2O2. This leads to more direct routes for the synthesis of different chiral compounds as well as to easier oxyfunctionalization of complex molecules. Unfortunately, due to the high sensitivity towards the process conditions, UPOs’ application at industrial level has been hampered until now. However, this challenge can be overcome by enzyme immobilization, a valid strategy that has been proven to give several benefits. Within this article, we present three different immobilization procedures suitable for UPOs and two of them led to very promising results. The immobilized enzyme, indeed, shows longer stability and increased robustness to reaction conditions. The immobilized enzyme half-life time is 15-fold higher than for the free AaeUPO PaDa-I and no enzyme deactivation occurred when incubated in organic media for 120 h. Moreover, AaeUPO PaDa-I is proved to be recycled and reused up to 7 times when immobilized.

AB - Unspecific peroxygenases (UPOs) are among the most studied enzymes in the last decade and their well-deserved fame owes to the enzyme’s ability of catalyzing the regio- and stereospecific hydroxylation of non-activated C–H bonds at the only expense of H2O2. This leads to more direct routes for the synthesis of different chiral compounds as well as to easier oxyfunctionalization of complex molecules. Unfortunately, due to the high sensitivity towards the process conditions, UPOs’ application at industrial level has been hampered until now. However, this challenge can be overcome by enzyme immobilization, a valid strategy that has been proven to give several benefits. Within this article, we present three different immobilization procedures suitable for UPOs and two of them led to very promising results. The immobilized enzyme, indeed, shows longer stability and increased robustness to reaction conditions. The immobilized enzyme half-life time is 15-fold higher than for the free AaeUPO PaDa-I and no enzyme deactivation occurred when incubated in organic media for 120 h. Moreover, AaeUPO PaDa-I is proved to be recycled and reused up to 7 times when immobilized.

KW - biocatalysis

KW - enzyme stability

KW - immobilization techniques

KW - process intensification

KW - unspecific peroxygenase

UR - http://www.scopus.com/inward/record.url?scp=85138239298&partnerID=8YFLogxK

U2 - 10.3389/fchem.2022.985997

DO - 10.3389/fchem.2022.985997

M3 - Article

C2 - 36110138

AN - SCOPUS:85138239298

VL - 10

JO - Frontiers in Chemistry

JF - Frontiers in Chemistry

SN - 2296-2646

M1 - 985997

ER -