Details
| Original language | English |
|---|---|
| Article number | 985997 |
| Journal | Frontiers in Chemistry |
| Volume | 10 |
| Publication status | Published - 30 Aug 2022 |
Abstract
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.
Keywords
- biocatalysis, enzyme stability, immobilization techniques, process intensification, unspecific peroxygenase
ASJC Scopus subject areas
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In: Frontiers in Chemistry, Vol. 10, 985997, 30.08.2022.
Research output: Contribution to journal › Article › Research › peer review
}
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 -