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Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications

Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxid...

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Autores principales: Di Fabio, Elisa, Iazzetti, Antonia, Incocciati, Alessio, Caseli, Valentina, Fabrizi, Giancarlo, Boffi, Alberto, Bonamore, Alessandra, Macone, Alberto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9223840/
https://www.ncbi.nlm.nih.gov/pubmed/35742969
http://dx.doi.org/10.3390/ijms23126529
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author Di Fabio, Elisa
Iazzetti, Antonia
Incocciati, Alessio
Caseli, Valentina
Fabrizi, Giancarlo
Boffi, Alberto
Bonamore, Alessandra
Macone, Alberto
author_facet Di Fabio, Elisa
Iazzetti, Antonia
Incocciati, Alessio
Caseli, Valentina
Fabrizi, Giancarlo
Boffi, Alberto
Bonamore, Alessandra
Macone, Alberto
author_sort Di Fabio, Elisa
collection PubMed
description Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme’s performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid.
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spelling pubmed-92238402022-06-24 Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications Di Fabio, Elisa Iazzetti, Antonia Incocciati, Alessio Caseli, Valentina Fabrizi, Giancarlo Boffi, Alberto Bonamore, Alessandra Macone, Alberto Int J Mol Sci Article Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme’s performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid. MDPI 2022-06-10 /pmc/articles/PMC9223840/ /pubmed/35742969 http://dx.doi.org/10.3390/ijms23126529 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Di Fabio, Elisa
Iazzetti, Antonia
Incocciati, Alessio
Caseli, Valentina
Fabrizi, Giancarlo
Boffi, Alberto
Bonamore, Alessandra
Macone, Alberto
Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
title Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
title_full Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
title_fullStr Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
title_full_unstemmed Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
title_short Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
title_sort immobilization of lathyrus cicera amine oxidase on magnetic microparticles for biocatalytic applications
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9223840/
https://www.ncbi.nlm.nih.gov/pubmed/35742969
http://dx.doi.org/10.3390/ijms23126529
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