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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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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. |
format | Online Article Text |
id | pubmed-9223840 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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