Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3

The use of monoamine oxidases (MAOs) in amine oxidation is a great example of how biocatalysis can be applied in the agricultural or pharmaceutical industry and manufacturing of fine chemicals to make a shift from traditional chemical synthesis towards more sustainable green chemistry. This article...

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Published in:Molecules
Main Authors: Iga Jodłowska, Aleksandra Twarda-Clapa, Kamil Szymczak, Aneta M. Białkowska
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2021
Subjects:
Online Access:https://doi.org/10.3390/molecules26206237
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spelling ftmdpi:oai:mdpi.com:/1420-3049/26/20/6237/ 2023-08-20T04:01:07+02:00 Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3 Iga Jodłowska Aleksandra Twarda-Clapa Kamil Szymczak Aneta M. Białkowska agris 2021-10-15 application/pdf https://doi.org/10.3390/molecules26206237 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/molecules26206237 https://creativecommons.org/licenses/by/4.0/ Molecules; Volume 26; Issue 20; Pages: 6237 psychrophilic fungi monoamine oxidase oxidative deamination Text 2021 ftmdpi https://doi.org/10.3390/molecules26206237 2023-08-01T02:58:11Z The use of monoamine oxidases (MAOs) in amine oxidation is a great example of how biocatalysis can be applied in the agricultural or pharmaceutical industry and manufacturing of fine chemicals to make a shift from traditional chemical synthesis towards more sustainable green chemistry. This article reports the screening of fourteen Antarctic fungi strains for MAO activity and the discovery of a novel psychrozyme MAOP3 isolated from the Pseudogymnoascus sp. P3. The activity of the native enzyme was 1350 ± 10.5 U/L towards a primary (n-butylamine) amine, and 1470 ± 10.6 U/L towards a secondary (6,6-dimethyl-3-azabicyclohexane) amine. MAO P3 has the potential for applications in biotransformations due to its wide substrate specificity (aliphatic and cyclic amines, pyrrolidine derivatives). The psychrozyme operates at an optimal temperature of 30 °C, retains 75% of activity at 20 °C, and is rather thermolabile, which is beneficial for a reduction in the overall costs of a bioprocess and offers a convenient way of heat inactivation. The reported biocatalyst is the first psychrophilic MAO; its unique biochemical properties, substrate specificity, and effectiveness predispose MAO P3 for use in environmentally friendly, low-emission biotransformations. Text Antarc* Antarctic MDPI Open Access Publishing Antarctic Molecules 26 20 6237
institution Open Polar
collection MDPI Open Access Publishing
op_collection_id ftmdpi
language English
topic psychrophilic fungi
monoamine oxidase
oxidative deamination
spellingShingle psychrophilic fungi
monoamine oxidase
oxidative deamination
Iga Jodłowska
Aleksandra Twarda-Clapa
Kamil Szymczak
Aneta M. Białkowska
Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3
topic_facet psychrophilic fungi
monoamine oxidase
oxidative deamination
description The use of monoamine oxidases (MAOs) in amine oxidation is a great example of how biocatalysis can be applied in the agricultural or pharmaceutical industry and manufacturing of fine chemicals to make a shift from traditional chemical synthesis towards more sustainable green chemistry. This article reports the screening of fourteen Antarctic fungi strains for MAO activity and the discovery of a novel psychrozyme MAOP3 isolated from the Pseudogymnoascus sp. P3. The activity of the native enzyme was 1350 ± 10.5 U/L towards a primary (n-butylamine) amine, and 1470 ± 10.6 U/L towards a secondary (6,6-dimethyl-3-azabicyclohexane) amine. MAO P3 has the potential for applications in biotransformations due to its wide substrate specificity (aliphatic and cyclic amines, pyrrolidine derivatives). The psychrozyme operates at an optimal temperature of 30 °C, retains 75% of activity at 20 °C, and is rather thermolabile, which is beneficial for a reduction in the overall costs of a bioprocess and offers a convenient way of heat inactivation. The reported biocatalyst is the first psychrophilic MAO; its unique biochemical properties, substrate specificity, and effectiveness predispose MAO P3 for use in environmentally friendly, low-emission biotransformations.
format Text
author Iga Jodłowska
Aleksandra Twarda-Clapa
Kamil Szymczak
Aneta M. Białkowska
author_facet Iga Jodłowska
Aleksandra Twarda-Clapa
Kamil Szymczak
Aneta M. Białkowska
author_sort Iga Jodłowska
title Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3
title_short Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3
title_full Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3
title_fullStr Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3
title_full_unstemmed Green Oxidation of Amines by a Novel Cold-Adapted Monoamine Oxidase MAO P3 from Psychrophilic Fungi Pseudogymnoascus sp. P3
title_sort green oxidation of amines by a novel cold-adapted monoamine oxidase mao p3 from psychrophilic fungi pseudogymnoascus sp. p3
publisher Multidisciplinary Digital Publishing Institute
publishDate 2021
url https://doi.org/10.3390/molecules26206237
op_coverage agris
geographic Antarctic
geographic_facet Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_source Molecules; Volume 26; Issue 20; Pages: 6237
op_relation https://dx.doi.org/10.3390/molecules26206237
op_rights https://creativecommons.org/licenses/by/4.0/
op_doi https://doi.org/10.3390/molecules26206237
container_title Molecules
container_volume 26
container_issue 20
container_start_page 6237
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