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Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations
BACKGROUND: Physiological aggregation of a recombinant enzyme into enzymatically active inclusion bodies could be an excellent strategy to obtain immobilized enzymes for industrial biotransformation processes. However, it is not convenient to recycle “gelatinous masses” of protein inclusion bodies f...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6122667/ https://www.ncbi.nlm.nih.gov/pubmed/30176877 http://dx.doi.org/10.1186/s12934-018-0987-7 |
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author | Koszagova, Romana Krajcovic, Tomas Palencarova-Talafova, Klaudia Patoprsty, Vladimir Vikartovska, Alica Pospiskova, Kristyna Safarik, Ivo Nahalka, Jozef |
author_facet | Koszagova, Romana Krajcovic, Tomas Palencarova-Talafova, Klaudia Patoprsty, Vladimir Vikartovska, Alica Pospiskova, Kristyna Safarik, Ivo Nahalka, Jozef |
author_sort | Koszagova, Romana |
collection | PubMed |
description | BACKGROUND: Physiological aggregation of a recombinant enzyme into enzymatically active inclusion bodies could be an excellent strategy to obtain immobilized enzymes for industrial biotransformation processes. However, it is not convenient to recycle “gelatinous masses” of protein inclusion bodies from one reaction cycle to another, as high centrifugation forces are needed in large volumes. The magnetization of inclusion bodies is a smart solution for large-scale applications, enabling an easier separation process using a magnetic field. RESULTS: Magnetically modified inclusion bodies of UDP–glucose pyrophosphorylase were recycled 50 times, in comparison, inclusion bodies of the same enzyme were inactivated during ten reaction cycles if they were recycled by centrifugation. Inclusion bodies of sialic acid aldolase also showed good performance and operational stability after the magnetization procedure. CONCLUSIONS: It is demonstrated here that inclusion bodies can be easily magnetically modified by magnetic iron oxide particles prepared by microwave-assisted synthesis from ferrous sulphate. The magnetic particles stabilize the repetitive use of the inclusion bodies [Image: see text]. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12934-018-0987-7) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6122667 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-61226672018-09-10 Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations Koszagova, Romana Krajcovic, Tomas Palencarova-Talafova, Klaudia Patoprsty, Vladimir Vikartovska, Alica Pospiskova, Kristyna Safarik, Ivo Nahalka, Jozef Microb Cell Fact Research BACKGROUND: Physiological aggregation of a recombinant enzyme into enzymatically active inclusion bodies could be an excellent strategy to obtain immobilized enzymes for industrial biotransformation processes. However, it is not convenient to recycle “gelatinous masses” of protein inclusion bodies from one reaction cycle to another, as high centrifugation forces are needed in large volumes. The magnetization of inclusion bodies is a smart solution for large-scale applications, enabling an easier separation process using a magnetic field. RESULTS: Magnetically modified inclusion bodies of UDP–glucose pyrophosphorylase were recycled 50 times, in comparison, inclusion bodies of the same enzyme were inactivated during ten reaction cycles if they were recycled by centrifugation. Inclusion bodies of sialic acid aldolase also showed good performance and operational stability after the magnetization procedure. CONCLUSIONS: It is demonstrated here that inclusion bodies can be easily magnetically modified by magnetic iron oxide particles prepared by microwave-assisted synthesis from ferrous sulphate. The magnetic particles stabilize the repetitive use of the inclusion bodies [Image: see text]. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12934-018-0987-7) contains supplementary material, which is available to authorized users. BioMed Central 2018-09-03 /pmc/articles/PMC6122667/ /pubmed/30176877 http://dx.doi.org/10.1186/s12934-018-0987-7 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Koszagova, Romana Krajcovic, Tomas Palencarova-Talafova, Klaudia Patoprsty, Vladimir Vikartovska, Alica Pospiskova, Kristyna Safarik, Ivo Nahalka, Jozef Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations |
title | Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations |
title_full | Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations |
title_fullStr | Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations |
title_full_unstemmed | Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations |
title_short | Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations |
title_sort | magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6122667/ https://www.ncbi.nlm.nih.gov/pubmed/30176877 http://dx.doi.org/10.1186/s12934-018-0987-7 |
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