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Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres
A methodology that programs eukaryotic or bacterial cells to encapsulate proteins of any kind inside micro/nanospheres formed by muNS-Mi viral protein was developed in our laboratory. In the present study such “in cellulo” encapsulation technology is utilized for immobilizing a protein with an enzym...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7854631/ https://www.ncbi.nlm.nih.gov/pubmed/33531567 http://dx.doi.org/10.1038/s41598-021-82468-x |
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author | Pose-Boirazian, Tomás Eibes, Gemma Barreiro-Piñeiro, Natalia Díaz-Jullien, Cristina Lema, Juan M. Martínez-Costas, Jose |
author_facet | Pose-Boirazian, Tomás Eibes, Gemma Barreiro-Piñeiro, Natalia Díaz-Jullien, Cristina Lema, Juan M. Martínez-Costas, Jose |
author_sort | Pose-Boirazian, Tomás |
collection | PubMed |
description | A methodology that programs eukaryotic or bacterial cells to encapsulate proteins of any kind inside micro/nanospheres formed by muNS-Mi viral protein was developed in our laboratory. In the present study such “in cellulo” encapsulation technology is utilized for immobilizing a protein with an enzymatic activity of industrial interest, CotA laccase. The encapsulation facilitates its purification, resulting in a cost-effective, one-step way of producing immobilized enzymes for industrial use. In addition to the ability to be recycled without activity loss, the encapsulated protein showed an increased pH working range and high resistance to chemical inactivation. Also, its activity was almost unaffected after 30 min incubation at 90 °C and 15 min at the almost-boiling temperature of 95 °C. Furthermore, the encapsulated laccase was able to efficiently decolorate the recalcitrant dye RB19 at room temperature. |
format | Online Article Text |
id | pubmed-7854631 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-78546312021-02-03 Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres Pose-Boirazian, Tomás Eibes, Gemma Barreiro-Piñeiro, Natalia Díaz-Jullien, Cristina Lema, Juan M. Martínez-Costas, Jose Sci Rep Article A methodology that programs eukaryotic or bacterial cells to encapsulate proteins of any kind inside micro/nanospheres formed by muNS-Mi viral protein was developed in our laboratory. In the present study such “in cellulo” encapsulation technology is utilized for immobilizing a protein with an enzymatic activity of industrial interest, CotA laccase. The encapsulation facilitates its purification, resulting in a cost-effective, one-step way of producing immobilized enzymes for industrial use. In addition to the ability to be recycled without activity loss, the encapsulated protein showed an increased pH working range and high resistance to chemical inactivation. Also, its activity was almost unaffected after 30 min incubation at 90 °C and 15 min at the almost-boiling temperature of 95 °C. Furthermore, the encapsulated laccase was able to efficiently decolorate the recalcitrant dye RB19 at room temperature. Nature Publishing Group UK 2021-02-02 /pmc/articles/PMC7854631/ /pubmed/33531567 http://dx.doi.org/10.1038/s41598-021-82468-x Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Pose-Boirazian, Tomás Eibes, Gemma Barreiro-Piñeiro, Natalia Díaz-Jullien, Cristina Lema, Juan M. Martínez-Costas, Jose Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres |
title | Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres |
title_full | Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres |
title_fullStr | Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres |
title_full_unstemmed | Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres |
title_short | Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres |
title_sort | chemical and thermal stabilization of cota laccase via a novel one-step expression and immobilization in muns-mi nanospheres |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7854631/ https://www.ncbi.nlm.nih.gov/pubmed/33531567 http://dx.doi.org/10.1038/s41598-021-82468-x |
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