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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...

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Autores principales: Pose-Boirazian, Tomás, Eibes, Gemma, Barreiro-Piñeiro, Natalia, Díaz-Jullien, Cristina, Lema, Juan M., Martínez-Costas, Jose
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
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.
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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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