Abstract

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.

Details

Title
Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres
Author
Pose-Boirazian Tomás 1 ; Eibes Gemma 2 ; Barreiro-Piñeiro, Natalia 1 ; Díaz-Jullien, Cristina 3 ; Lema, Juan M 2 ; Martínez-Costas, Jose 1 

 Universidade de Santiago de Compostela, Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CiQUS), Departamento de Bioquímica y Biología Molecular, Santiago de Compostela, Spain (GRID:grid.11794.3a) (ISNI:0000000109410645) 
 Universidade de Santiago de Compostela, CRETUS Institute, Dept. of Chemical Engineering, Santiago de Compostela, Spain (GRID:grid.11794.3a) (ISNI:0000000109410645) 
 Universidade de Santiago de Compostela, Centro de Investigación en Bioloxía (CiBUS), Departamento de Bioquímica y Biología Molecular, Santiago de Compostela, Spain (GRID:grid.11794.3a) (ISNI:0000000109410645) 
Publication year
2021
Publication date
2021
Publisher
Nature Publishing Group
e-ISSN
20452322
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2485325247
Copyright
© The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.