학술논문
Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres.
Document Type
Academic Journal
Author
Pose-Boirazian T; Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CiQUS), Departamento de Bioquímica y Biología Molecular, Universidade de Santiago de Compostela, 15782, Santiago de Compostela, Spain.; Eibes G; CRETUS Institute, Dept. of Chemical Engineering, Universidade de Santiago de Compostela, 15782, Santiago de Compostela, Spain.; Barreiro-Piñeiro N; Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CiQUS), Departamento de Bioquímica y Biología Molecular, Universidade de Santiago de Compostela, 15782, Santiago de Compostela, Spain.; Díaz-Jullien C; Centro de Investigación en Bioloxía (CiBUS), Departamento de Bioquímica y Biología Molecular, Universidade de Santiago de Compostela, 15782, Santiago de Compostela, Spain.; Lema JM; CRETUS Institute, Dept. of Chemical Engineering, Universidade de Santiago de Compostela, 15782, Santiago de Compostela, Spain.; Martínez-Costas J; Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CiQUS), Departamento de Bioquímica y Biología Molecular, Universidade de Santiago de Compostela, 15782, Santiago de Compostela, Spain. jose.martinez.costas@usc.es.
Source
Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: PubMed not MEDLINE; MEDLINE
Subject
Language
English
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.