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RevistaCatalysts
Año2019
Volumen9
Páginas657
Internacional

Combi-CLEAs of glucose oxidase and catalase for conversion of glucose to gluconic acid eliminating the hydrogen peroxide to maintain enzyme activity in a bubble column reactor

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Agnes Cristina Oliveira Mafra1‡, Letícia Gazzotto Ulrich2, Jakub F. Kornecki3, Roberto Fernandez-Lafuente3*, Paulo Waldir Tardioli1,2* and Marcelo Perencin de Arruda Ribeiro1,2*
1     Programa de Pós-Graduação em Engenharia Química, Universidade Federal de São Carlos, Rodovia Washington Luís, km 235, 13565-905, São Carlos, SP, Brazil; agnescmafra@gmail.com (A. C. O. Mafra); pwtardioli@ufscar.br (P. W. Tardioli); marceloribeiro@ufscar.br (M. P. A. Ribeiro).
2     Departamento de Engenharia Química,  Universidade Federal de São Carlos, Rodovia Washington Luís, km 235, 13565-905, São Carlos, SP, Brazil; leticiagulrich@gmail.com (L. G. Ulrich).
3     Department of Biocatalysis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, ZC 28049, Madrid, Spain; yakokornecki@hotmail.es (J. F. Kornecki); rfl@icp.csic.es (R. Fernandez-Lafuente).
*   Corresponding authors: pwtardioli@ufscar.br, Tel. +55 16 33519362 (Paulo W. Tardioli); marceloribeiro@ufscar.br, Tel: +55 16 33066434 (Marcelo P. A. Ribeiro); rfl@icp.csic.es, Tel: +34 915854804 (Roberto Fernandez-Lafuente).
‡     Current address: Instituto de Educação, Agricultura e Ambiente, Universidade Federal do Amazonas, Campus Vale do Rio Madeira, Rua Vinte e Nove de Agosto, 786, 69800-000 Humaitá, AM, Brazil.



Abstract: In this work, combined cross-linked aggregates of catalase from bovine liver and glucose-oxidase from Aspergillus niger were prepared, evaluating the effect of the precipitant and crosslinking agents, as well as the use of bovine serum albumin (BSA) as feeder protein on enzyme immobilization yield and thermal stability of both enzymes. Combi-CLEAs prepared using dimethoxyethane as precipitant, 25 mM glutaraldehyde and BSA/enzymes mass ratio of 5.45 (w/w) gave the highest enzymes activities and stabilities at 40 °C, pH 6.0, and 250 rpm for 5 h. The stability of both immobilized enzymes was fairly similar, eliminating one of the problems of enzyme coimmobilization. Combi-CLEAs were used in gluconic acid (GA) production in a bubble column reactor operated at 40 °C, pH 6.0 and 10 vvm of aeration, using 26 g L-1 glucose as substrate. Results showed conversion of around 96% and a reaction course very similar to the same process using free enzymes. The operational half-life was 34 h, determined from kinetic profiles and first order inactivation model. Combi-CLEAs of glucose-oxidase and catalase showed to be a robust biocatalyst for applications in the production of gluconic acid from glucose.

Palabras clave:Glucose-oxidase, catalase, combi-CLEAs, gluconic acid, pneumatic reactor
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