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Synthesis and Characterization of Cross-Linked Aggregates of Peroxidase from Megathyrsus maximus (Guinea Grass) and Their Application for Indigo Carmine Decolorization.
Perez, Angie V; Gaitan-Oyola, Jorge A; Vargas-Delgadillo, Diana P; Castillo, John J; Barbosa, Oveimar; Fernandez-Lafuente, Roberto.
Afiliação
  • Perez AV; Grupo de Investigación en Materiales Porosos con Aplicaciones Ambientales y Tecnológicas, Departamento de Química, Universidad del Tolima, Ibagué 730006299, Colombia.
  • Gaitan-Oyola JA; Grupo de Investigación en Materiales Porosos con Aplicaciones Ambientales y Tecnológicas, Departamento de Química, Universidad del Tolima, Ibagué 730006299, Colombia.
  • Vargas-Delgadillo DP; Grupo de Investigación en Materiales Porosos con Aplicaciones Ambientales y Tecnológicas, Departamento de Química, Universidad del Tolima, Ibagué 730006299, Colombia.
  • Castillo JJ; Grupo de Investigación en Bioquímica y Microbiología, Escuela de Química, Universidad Industrial de Santander, Bucaramanga 680002, Colombia.
  • Barbosa O; Grupo de Investigación en Materiales Porosos con Aplicaciones Ambientales y Tecnológicas, Departamento de Química, Universidad del Tolima, Ibagué 730006299, Colombia.
  • Fernandez-Lafuente R; Departamento de Biocatálisis, ICP-CSIC, Campus Cantoblanco UAM-CSIC, C/Marie Curie 2, 28049 Madrid, Spain.
Molecules ; 29(11)2024 Jun 06.
Article em En | MEDLINE | ID: mdl-38893568
ABSTRACT
We present the synthesis of a cross-linking enzyme aggregate (CLEAS) of a peroxidase from Megathyrsus maximus (Guinea Grass) (GGP). The biocatalyst was produced using 50%v/v ethanol and 0.88%w/v glutaraldehyde for 1 h under stirring. The immobilization yield was 93.74% and the specific activity was 36.75 U mg-1. The biocatalyst surpassed by 61% the free enzyme activity at the optimal pH value (pH 6 for both preparations), becoming this increase in activity almost 10-fold at pH 9. GGP-CLEAS exhibited a higher thermal stability (2-4 folds) and was more stable towards hydrogen peroxide than the free enzyme (2-3 folds). GGP-CLEAS removes over 80% of 0.05 mM indigo carmine at pH 5, in the presence of 0.55 mM H2O2 after 60 min of reaction, a much higher value than when using the free enzyme. The operational stability showed a decrease of enzyme activity (over 60% in 4 cycles), very likely related to suicide inhibition.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peroxidase / Enzimas Imobilizadas / Peróxido de Hidrogênio / Índigo Carmim Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peroxidase / Enzimas Imobilizadas / Peróxido de Hidrogênio / Índigo Carmim Idioma: En Ano de publicação: 2024 Tipo de documento: Article