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Modeling and experimental validation of covalent immobilization of Trametes maxima laccase on glyoxyl and MANA-Sepharose CL 4B supports, for the use in bioconversion of residual colorants.
Cutiño-Avila, Bessy V; Sánchez-López, María I; Cárdenas-Moreno, Yosberto; González-Durruthy, Michael; Ramos-Leal, Miguel; Guerra-Rivera, Gilda; González-Bacerio, Jorge; Guisán, José M; Ruso, Juan M; Del Monte-Martínez, Alberto.
Afiliação
  • Cutiño-Avila BV; Centro de Estudio de Proteínas, Facultad de Biología, Universidad de La Habana, La Habana, Cuba.
  • Sánchez-López MI; Departamento de Microbiología y Virología, Facultad de Biología, Universidad de La Habana, La Habana, Cuba.
  • Cárdenas-Moreno Y; Departamento de Microbiología y Virología, Facultad de Biología, Universidad de La Habana, La Habana, Cuba.
  • González-Durruthy M; LAQV-REQUIMTE of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, Porto, Portugal.
  • Ramos-Leal M; Soft Matter and Molecular Biophysics Group, Department of Applied Physics, University of Santiago de Compostela, Santiago de Compostela, Spain.
  • Guerra-Rivera G; Departamento de Microbiología y Virología, Facultad de Biología, Universidad de La Habana, La Habana, Cuba.
  • González-Bacerio J; Instituto de Fruticultura Tropical, La Habana, Cuba.
  • Guisán JM; Departamento de Microbiología y Virología, Facultad de Biología, Universidad de La Habana, La Habana, Cuba.
  • Ruso JM; Centro de Estudio de Proteínas, Facultad de Biología, Universidad de La Habana, La Habana, Cuba.
  • Del Monte-Martínez A; Departamento de Bioquímica, Facultad de Biología, Universidad de La Habana, La Habana, Cuba.
Biotechnol Appl Biochem ; 69(2): 479-491, 2022 Apr.
Article em En | MEDLINE | ID: mdl-33580532
Our novel strategy for the rational design of immobilized derivatives (RDID) is directed to predict the behavior of the protein immobilized derivative before its synthesis, by the usage of mathematic algorithms and bioinformatics tools. However, this approach needs to be validated for each target enzyme. The objective of this work was to validate the RDID strategy for covalent immobilization of the enzyme laccase from Trametes maxima MUCL 44155 on glyoxyl- and monoaminoethyl-N-aminoethyl (MANA)-Sepharose CL 4B supports. Protein surface clusters, more probable configurations of the protein-supports systems at immobilization pHs, immobilized enzyme activity, and protein load were predicted by RDID1.0 software. Afterward, immobilization was performed and predictions were experimentally confirmed. As a result, the laccase-MANA-Sepharose CL 4B immobilized derivative is better than laccase-glyoxyl-Sepharose CL 4B in predicted immobilized derivative activity (63.6% vs. 29.5%). Activity prediction was confirmed by an experimentally expressed enzymatic activity of 68%, using 2,6-dimethoxyphenol as substrate. Experimental maximum protein load matches the estimated value (11.2 ± 1.3 vs. 12.1 protein mg/support mL). The laccase-MANA-Sepharose CL 4B biocatalyst has a high specificity for the acid blue 62 colorant. The results obtained in this work suggest the possibility of using this biocatalyst for wastewater treatment.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Lacase / Trametes Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Lacase / Trametes Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2022 Tipo de documento: Article