INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
This work presents a comparative study of the influence of the nature of the substrate and the immobilization and laccase enzyme activity and stability. The supports employed were: hydrotalcite-like particles mechanism onsediments) S.A. Medina-Moreno, S. Huerta-Ochoa, C.A. surface. Two immobilizatio...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2013 |
| País: | México |
| Institución: | Universidad Autónoma Metropolitana |
| Repositorio: | Redalyc-UAM |
| OAI Identifier: | oai:redalyc.org:62030721005 |
| Acceso en línea: | https://www.redalyc.org/articulo.oa?id=62030721005 |
| Access Level: | acceso abierto |
| Palabra clave: | Ingeniería thiol laccase hydrotalcite glassy carbon immobilization |
| Sumario: | This work presents a comparative study of the influence of the nature of the substrate and the immobilization and laccase enzyme activity and stability. The supports employed were: hydrotalcite-like particles mechanism onsediments) S.A. Medina-Moreno, S. Huerta-Ochoa, C.A. surface. Two immobilization mechanisms were applied: one (ZnAl2 ), amorphous silica crystals, and glassy carbon Lucho-Constantino, L. Aguilera-Vázquez, A. Jiménez- physical, by adsorption, Gutiérrez-Rojaschemical, with two versions of covalent bonding. In the first, using silanes González y M. and the other and glutaraldehyde (GA), in the second, thiols were used as anchoring reagents. Hydrotalcite and silica supports 259 Crecimiento, sobrevivencia y adaptación the enzyme by X-ray diffraction analysis (XRD), while in the case were characterized before and after immobilizingde Bifidobacterium infantis a condiciones ácidas of glassy carbon supports electrochemical characterization was performed. The catalytic properties Km and Kcat /Km (Growth, survival and adaptation of Bifidobacterium infantis to acidic conditions) of every enzymatic system were evaluated in a complementary fashion, as well as the free enzyme. The kinetic L. Mayorga-Reyes, P. Bustamante-Camilo, A. Gutiérrez-Nava, E. Barranco-Florido y A. Azaola- characterizations were done using ABTS (ammonium 2,2’azino-bis-(3-ethylbenzothiazoline-6-sulfonate acid)), as a reagent typical of laccase in 0.1 M acetate buffer solution pH 3.7. Efficiency of the enzyme adsorbed on each Espinosa support it was demonstrated that optimization of immobilization is decisive in the catalysis. Greater efficiency was the method of ethanol fermentation by Saccharomyces cerevisiae in the 265 Statistical approach to observed in the system that employed glassy carbon with either immobilization mechanism and these results are analogous with the of Valfor® zeolite NaA presence free enzyme. |
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