Enhancing oxidation activity and stability of iso-1-cytochrome c and chloroperoxidase by immobilization in nanostructured supports
Por:
Águila S., Vazquez-Duhalt R., Covarrubias C., Pecchi G., Alderete J.B.
Publicada:
1 jul 2011
Resumen:
The immobilization of enzymes in inorganic materials has been widely used because it can produce an enhancement of the catalytic stability and enzymatic activity. In this article, the effect of the immobilization of iso-1-cytochrome c (CYC-Sc) from Saccharomyces cerevisiae and chloroperoxidase (CPO) from Caldariomyces fumago on the enzyme stability and catalytic oxidation of styrene was studied. The immobilization was carried out in three silica nanostructured supports with different pore size MCM-41 (3.3 nm), SBA-15 (6.4 nm) and MCF (12.1 nm). The adsorption parameters and leaching degree of immobilized enzymes were determined. Catalytic parameters of immobilized and free enzymes were determined at different temperatures (20-60 degrees C) and in different acetonitrile/water mixtures (15-85% of acetonitrile). The results show that there is low leaching of the enzymes in the three supports assayed and the adsorption capacity (q(max)) was higher as the pore size of the support increased.
Filiaciones:
Águila S.:
Facultad de Ciencias Químicas, Universidad de Concepció, Casilla 160-C, Concepción, Chile
Vazquez-Duhalt R.:
UNAM, Inst Biotecnol, Cuernavaca 62210, Morelos, Mexico
Covarrubias C.:
Centro Para la Investigación Interdisciplinaria Avanzada en Ciencias de Los Materiales, Universidad de Chile, Santiago, Chile
Pecchi G.:
Facultad de Ciencias Químicas, Universidad de Concepció, Casilla 160-C, Concepción, Chile
Alderete J.B.:
Facultad de Ciencias Químicas, Universidad de Concepció, Casilla 160-C, Concepción, Chile
Universidad de Concepción, Quimica Organica, Edmundo Larenas 129, Concepción, Chile
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