Obtaining of nanobiocatalysts through the immobilization of calb in superparamagnetics nanoparticles

• Autor(a) principal: Victor Moreira da Costa
• Data de Publicação: 2014
• Tipo de documento: Dissertação
• Idioma: por
• Título da fonte: Biblioteca Digital de Teses e Dissertações da UFC
• Texto Completo: http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=12422
• topic: Magnetita; APTES; CALB; nanopartÃculas; Nanobiocatalisadores; Magnetite; APTES; CALB; nanoparticles; Nanobiocatalysts; QUIMICA INORGANICA

The magnetic nanomaterials have attracted interest in many areas due to their unique properties and a wide range of applications. One of the most used nanoparticles is magnetite, formed of an oxide of Fe +2 and Fe +3 which has a high saturation magnetization and high surface area. These properties allow the immobilization of various molecules , such as surfactants , co - polymers , drugs and enzymes for application in biomedicine , food engineering , nanochips and biocatalysts . In the present work nanobiocatalysts were produced by immobilization of CALB (Lipase B) in superparamagnetic nanoparticles functionalized with different concentrations of APTES. The structural, morphological and magnetic properties of the samples were investigated by X- ray diffraction (XRD), Spectroscopy with Fourier Transform Infrared in Region (FTIR), Thermogravimetric Analysis (TGA), adsorption/desorption of nitrogen (BET), Magnetometer Sample Vibrant (VSM), and Analysis of Catalytic Activity (Activity derivative). The XRD showed peaks crystallographic structure of spinel for magnetite in the sample. The average particle size obtained by XRD and VSM was 10nm for magnetite and 13nm for NP/ APTES. The magnetic parameters of the samples were observed by VSM and all showed superparamagnetic behavior with a decrease in the saturation magnetization of 69 emu / g of magnetite to about 35 emu / g for the complete system . TG analyzes and FTIR revealed the presence of molecules of APTES on the surface of the nanoparticle in which were found the best values of adsorption for sample NP / APTES (1:3) and this used for the immobilization of the enzyme. Was performed analysis of the hydrolytic activity of the immobilized enzyme prepared in different media concentrations of APTES. Which showed a maximum activity of 47 U / g for NP/APTES (1:3)/CALB(200). Therefore, the potential presented nanobiocatalysts formed in reactions of industrial interest.