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http://dspace.udla.edu.ec/handle/33000/6183| Tipo de material : | bachelorThesis |
| Título : | Optimización de un medio de cultivo para la producción de enzimas oxidorreductasas tipo lacasas de pleurotus ostreatus, para su posterior inmovilización enzimática en alginato de calcio |
| Autor : | Larrea Sarmiento, Adriana Estefanía |
| Tutor : | Cruz Salazar, María Alejandra |
| Palabras clave : | ENZIMOLOGÍA;LACASA;PLEUROTUS OSTREATUS;ESTABILIDAD ENZIMÁTICA |
| Fecha de publicación : | 2016 |
| Editorial : | Quito: Universidad de las Américas, 2016 |
| Citación : | Larrea Sarmiento, A. E. (2016). Optimización de un medio de cultivo para la producción de enzimas oxidorreductasas tipo lacasas de pleurotus ostreatus, para su posterior inmovilización enzimática en alginato de calcio. (Tesis de pregrado). Universidad de las Américas, Quito. |
| Resumen : | Las lacasas son enzimas oxidasas multicobre, secretadas extracelularmente por varios organismos, incluyendo a Pleurotus ostreatus... |
| Descripción : | The laccases are multicopper oxidase enzymes secreted extracellularly by several organisms, including Pleurotus ostreatus. These have been the focus of studies for their ability to oxidize a wide variety of organic and inorganic substrates, so its scope is varied. The aim of this project was to evaluate the production of laccase-type enzymes, depending on the concentration of Cu2+ ion as an inducing agent and three substrates as a carbon source, for further immobilization in 2% calcium alginate and 0.5% glutaraldehyde beads. The results showed that glucose was the best carbon source compared to rice husks and wheat bran, whereas statistical analyzes indicated that T2 (0.2 g/L Cu2 +, 9.23 g/L glucose) presented the largest enzyme activity at day 38 with a value of 100.62 U/mL. The enzymatic activity of crude extract and immobilized enzyme, with respect to temperature and pH, presented the same pattern: it proportionally increased reaching a maximum point and then decreased. The optimum pH and temperature were 6.05 and 30°C for crude extract and 5.5 and 40°C for immobilized enzyme, respectively. Furthermore, the kinetic parameters Vmax and Km indicated that the immobilization produced a decrease in the affinity of the laccase toward guaiacol substrate compared with the crude extract, but the catalytic efficiency was higher for the immobilized enzyme. So it is concluded that it is possible to optimize the production of the laccase enzyme and its immobilization would address future applications in the industry of Ecuador. |
| URI : | http://dspace.udla.edu.ec/handle/33000/6183 |
| Aparece en las colecciones: | Ingeniería en Biotecnología |
Ficheros en este ítem:
| Fichero | Descripción | Tamaño | Formato | |
|---|---|---|---|---|
| UDLA-EC-TIB-2016-14.pdf | 1,66 MB | Adobe PDF |  Visualizar/Abrir |
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