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http://dspace.udla.edu.ec/handle/33000/7383| Tipo de material : | bachelorThesis |
| Título : | Optimización del medio de crecimiento de Mucor sp para la producción de ureasa y su posterior inmovilización enzimática |
| Autor : | Pilco Paguay, Angel Roberto |
| Tutor : | Morera Córdova, Vivian |
| Palabras clave : | INHIBIDORES DE LA UREASA;UREA-ENZIMAS |
| Fecha de publicación : | 2017 |
| Editorial : | Quito: Universidad de las Américas, 2017 |
| Citación : | Pilco Paguay, Angel Roberto (2017). Optimización del medio de crecimiento de Mucor sp para la producción de ureasa y su posterior inmovilización enzimática. Facultad de Ingenierías y Ciencias Aplicadas. UDLA. Quito. 87 p. |
| Resumen : | La ureasa es un tipo de metaloenzima hexamérica que depende de dos iones de níquel por subunidad e hidroliza la urea para producir amoniaco y carbamato... |
| Descripción : | Urease is a type of hexameric metalloenzyme, it depends of two nickel ions per subunit and hydrolyzes urea to produce ammonia and carbamate. The latter compound is spontaneously hydrolysed to form carbonic acid and another molecule of ammonia. The applications of this enzyme are varied, it is used for the total determination of urea in the blood and urine, in the wine industry, for the removal of urea during dialysis and is used as a pH controller. The aim of the present work was to optimize the growth medium of a filamentous fungus Mucor sp for the production and immobilization of urease. An experimental design of a rotational 2k response surface was used to evaluate the variables: pH and nickel concentration for the optimization of the fungus growth medium,% glutaraldehyde and time for urease immobilization. The enzymatic activity was the response variable. The best results of this design were obtained at pH 6.65 and concentration of Ni2+ 0.044 g/L. These conditions produced a theoretical enzymatic activity of 0.213 U/mL. When carrying out the experiments with the optimal parameters, the experimental value of the enzymatic activity was 0.2209 U/mL. As for the immobilized enzyme, the optimal glutaraldehyde concentration and activation time were 1.37% and 81.31 minutes, respectively, and a theoretical activity of 1.3107 U/mL, and when the experiment was carried out with the optimal parameters, the enzymatic activity was 1,239 U/mL. In addition, the kinetic constants Km and Vmax of both the free enzyme and the enzyme immobilized by the Lineweaver-Burk method were evaluated. The Km of the immobilized enzyme resulted in 1.42 compared to 8.04 of the free enzyme. This result indicates that there is high affinity of the substrate for the active site of the urease enzyme. |
| URI : | http://dspace.udla.edu.ec/handle/33000/7383 |
| Aparece en las colecciones: | Ingeniería en Biotecnología |
Ficheros en este ítem:
| Fichero | Descripción | Tamaño | Formato | |
|---|---|---|---|---|
| UDLA-EC-TIB-2017-07.pdf | 2,37 MB | Adobe PDF |  Visualizar/Abrir |
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