Obtención de Variantes Hiperactivas e Inactivas de la Endocelulasa Cel9 de Myxobacter Sp. Al-1
Due to its biotechnological impact, there is currently a growing interest in the production of cellulases with novel biochemical properties. Here, multiple generations of random mutagenesis in vivo and screening were employed to generate variants of the modular cellulase Cel9 from Myxobacter Sp. AL-...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2006 |
| País: | México |
| Institución: | UNIVERSIDAD DE GUANAJUATO |
| Repositorio: | Acta Universitaria |
| Idioma: | español |
| OAI Identifier: | oai:www.actauniversitaria.ugto.mx:article/196 |
| Acceso en línea: | https://www.actauniversitaria.ugto.mx/index.php/acta/article/view/196 |
| Access Level: | acceso abierto |
| Palabra clave: | Celulosa Celulasas Evolución de proteínas. Cellulose Cellulases Protein evolution. |
| Sumario: | Due to its biotechnological impact, there is currently a growing interest in the production of cellulases with novel biochemical properties. Here, multiple generations of random mutagenesis in vivo and screening were employed to generate variants of the modular cellulase Cel9 from Myxobacter Sp. AL-1. Following this approach, Cel9 variants which showed increases upto 7.5 fold of cellulase activity were obtained. In addition, Cel9 mutants which completely lost the ability to degrade cellulose were also obtained. Results revealed that mutations associated with the phenotype of the Cel9 variants occurred on the mutant gene sequence and that themutants with null or reduced activity did not accumulate in the cell. In addition to the potential biotechnological application of the enzymes with improved activity obtained here, the results of this work will contribute to the understanding of the structure and function of cellulases grouped in the family 9 of glycosyl hydrolases. |
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