Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
Abstract: Aspergillus niger HPD-2 has interesting growth characteristics, it grows at a temperature of 38 ºC and pH of 3, it is also known that it produces various enzymes of commercial interest such as glucoamylase, which is present in the medium even under non-inducible conditions and has importan...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2023 |
| País: | México |
| Institución: | UNIVERSIDAD DE SONORA |
| Repositorio: | Biotecnia |
| Idioma: | inglés |
| OAI Identifier: | oai:oai.biotecnia.unison.mx:article/2024 |
| Acceso en línea: | https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024 |
| Access Level: | acceso abierto |
| Palabra clave: | Glucoamylase A. niger Biochemical characterization Molecular characterization Enzyme kinetic Glucoamilasa caracterización molecular caracterización bioquímica cinética enzimática |
| Sumario: | Abstract: Aspergillus niger HPD-2 has interesting growth characteristics, it grows at a temperature of 38 ºC and pH of 3, it is also known that it produces various enzymes of commercial interest such as glucoamylase, which is present in the medium even under non-inducible conditions and has important activity characteristics such as an optimum temperature of 70 ºC and an optimum pH of 3-4. These features are very important because they will help to minimize microbial contamination risk in industrial hydrolysis processes. For the characterization of A. niger HPD-2 glucoamylase, the presence and activity of the enzyme were verified in a non-inducing medium. The apparent kinetic parameters Km, Ki and Vmax were determined, 6.66 mM, 0.601 M and 66.5 mM/min respectively. As well as its optimum pH and temperature activity (pH 3 and 70 °C). Comparatively speaking, these data are competitive against those reported for similar purified enzymes. On the other hand, DNA sequence analysis of A. niger HPD-2 glucoamylase gene showed no changes in the promoter region or starch-binding domains. Therefore, the presence of the enzyme in a non-inducing medium could be related to changes in a repressor protein CreA. |
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