Stabilization of an amylase from Neurospora crassa by Immobilization on Highly Activated Supports
The amylase from Neurospora crassa is an interesting enzyme, having higher stability than amylase from Aspergillus oryzea under a broad range of pH values. Moreover, the N. crassa enzyme may be immobilized on different supports with good retention of enzyme activity. The best stabilizations were ach...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2008 |
| País: | Brasil |
| Institución: | Universidade Estadual Paulista (UNESP) |
| Repositorio: | Repositório Institucional da UNESP |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.unesp.br:11449/225248 |
| Acceso en línea: | http://dx.doi.org/10.1080/08905430802262616 http://hdl.handle.net/11449/225248 |
| Access Level: | acceso abierto |
| Palabra clave: | Amylase Enzyme immobilization Enzyme stabilization Glyoxyl agarose Neurospora crassa |
| Sumario: | The amylase from Neurospora crassa is an interesting enzyme, having higher stability than amylase from Aspergillus oryzea under a broad range of pH values. Moreover, the N. crassa enzyme may be immobilized on different supports with good retention of enzyme activity. The best stabilizations were achieved using Eupergit C 250 L or glyoxyl agarose, with which the enzyme remained fully active at 60°C for 24 h while the soluble enzyme remained about 17%. The glyoxyl agarose immobilized enzyme had high thermostability, high optimal temperature (65°C) and broad pH/activity profile, suggesting that this enzyme has potential for food and industrial applications for starch modification. Copyright © Taylor & Francis Group, LLC. |
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