Purification of an exopolygalacturonase from Penicillium viridicatum RFC3 produced in submerged fermentation
An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50-55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturoni...
| Autores: | , , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2009 |
| País: | Brasil |
| Recursos: | Universidade Estadual Paulista (UNESP) |
| Repositorio: | Repositório Institucional da UNESP |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.unesp.br:11449/71313 |
| Acesso em linha: | http://dx.doi.org/10.1155/2009/631942 http://hdl.handle.net/11449/71313 |
| Access Level: | acceso abierto |
| Palavra-chave: | Penicillium Penicillium viridicatum |
| Resumo: | An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50-55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of pectin with a high degree of esterification (D.E.). Ions Ca 2+ enhanced the stability of enzyme and its activity by 30%. The K m was 1.30 in absence of Ca 2+ and 1.16mg mL -1 in presence of this ion. In relation to the Vmax the presence of this ion increased from 1.76 to 2.07 μmol min -1mg -1. Copyright © 2009 Eleni Gomes et al. |
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