Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads
Thermomyces lanuginosus lipase was immobilized in PVAalginate beads, obtaining immobilization % in the range of 94.4-98.4% using PVA concentrations ranging from 11% to 12.5%, and with cross linking times of 45 and 60 min using boric acid. Initial reaction rate was determined in free and immobilized...
| Autores: | , , , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2011 |
| País: | México |
| Recursos: | Universidad Autónoma de Coahuila |
| Repositorio: | Redalyc-UADEC |
| OAI Identifier: | oai:redalyc.org:47521300008 |
| Acesso em linha: | https://www.redalyc.org/articulo.oa?id=47521300008 |
| Access Level: | acceso abierto |
| Palavra-chave: | Química PVA Lipase alginate immobilized Thermomyces lanuginosus |
| Resumo: | Thermomyces lanuginosus lipase was immobilized in PVAalginate beads, obtaining immobilization % in the range of 94.4-98.4% using PVA concentrations ranging from 11% to 12.5%, and with cross linking times of 45 and 60 min using boric acid. Initial reaction rate was determined in free and immobilized state by hydrolysis of p-nitrophenol palmitate. Operational stability at different pH (4-7), agitation (100-500 r.p.m.), and temperature (40-80 °C) was investigated. Results showed that pH 6 and 7 no considerable loss of enzyme activity or enzyme was observed. At temperatures over 70 °C, enzyme suffers physical damage and showed a considerable loss of activity. No significant difference was observed when agitation was varied from 100 to 500 r.p.m. |
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