| Revista: | Quimica nova |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000313181 |
| ISSN: | 0100-4042 |
| Autors: | Gomes, Fabricio M1 Paula, Ariela V. de Silva, Grazielle dos S Castro, Heizir F. de |
| Institucions: | 1Faculdade de Engenharia Quimica de Lorena, Departamento de Engenharia Quimica, Lorena, Sao Paulo. Brasil |
| Any: | 2006 |
| Període: | Jul |
| Volum: | 29 |
| Número: | 4 |
| Paginació: | 710-718 |
| País: | Brasil |
| Idioma: | Portugués |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental, aplicado |
| Resumen en inglés | Microbial lipase from Candida rugosa was immobilized by covalent binding on wood cellulignin (Eucaliptus grandis) chemically modified with carbonyldiimidazole. The immobilized system was fully evaluated in aqueous (olive oil hydrolysis) and organic (ester synthesis) media. A comparative study between free and immobilized lipase was carried out in terms of pH, temperature and thermal stability. A higher pH value (8.0) was found optimal for the immobilized lipase. The optimal reaction temperature shifted from 37 °C for the free lipase to 45 °C for the immobilized lipase. The pattern of heat stability indicated that the immobilization process tends to stabilize the enzyme. Kinetics tests at 37 °C following the hydrolysis of olive oil obeyed the Michaelis-Menten rate equation. Values for Km = 924.9 mM and Vmax = 198.3 U/mg were lower than for free lipase, suggesting that the affinity towards the substrate changed and the activity of the immobilized lipase decreased during the course of immobilization. The immobilized derivative was also tested in the ester synthesis from several alcohols and carboxylic acids |
| Disciplines | Química |
| Paraules clau: | Bioquímica, Biotecnología, Enzimas inmovilizadas, Catálisis, Celulignina, Lipasas, Candida rugosa |
| Keyword: | Chemistry, Biochemistry, Biotechnology, Immobilized enzymes, Catalysis, Cellulignin, Lipases, Candida rugosa |
| Text complet: | Texto completo (Ver HTML) |
