| Revista: | Brazilian journal of chemical engineering |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000308999 |
| ISSN: | 0104-6632 |
| Autores: | Adriano, W.S1 Filho, E.H.C2 Silva, J.A Giordano, R.L.C Goncalves, L.R.B |
| Instituciones: | 1Universidade Federal de Sao Carlos, Departamento de Engenharia Quimica, Sao Carlos, Sao Paulo. Brasil 2Universidade Federal do Ceara, Departamento de Engenharia Quimica, Fortaleza, Ceara. Brasil |
| Año: | 2005 |
| Periodo: | Dic |
| Volumen: | 22 |
| Número: | 4 |
| Paginación: | 529-538 |
| País: | Brasil |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental, aplicado |
| Resumen en inglés | The objective of this work was to study enzyme immobilization on chitosan activated with glutaraldehyde, aiming to produce a cheap biocatalyst. Two different immobilization strategies were studied: one-point and multipoint covalent attachment to the solid matrix. The multipoint covalent attachment derivative had an 82% immobilization yield. It was 4.9-fold more stable than the free enzyme at 50°C and 4.5-fold more stable than soluble enzyme at pH 10.0. The one-point derivative had an 85% immobilization yield. It was 2.7-fold more stable than the free enzyme at 50°C and 3.8-fold more stable than soluble PGA at pH 10.0. Results indicated that chitosan can be loaded with PGA above 330 IU/g. Intraparticle diffusive effects, however, limited hydrolysis of penicillin G catalyzed by those derivatives at 37°C and 25°C. Operational stability assays were performed and the multipoint derivative exhibited a half-life of 40 hours |
| Disciplinas: | Química |
| Palabras clave: | Química farmacéutica, Biotecnología, Inmovilización enzimática, Estabilidad química, Penicilina G acilasa, Quitosana |
| Keyword: | Chemistry, Medicinal chemistry, Biotechnology, Enzyme immobilization, Chemical stability, Penicillin G acylase, Chitosan |
| Texto completo: | Texto completo (Ver HTML) |
