| Revista: | Brazilian journal of chemical engineering |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000308653 |
| ISSN: | 0104-6632 |
| Autores: | Tamagawa, R.E1 Azzoni, A.R Miranda, E.A Vijayalakshmi, M.A2 |
| Instituciones: | 1Universidade Estadual de Campinas, Faculdade de Engenharia Quimica, Campinas, Sao Paulo. Brasil 2Universite Technologie de Compiegne, Centre de Recherches de Royallieu, Compiegne, Oise. Francia |
| Año: | 1999 |
| Periodo: | Jun |
| Volumen: | 16 |
| Número: | 2 |
| Paginación: | 119-127 |
| País: | Brasil |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental, aplicado |
| Resumen en inglés | Two adsorption techniques were studied as potential methods for the recovery of aprotinin: a biospecific adsorption (using immobilized trypsin and chymotrypsin as ligants) and a pseudobiospecific adsorption of aprotinin-trypsin complex onto IMAC matrix. These studies indicated that ionic strength has an important effect on aprotinin adsorption on immobilized trypsin, and the pH was the most significant variable in aprotinin desorption from both immobilized enzymes. The aprotinin-trypsin complex adsorption onto the IMAC matrix was not as significantly affected by changes in pH as it was for changes in ionic strength. For the desorption step, both variables significantly affected the complex recovery. However, the effect of ionic strength was markedly stronger for this desorption step |
| Disciplinas: | Química |
| Palabras clave: | Química farmacéutica, Aprotinina, Recuperación de proteínas, Adsorción por afinidad |
| Keyword: | Chemistry, Medicinal chemistry, Aprotinin, Protein recovery, Affinity adsorption |
| Texto completo: | Texto completo (Ver HTML) |
