β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
The effect of β-cyclodextrin modifications (polymerization (PCD) and later carboxymethylation (CMPCD)) on their action as enzyme stabilizers was analyzed during freeze-drying and thermal treatment. Combined polymer-trehalose matrices were also employed. Due to their higher Tg values, PCD and CMPCD p...
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2011 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/113194 |
| Acceso en línea: | http://hdl.handle.net/11336/113194 |
| Access Level: | acceso abierto |
| Palabra clave: | ADDITIVES ENZYME STABILITY FREEZE-DRIED ENZYME FORMULATIONS MODIFIED CYCLODEXTRINS POLYCYCLODEXTRIN https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| Sumario: | The effect of β-cyclodextrin modifications (polymerization (PCD) and later carboxymethylation (CMPCD)) on their action as enzyme stabilizers was analyzed during freeze-drying and thermal treatment. Combined polymer-trehalose matrices were also employed. Due to their higher Tg values, PCD and CMPCD provided better structural stability to the freeze-dried formulations than β-CD. However, only PCD was a good excipient to protect invertase both in amorphous and supercooled systems. FT-IR revealed increased protein denaturation in the presence of CMPCD, but not in the presence of PCD. Even though all polymers inhibited/delayed trehalose crystallization, only trehalose (T) combined with PCD (PCD + T) and with β-cyclodextrin (β-CD + T) offered the best stability to the enzyme. In β-CD + T system, trehalose was the main responsible for the protection. In PCD + T system, both additives contributed to improve the enzyme stability. FT-IR and DSC were useful to analyze the combined role of molecular and supramolecular interactions on enzyme stability in dehydrated model systems. |
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