Characterization of chymotrypsin-ι-carrageenan complex in aqueous solution: A solubility and thermodynamical stability study
The aim of this study is to report the results of research work on the molecular mechanism of complex formation between chymotrypsin and a negatively charged natural strong polyelectrolyte, ι-carrageenan, using spectroscopy techniques. The carrageenan-chymotrypsin complex showed a maximal non-solubi...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2012 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/197440 |
| Acceso en línea: | http://hdl.handle.net/11336/197440 |
| Access Level: | acceso abierto |
| Palabra clave: | BTEE CAR CARRAGEENAN CHY CHYMOTRYPSIN POLYELECTROLYTE https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| Sumario: | The aim of this study is to report the results of research work on the molecular mechanism of complex formation between chymotrypsin and a negatively charged natural strong polyelectrolyte, ι-carrageenan, using spectroscopy techniques. The carrageenan-chymotrypsin complex showed a maximal non-solubility at pH around 4.50 with a stoichiometric ratio between 8 and 33. g of chymotrypsin per g of carrageenan. These values were depended on the enzyme concentration, pH and ionic strength medium. The insoluble complex was redissolved by modifying the pH and by a NaCl concentration around 0.2. M in agreement with a coulombic mechanism of complex formation. The non-soluble complex formation showed biphasic kinetics. A fast step was carried out around 10. s and a coulombic mechanism takes place, and a slower step of around 120. s, where participate only Van der Waals forces. The enzymatic activity of chymotrypsin was maintained even in the presence of carrageenan (0.005%, w/v). |
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