A new platform for chymotrypsin isolation from fresh bovine pancreas using an environmental friendly polyelectrolyte: Alginate
The separation of chymotrypsin from a crude filtrate of fresh bovinepancreas homogenate was carried out using precipitation with acommercially available negatively charged natural weak polyelectrolyte:sodium alginate. The zymogen form of the enzyme was activated by theaddition of trypsin at pH 8.2 i...
| Autores: | , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2015 |
| País: | Argentina |
| Recursos: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/53202 |
| Acesso em linha: | http://hdl.handle.net/11336/53202 |
| Access Level: | acceso abierto |
| Palavra-chave: | PURIFICATION CONCENTRATION ALGINATE PEROXIDASE CHYMOTRYPSIN POLYELECTROLYTE ENZYME-POLYELECTROLYTE COMPLEX https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
| Resumo: | The separation of chymotrypsin from a crude filtrate of fresh bovinepancreas homogenate was carried out using precipitation with acommercially available negatively charged natural weak polyelectrolyte:sodium alginate. The zymogen form of the enzyme was activated by theaddition of trypsin at pH 8.2 in the absence of Ca++, then, the enzyme wasprecipitated by sodium alginate addition at pH 5.00. The non-solublecomplex was separated by simple centrifugation and re-dissolved by apH change to 8.20. The recovery of chymotrypsin biological activity was36.1 % of the initial activity in the pancreas homogenate with a 3.2 foldincrease in its specific activity. The volume of the final product decreasedto 6.25 % of the initial feedstock, concentrating the sample up to 16times. |
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