Isolation of lactoferrin from whey by dye-affinity chromatography with Yellow HE-4R attached to chitosan mini-spheres
Novel integrated chromatographic methods need to be developed for specific, low-cost protein purification from raw materials. Here, a process for bovine lactoferrin (Lf) isolation from sweet whey was developed using cross-linked chitosan mini-spheres with immobilised Yellow HE-4R dye as a low-cost l...
| Autores: | , , , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2014 |
| País: | Argentina |
| Recursos: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/15741 |
| Acesso em linha: | http://hdl.handle.net/11336/15741 |
| Access Level: | acceso abierto |
| Palavra-chave: | Lactoferrin Purification Dye Affinity Chromatography Yellow He-4r https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
| Resumo: | Novel integrated chromatographic methods need to be developed for specific, low-cost protein purification from raw materials. Here, a process for bovine lactoferrin (Lf) isolation from sweet whey was developed using cross-linked chitosan mini-spheres with immobilised Yellow HE-4R dye as a low-cost ligand. The maximum adsorption capacity was between 51.14 and 58.28 mg Lf g−1 matrix. In addition, the mini-spheres adsorbed around 95% of the Lf present in the sweet whey and eluted more than 80% of the adsorbed Lf. A yield of 77% with purity greater than 90% was achieved in only one purification step. The purification process was efficient for three consecutive cycles without regeneration steps. |
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