Partição de proteínas de soro de leite em sistemas aquosos bifásicos baseados em líquidos iônicos
In this work, we used an aqueous two-phase system (ATPS) consisting of the ionic liquid [C4mim][Cl] and the salt K2HPO4 to partition α-lactalbumin, β-lactoglobulin, and lactoferrin whey proteins. Extraction efficiency values above 87% indicate that the proteins primarily migrated to the ionic liquid...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2015 |
| País: | Brasil |
| Institución: | Universidade Federal de Viçosa (UFV) |
| Repositorio: | LOCUS Repositório Institucional da UFV |
| Idioma: | portugués |
| OAI Identifier: | oai:locus.ufv.br:123456789/24972 |
| Acceso en línea: | http://dx.doi.org/10.5935/0100-4042.20150123 http://www.locus.ufv.br/handle/123456789/24972 |
| Access Level: | acceso abierto |
| Palabra clave: | Liquid–liquid extraction Ionic liquid Partition coefficient Proteins |
| Sumario: | In this work, we used an aqueous two-phase system (ATPS) consisting of the ionic liquid [C4mim][Cl] and the salt K2HPO4 to partition α-lactalbumin, β-lactoglobulin, and lactoferrin whey proteins. Extraction efficiency values above 87% indicate that the proteins primarily migrated to the ionic liquid-rich phase (top phase). Partition coefficient values ranged from 6.17 to 8.93 for a-lactalbumin, from 22.80 to 34.55 for β-lactoglobulin, and from 26.46 to 40.06 for lactoferrin. Therefore, the saline ATPS with the ionic liquid examined in this study can be considered to be a promising alternative for extracting whey proteins. |
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