Artículos de revistas
Bovine lactoferrin purification from whey using Yellow HE-4R as the chromatographic affinity ligand
Fecha
2014-01Registro en:
Baieli, María Fernanda; Urtasun, Nicolás; Miranda, Maria Victoria; Cascone, Osvaldo; Wolman, Federico Javier; Bovine lactoferrin purification from whey using Yellow HE-4R as the chromatographic affinity ligand; Wiley VCH Verlag; Journal of Separation Science; 37; 5; 1-2014; 484-487
1615-9306
1615-9314
CONICET Digital
CONICET
Autor
Baieli, María Fernanda
Urtasun, Nicolás
Miranda, Maria Victoria
Cascone, Osvaldo
Wolman, Federico Javier
Resumen
The worldwide production of whey increases by around 186 million tons each year and it is generally considered as a waste, even when several whey proteins have important economic relevance. For its valorization, inexpensive ligands and integrated chromatography methods need to be developed for specific and low-cost protein purification. Here, we describe a novel affinity process with the dye Yellow HE-4R immobilized on Sepharose for bovine lactoferrin purification. This approach based on a low-cost ligand showed an efficient performance for the recovery and purification of bovine lactoferrin directly from whey, with a yield of 71% and a purification factor of 61.