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Bovine lactoferrin purification from whey using Yellow HE ‐4 R as the chromatographic affinity ligand
Author(s) -
Baieli María Fernanda,
Urtasun Nicolás,
Miranda María Victoria,
Cascone Osvaldo,
Wolman Federico Javier
Publication year - 2014
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.201301086
Subject(s) - lactoferrin , chemistry , affinity chromatography , chromatography , ligand (biochemistry) , sepharose , yield (engineering) , recombinant dna , whey protein , protein purification , biochemistry , enzyme , materials science , receptor , metallurgy , gene
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 Y ellow HE ‐4R immobilized on S epharose 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.