Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2434286 | International Dairy Journal | 2014 | 7 Pages |
Abstract
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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Authors
María Fernanda Baieli, Nicolás Urtasun, María Victoria Miranda, Osvaldo Cascone, Federico Javier Wolman,