Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1217386 | Journal of Chromatography B | 2011 | 5 Pages |
Abstract
A method for the recovery and fractionation of whey proteins from a whey protein concentrate (80%, w/w) by hydrophobic interaction chromatography is proposed. Standard proteins and WPC 80 dissolved in phosphate buffer with ammonium sulfate 1 M were loaded in a HiPrep Octyl Sepharose FF column coupled to a fast protein liquid chromatography (FPLC) system and eluted by decreasing the ionic strength of the buffer using a salt gradient. The results showed that the most hydrophobic protein from whey is α-lactalbumin and the less hydrophobic is lactoferrin. It was possible to recover 45.2% of β-lactoglobulin using the HiPrep Octyl Sepharose FF column from the whey protein concentrate mixture with 99.6% purity on total protein basis.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Maria João Santos, José A. Teixeira, Lígia R. Rodrigues,