Preparation of Lactoferrin by Hydrophobic Interaction Chromatography from Milk Acid Whey

Abstract

Lactoferrin was isolated from 1.8 M ammonium sulfate whey, which had been prepared from bovine milk acid whey, by hydrophobic interaction chromatography using Butyl Toyopearl 650M and by DEAE ion exchange chromatography. The hydrophobic interaction chromatography of 1.8 M ammonium sulfate whey supernatant resulted in concentration of the whey proteins and fractionation into a fraction eluting in deionized water, a fraction eluting in .25 M acetic acid, and a fraction eluting in .2 N NaOH. Lactoferrin was contained only in the fraction released by .25 M acetic acid from the matrix of Butyl Toyopearl 650M. It is estimated that approximately 80 mg of lactoferrin can be obtained by this method from 1 L of neutralized acid whey. The isoelectric point of lactoferrin is between pH 4.8 and pH 5.3 as determined by isoelectric focusing. © 1989, American Dairy Science Association. All rights reserved.