Purification of the two major proteins from whey concentrate using a cation-exchange selective adsorption process.
The packed-bed adsorption and elution of aqueous solutions of whey concentrate powders were investigated at pH 3.7 using a 5-mL SP Sepharose FF column to separate and isolate two major proteins namely, alpha-lactalbumin (ALA) and beta-lactoglobulin (BLG) from these solutions. ALA displaced and eluted BLG from the column in a pure form. Pure ALA could then be eluted with good recovery. A novel consecutive two-stage separation process was developed to separate ALA and BLG from whey concentrate mixtures. Almost all of the BLG in the feed was recovered, with 78% being recovered at 95% purity and a further 20% at 86% purity. In addition, 67% of ALA was recovered, 48% at 54% purity and 19% at 60% purity.
El-Sayed
Mayyada M H
MM
Dept. of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, U.K. mmhae2@cam.ac.uk
Chase
Howard A
HA
D000327:Adsorption; D002412:Cations / Q000737:chemistry; D002852:Chromatography, Ion Exchange / Q000379:methods*; D007768:Lactalbumin / Q000737:chemistry / Q000302:isolation & purification*; D007782:Lactoglobulins / Q000737:chemistry / Q000302:isolation & purification*; D008894:Milk Proteins / Q000737:chemistry*; D012685:Sepharose / Q000737:chemistry*; D012996:Solutions; D013499:Surface Properties; D000067816:Whey Proteins
D002412:Cations; D007782:Lactoglobulins; D008894:Milk Proteins; D012996:Solutions; D000067816:Whey Proteins; C097574:sepharose fast flow SP; D012685:Sepharose; D007768:Lactalbumin