Separation of a glycosylated and non-glycosylated fraction of caseinomacropeptide using different anion-exchange stationary phases.
Caseinomacropeptide (CMP), a heterogeneous group of peptides regarding the degree of glycosylation and phosphorylation, has so far not been effectively fractionated into its two major fractions: the glycosylated gCMP and the non-glycosylated aCMP. Therefore, an anion-exchange chromatography (AEC) process for the fractionation of CMP in those two fractions was developed and optimized. Furthermore, the method was applied to compare membrane adsorption chromatography (MAC) devices with classical bead-based column chromatography. It was shown that MAC devices can separate gCMP from aCMP, however, at a lower level of binding capacity and chromatographic resolution compared to classical chromatography. On the other hand, a fractionation is achieved at a four times faster separation speed.
Kreuss
Markus
M
Technische Universitaet Muenchen, Chair for Food Process Engineering and Dairy Technology, Weihenstephaner Berg 1, 85354 Freising, Germany. markus.kreuss@wzw.tum.de
Krause
Ingolf
I
Kulozik
Ulrich
U
D002364:Caseins / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D006031:Glycosylation; D010446:Peptide Fragments / Q000302:isolation & purification*
D002364:Caseins; D010446:Peptide Fragments; C065989:caseinomacropeptide