title: Gram scale separation of casein proteins from whole casein on a Source 30Q anion-exchange resin column utilizing fast protein liquid chromatography (FPLC).
abstract: Casein is used as an additive in binders or paints and as such exhibits unique properties which might be based on the properties of certain subproteins in the complex whole casein mixture. Therefore, the separation of whole casein (CN) from cow milk was performed on a gram scale in order to yield sufficient amounts of the protein subfractions alpha-, beta-, and kappa-casein for further testing utilizing fast protein liquid chromatography (FPLC) and preceding enrichment in the case of kappa-casein. Construction chemical grade casein, which differs in quality from dairy grade casein, was used for separation because of our interest in the proteins responsible for plastification of cementitious systems such as mortar. The solubilized proteins were separated chromatographically via ion exchange chromatography (IEX) and the subsequently desalted protein fractions were tested for purity by isoelectric focusing (IEF).
authors.affiliation: Chair for Construction Chemicals, Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany. johann.plank@bauchemie.ch.tum.de <johann.plank@bauchemie.ch.tum.de>
authors.forename: Johann
authors.initials: J
authors.lastname: Plank
authors.forename: Philip R
authors.initials: PR
authors.lastname: Andres
authors.forename: Ingolf
authors.initials: I
authors.lastname: Krause
authors.forename: Christian
authors.initials: C
authors.lastname: Winter
mesh_terms: D000837:Anion Exchange Resins; D002364:Caseins / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D007525:Isoelectric Focusing
chemical_list: D000837:Anion Exchange Resins; D002364:Caseins