Gram scale separation of casein proteins from whole casein on a Source 30Q anion-exchange resin column utilizing fast protein liquid chromatography (FPLC)

Johann Plank, Philip R. Andres, Ingolf Krause, Christian Winter

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

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 α-, β-, and κ-casein for further testing utilizing fast protein liquid chromatography (FPLC) and preceding enrichment in the case of κ-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).

Original languageEnglish
Pages (from-to)176-181
Number of pages6
JournalProtein Expression and Purification
Volume60
Issue number2
DOIs
StatePublished - Aug 2008
Externally publishedYes

Keywords

  • Biopolymers
  • Casein
  • Chromatography
  • Protein
  • Separation

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