Separation of whey proteins by anion-exchange membranes

Jung Il Kim, Du Young Choi, Kyung Ho Row

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Three strong anion-exchange membranes (CIM QA, Q100 and HiTrap Q) were investigated for the separation of the major proteins, which were contained in whey, such as α-Lactallbumin, BSA and β-Lactoglobulin. Experiments were performed to determine the optimum mobile phase composition for separating the whey proteins using the standard chemicals of the proteins. The mobile phase was buffer A (20 mM piperazine-HCl pH 6.4) and buffer B (buffer A+l M NaCl) and the linear gradient elution changes of salt concentration were applied. The standard chemicals of the proteins were used to investigate the optimal mobile phase compositions with the three anion-exchange membranes. From the experimental results, it was found that HiTrap Q was the most effective in separating whey proteins.

Original languageEnglish
Pages (from-to)538-541
Number of pages4
JournalKorean Journal of Chemical Engineering
Volume20
Issue number3
DOIs
StatePublished - May 2003

Bibliographical note

Funding Information:
The authors gratefully acknowledge the financial support of Center for Advanced Bioseparation Technology. This work was performed in the High-Purity Separation Laboratory of Inha University, Incheon, Korea.

Keywords

  • Anion-exchange Membrane
  • Buffer
  • Optimal Mobile Phase Composition
  • Whey Proteins

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