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Protein separation using affinity-based reversed micelles

Sun1, Gu, Tong

  • 1Department of Biochemical Engineering, Tianjin University, Tianjin 300072, People's Republic of China, Institute of Applied Biochemistry, Tsukuba University, Tsukuba, Ibaraki 305, Japan, and Department of Chemical Systems and Engineering.

Biotechnology Progress
|June 5, 1999
PubMed
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This study developed an improved reversed micellar extraction technique using Cibacron Blue F3G-A (CB) immobilized on lecithin micelles. Adding Tween 85 significantly enhanced lysozyme separation and purification from complex mixtures.

Area of Science:

  • Biochemical Engineering
  • Separation Science
  • Affinity Chromatography

Background:

  • Reversed micellar two-phase extraction is an emerging protein separation method.
  • Immobilizing affinity ligands enhances selectivity and capacity of reversed micelles.
  • Cibacron Blue F3G-A (CB) is an effective affinity ligand for protein purification.

Purpose of the Study:

  • To immobilize Cibacron Blue F3G-A (CB) onto soybean lecithin reversed micelles.
  • To investigate the affinity partitioning of lysozyme and bovine serum albumin (BSA).
  • To enhance lysozyme solubilization and binding effectiveness using Tween 85.

Main Methods:

  • Two-phase reaction to immobilize CB onto lecithin reversed micelles.
  • Studying lysozyme and BSA partitioning with and without Tween 85.

Related Experiment Videos

  • Langmuir equation to analyze partitioning isotherms and binding constants.
  • Recycling affinity-based reversed micellar phase for purification.

    • Main Results:

    • Tween 85 increased lysozyme solubilization and micellar size, boosting extraction capacity by 42%.
    • CB-lecithin micelles demonstrated size exclusion for BSA, enabling selective lysozyme separation.
    • Recycled affinity-based reversed micellar phase achieved 16-18-fold lysozyme purity increase (60-70%).

    Conclusions:

    • Immobilized CB on lecithin micelles, enhanced by Tween 85, is effective for selective lysozyme separation.
    • This method offers improved capacity and recyclability for protein purification.
    • The technique shows promise for purifying lysozyme from crude biological sources.