Applied Microbiology and Biotechnology

, Volume 75, Issue 2, pp 347–355 | Cite as

Enhanced stability of heterologous proteins by supramolecular self-assembly

  • Jin-Seung Park
  • Ji-Young Ahn
  • Sung-Hyun Lee
  • Hyewon Lee
  • Kyung-Yeon Han
  • Hyuk-Seong Seo
  • Keum-Young Ahn
  • Bon Hong Min
  • Sang Jun Sim
  • Insung S. Choi
  • Yang Hoon Kim
  • Jeewon Lee
Biotechnologically Relevant Enzymes and Proteins

Abstract

Recently, we reported on the dual function of human ferritin heavy chain (hFTN-H) used for the fusion expression and solubility enhancement of various heterologous proteins: (1) high-affinity interaction with HSP70 chaperone DnaK and (2) formation of self-assembled supramolecules with limited and constant sizes. Especially the latter, the self-assembly function of hFTN-H is highly useful in avoiding the undesirable formation of insoluble macroaggregates of heterologous proteins in bacterial cytoplasm. In this study, using enhanced green fluorescent protein (eGFP) and several deletion mutants of Mycoplasma arginine deiminase (ADI132–410) as reporter proteins, we confirmed through TEM image analysis that the recombinant fusion proteins (hFTN-H::eGFP and hFTN-H::ADI132–410) formed intracellular spherical particles with nanoscale diameter (≈10 nm), i.e., noncovalently cross-linked supramolecules. Surprisingly, the supramolecular eGFP and ADI showed much enhanced stability in bioactivity. That is, the activity level was much more stably maintained for the prolonged period of time even at high temperature, at high concentration of Gdn–HCl, and in wide range of pH. The stability enhancement by supramolecular self-assembly may make it possible to utilize the protein supramolecules as novel means for drug delivery, enzymatic material conversion (biotransformation), protein chip/sensor, etc. where the maintenance of protein/enzyme stability is strictly required.

Keywords

Human ferritin heavy chain Self-assembly Supramolecules Enhanced stability 

Notes

Acknowledgment

This study was supported by a grant (A050750) of the Korea Health 21 R&D Project, Ministry of Health and Welfare, Republic of Korea. This work was also supported by the Korea Science and Engineering Foundation Grant (R01-2005-000-10355-0) and the Korea Research Foundation Grant (KRF-2004-005-D00057).

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Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • Jin-Seung Park
    • 1
  • Ji-Young Ahn
    • 1
  • Sung-Hyun Lee
    • 1
  • Hyewon Lee
    • 1
  • Kyung-Yeon Han
    • 1
  • Hyuk-Seong Seo
    • 1
  • Keum-Young Ahn
    • 1
  • Bon Hong Min
    • 2
  • Sang Jun Sim
    • 3
  • Insung S. Choi
    • 4
  • Yang Hoon Kim
    • 5
  • Jeewon Lee
    • 1
  1. 1.Department of Chemical and Biological Engineering, College of EngineeringKorea UniversitySeoulSouth Korea
  2. 2.Department of Pharmacology, College of MedicineKorea UniversitySeoulSouth Korea
  3. 3.Department of Chemical EngineeringSungkyunkwan UniversitySuwonSouth Korea
  4. 4.Department of ChemistryKorea Advanced Institute of Science and TechnologyTaejonSouth Korea
  5. 5.School of Life ScienceChungbuk National UniversityCheongjuSouth Korea

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