Quality screening of incorrectly folded soluble aggregates from functional recombinant proteins

Soon Bin Kwon, Ji Eun Yu, Jihoon Kim, Hana Oh, Chan Park, Jinhee Lee, Baik L. Seong

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Solubility is the prime criterion for determining the quality of recombinant proteins, yet it often fails to represent functional activity due to the involvement of non-functional, misfolded, soluble aggregates, which compromise the quality of recombinant proteins. However, guidelines for the quality assessment of soluble proteins have neither been proposed nor rigorously validated experimentally. Using the aggregation-prone enhanced green-fluorescent protein (EGFP) folding reporter system, we evaluated the folding status of recombinant proteins by employing the commonly used sonication and mild lysis of recombinant host cells. We showed that the differential screening of solubility and folding competence is crucial for improving the quality of recombinant proteins without sacrificing their yield. These results highlight the importance of screening out incorrectly folded soluble aggregates at the initial purification step to ensure the functional quality of recombinant proteins.

Original languageEnglish
Article number907
JournalInternational journal of molecular sciences
Issue number4
Publication statusPublished - 2019 Feb 2

Bibliographical note

Funding Information:
Acknowledgments: This work was supported by a grant from the National Research Foundation of Korea (2018M3A9H4079358).

Publisher Copyright:
© 2019 by the authors. Licensee MDPI, Basel, Switzerland.

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


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