Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli

Jin Seung Park, Kyung Yeon Han, Jong A. Song, Keum Young Ahn, Hyuk Seong Seo, Jeewon Lee

Research output: Contribution to journalArticle

7 Citations (Scopus)


Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.

Original languageEnglish
Pages (from-to)1513-1518
Number of pages6
JournalBiotechnology Letters
Issue number10
Publication statusPublished - 2007 Oct 1



  • Escherichia coli proteome
  • Malate dehydrogenase
  • Solubility enhancer
  • Stress response

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Microbiology

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