Bacterial bioreactors for high yield production of recombinant protein

Motoo Suzuki, Rohini Roy, Haiyan Zheng, Nancy Woychik, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

47 Scopus citations


We developed a new bacterial expression system that utilizes a combination of attributes (low temperature, induction of an mRNA-specific endoribonuclease causing host cell growth arrest, and culture condensation) to facilitate stable, high level protein expression, almost 30% of total cellular protein, without background protein synthesis. With the use of an optimized vector, exponentially growing cultures could be condensed 40-fold without affecting protein yields, which lowered sample labeling costs to a few percent of the cost of a typical labeling experiment. Because the host cells were completely growth-arrested, toxic amino acids such as selenomethionine and fluorophenylalanine were efficiently incorporated into recombinant proteins in the absence of cytotoxicity. Therefore, this expression system using Escherichia coli as a bioreactor is especially well suited to structural genomics, large-scale protein expressions, and the production of cytotoxic proteins.

Original languageEnglish (US)
Pages (from-to)37559-37565
Number of pages7
JournalJournal of Biological Chemistry
Issue number49
StatePublished - Dec 8 2006

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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