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      Secretion of human epidermal growth factor by Corynebacterium glutamicum.

      Letters in Applied Microbiology
      Blotting, Western, methods, Cell Line, Tumor, Cloning, Molecular, Corynebacterium glutamicum, genetics, metabolism, Electrophoresis, Polyacrylamide Gel, Epidermal Growth Factor, pharmacology, Gene Expression Regulation, Bacterial, Humans, Plasmids, Transformation, Genetic

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          Abstract

          To examine the secretion of human epidermal growth factor (hEGF) by Corynebacterium glutamicum. We recently showed that a novel protein-secretion system in C. glutamicum could produce Streptomyces mobaraensis transglutaminase. In the present study, the industrially important protein hEGF was secreted into the culture medium in a fully active form by C. glutamicum and accumulated at a rate of up to 156 mg l(-1) day(-1). These results demonstrated that the hEGF protein could be secreted in an active form by C. glutamicum. Our data confirmed that the pharmaceutically important human protein hEGF could be efficiently secreted in an active form by the C. glutamicum protein-expression system. Moreover, we demonstrated that this bacterium has potential as a host for the industrial-scale production of human proteins.

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