한국미생물·생명공학회지 (Microbiology and Biotechnology Letters)

  • 제47권2호
  • /
  • Pages.242-249
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  • 2019
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  • 1598-642X(pISSN)
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  • 2234-7305(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
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Production of Indole-3-acetate in Corynebacterium glutamicum by Heterologous Expression of the Indole-3-pyruvate Pathway Genes

  • Kim, Yu-mi (Biotech R&D Center, Amicogen Co.) ;
  • Kwak, Mi-hyang (School of Food Biotechnology and Nutrition, Kyungsung University) ;
  • Kim, Hee-sook (School of Food Biotechnology and Nutrition, Kyungsung University) ;
  • Lee, Jin-ho (School of Food Biotechnology and Nutrition, Kyungsung University)
  • 투고 : 2019.01.29
  • 심사 : 2019.03.08
  • 발행 : 2019.06.28
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초록

Biosynthesis of indole-3-acetate (IAA) from L-tryptophan via indole-3-pyruvate pathway requires three enzymes including aminotransferase, indole-3-pyruvate decarboxylase, and indole-3-acetate dehydrogenase. To establish a bio-based production of IAA, the aspC, ipdC, and iad1 from Escherichia coli, Enterobacter cloacae, and Ustilago maydis, respectively, were expressed under control of the tac, ilvC, and sod promoters in C. glutamicum. Cells harboring ipdC produced tryptophol, indicating that the ipdC product is functional in this host. Analyses of SDS-PAGE and enzyme activity revealed that genes encoding AspC and Iad1 were efficiently expressed from the sod promoter, and their enzyme activities were 5.8 and 168.5 nmol/min/mg-protein, respectively. The final resulting strain expressing aspC, ipdC, and iad1 produced 2.3 g/l and 7.3 g/l of IAA from 10 g/l L-tryptophan, respectively, in flask cultures and a 5-L bioreactor.

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참고문헌

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