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http://dx.doi.org/10.4014/mbl.1901.01013

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)
Publication Information
Microbiology and Biotechnology Letters / v.47, no.2, 2019 , pp. 242-249 More about this Journal
Abstract
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.
Keywords
Indole-3-acetate; aminotransferase; indole-3-pyruvate decarboxylase; indole-3-acetaldehyde dehydrogenase; Corynebacterium glutamicum;
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