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It is used in dairy products, tea drinks, and fine fragrances due to its distinct floral odor typical of jasmine blossoms. The current production of indole based on isolation from coal tar is non-sustainable and its isolation from plants is often unprofitable due to low yields. To offer an alternative to the conventional production, biosynthesis of indole has been studied recently. A glucose-based indole production was achieved by employing the\n                      <jats:italic>Corynebacterium glutamicum<\/jats:italic>\n                      tryptophan synthase \u03b1-subunit (TrpA) or indole-3-glycerol phosphate lyase (IGL) from wheat\n                      <jats:italic>Triticum aestivum<\/jats:italic>\n                      in a genetically-engineered\n                      <jats:italic>C. glutamicum<\/jats:italic>\n                      strain. In addition, a highly efficient bioconversion process using\n                      <jats:italic>C. glutamicum<\/jats:italic>\n                      heterologously expressing tryptophanase gene (\n                      <jats:italic>tnaA<\/jats:italic>\n                      ) from\n                      <jats:italic>Providencia rettgeri<\/jats:italic>\n                      as a biocatalyst was developed. In this work, de novo indole production from glucose was enabled by expressing the\n                      <jats:italic>P. rettgeri tnaA<\/jats:italic>\n                      in a tryptophan-producing\n                      <jats:italic>C. glutamicum<\/jats:italic>\n                      strain. By metabolic engineering of a\n                      <jats:italic>C. glutamicum<\/jats:italic>\n                      shikimate accumulating base strain, tryptophan production of 2.14 \u00b1 0.02 g L\n                      <jats:sup>-1<\/jats:sup>\n                      was achieved. Introduction of the tryptophanase form\n                      <jats:italic>P. rettgeri<\/jats:italic>\n                      enabled indole production, but to low titers, which could be improved by sequestering indole into the water-immiscible solvent tributyrin during fermentation and a titer of 1.38 \u00b1 0.04 g L\n                      <jats:sup>-1<\/jats:sup>\n                      was achieved. The process was accelerated by decoupling growth from production increasing the volumetric productivity about 4-fold to 0.08 g L\n                      <jats:sup>-1<\/jats:sup>\n                      h\n                      <jats:sup>-1<\/jats:sup>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Key points<\/jats:title>\n                    <jats:p>\n                      \u2022\n                      <jats:italic>Efficient de novo indole production via tryptophanases from glucose<\/jats:italic>\n                    <\/jats:p>\n                    <jats:p>\n                      \u2022\n                      <jats:italic>Increased indole titers by product sequestration and improved precursor supply<\/jats:italic>\n                    <\/jats:p>\n                    <jats:p>\n                      \u2022\n                      <jats:italic>Decoupling growth from production accelerated indole production<\/jats:italic>\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1007\/s00253-023-12397-4","type":"journal-article","created":{"date-parts":[[2023,2,14]],"date-time":"2023-02-14T03:04:30Z","timestamp":1676343870000},"page":"1621-1634","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["De novo tryptophanase-based indole production by metabolically engineered Corynebacterium glutamicum"],"prefix":"10.1007","volume":"107","author":[{"given":"Melanie","family":"Mindt","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lenny","family":"Ferrer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk","family":"Bosch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5149-4192","authenticated-orcid":false,"given":"Katarina","family":"Cankar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Volker F.","family":"Wendisch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2023,2,14]]},"reference":[{"key":"12397_CR1","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1007\/s00253-003-1262-2","volume":"62","author":"N Awano","year":"2003","unstructured":"Awano N, Wada M, Kohdoh A, Oikawa T, Takagi H, Nakamori S (2003) Effect of cysteine desulfhydrase gene disruption on l-cysteine overproduction in Escherichia coli. 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