4.7 Article

Fermentative Indole Production via Bacterial Tryptophan Synthase Alpha Subunit and Plant Indole-3-Glycerol Phosphate Lyase Enzymes

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 70, Issue 18, Pages 5634-5645

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.2c01042

Keywords

Corynebacterium glutamicum; indole; indole-3-glycerol phosphate lyase; tryptophan synthase ?-subunit; bioprospecting; fermentative production

Funding

  1. European Union [722361]
  2. Dutch research council (NWO) [053.80.732]
  3. Renewable Resources Scheme (FNR) of the Federal Ministry of Food and Agriculture, Germany [22023517]
  4. Republic of Slovenia, Ministry of Education, Science and Sport (MIZS) [C3330-18-252004]

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Indole, a compound with a characteristic odor, is produced by various organisms in nature and plays a role in food flavor and fragrance industry. Researchers discovered a bacterial enzyme that can synthesize indole, leading to an increase in indole production.
Indole is produced in nature by diverse organisms and exhibits a characteristic odor described as animal, fecal, and floral. In addition, it contributes to the flavor in foods, and it is applied in the fragrance and flavor industry. In nature, indole is synthesized either from tryptophan by bacterial tryptophanases (TNAs) or from indole-3-glycerol phosphate (IGP) by plant indole-3-glycerol phosphate lyases (IGLs). While it is widely accepted that the tryptophan synthase alpha-subunit (TSA) has intrinsically low IGL activity in the absence of the tryptophan synthase beta-subunit, in this study, we show that Corynebacterium glutamicum TSA functions as a bona fide IGL and can support fermentative indole production in strains providing IGP. By bioprospecting additional bacterial TSAs and plant IGLs that function as bona fide IGLs were identified. Capturing indole in an overlay enabled indole production to titers of about 0.7 g L-1 in fermentations using C. glutamicum strains expressing either the endogenous TSA gene or the IGL gene from wheat.

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