Title: | Fermentative indole production via bacterial tryptophan synthase alpha subunit and plant indole-3-glycerol phosphate lyase enzymes |
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Authors: | ID Ferrer, Lenny (Author) ID Mindt, Melanie (Author) ID Suarez-Diez, Maria (Author) ID Jilg, Tatjana (Author) ID Zagorščak, Maja (Author) ID Lee, Jin-Ho (Author) ID Gruden, Kristina (Author) ID Wendisch, Volker F. (Author) ID Cankar, Katarina (Author) |
Files: | URL - Source URL, visit https://pubs.acs.org/doi/10.1021/acs.jafc.2c01042
PDF - Presentation file, download (2,24 MB) MD5: A6FE1B294683FAD26A9E286D6DE976B8
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Language: | English |
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Typology: | 1.01 - Original Scientific Article |
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Organization: | NIB - National Institute of Biology
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Abstract: | 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 α-subunit (TSA) has intrinsically low IGL activity in the absence of the tryptophan synthase β-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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Keywords: | Corynebacterium glutamicum, indole, indole-3-glycerol phosphate lyase, tryptophan synthase α-subunit, bioprospecting, fermentative production |
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Publication status: | Published |
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Publication version: | Version of Record |
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Publication date: | 02.05.2022 |
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Year of publishing: | 2022 |
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Number of pages: | str. 5634-5645 |
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Numbering: | Vol. 70, no. 18 |
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PID: | 20.500.12556/DiRROS-19342 |
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UDC: | 60:632 |
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ISSN on article: | 0021-8561 |
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DOI: | 10.1021/acs.jafc.2c01042 |
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COBISS.SI-ID: | 107216387 |
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Publication date in DiRROS: | 16.07.2024 |
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Views: | 366 |
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Downloads: | 242 |
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