色氨酸合酶
吲哚试验
生物化学
酶
色氨酸
ATP合酶
甘油
化学
生物合成
磷酸盐
裂解酶
生物
氨基酸
作者
Lenny Ferrer,Melanie Mindt,María Suárez-Diez,Tatjana Jilg,Maja Zagorščak,Jinho Lee,Kristina Gruden,Volker F. Wendisch,Katarina Cankar
标识
DOI:10.1021/acs.jafc.2c01042
摘要
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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