Degradation of indole via a two-component indole oxygenase system from Enterococcus hirae GDIAS-5

文献类型: 外文期刊

第一作者: Deng, Jun-Jin

作者: Deng, Jun-Jin;Li, Yang;Wang, Zhi-Lin;Deng, Jun-Jin;Li, Jia-Zhou;Hu, Jing-Yi;Han, Xue-ying;Luo, Xiao-Chun;Li, Jia-Zhou

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关键词: Odor management; Indole degradation operon; Two-component oxygenase system; Engineered Escherichia coli; 2-acetaminophenol pathway

期刊名称:JOURNAL OF HAZARDOUS MATERIALS ( 影响因子:13.6; 五年影响因子:12.7 )

ISSN: 0304-3894

年卷期: 2023 年 458 卷

页码:

收录情况: SCI

摘要: Animal farming copiously generates indoles, which contribute to odor and pose a challenge for deodorization. While biodegradation is widely accepted, there is a lack of suitable indole-degrading bacteria for animal husbandry. In this study, we aimed to construct genetically engineered strains with indole-degrading abilities. Enterococcus hirae GDIAS-5 is a highly efficient indole-degrading bacterium, which functions via a monooxygenase YcnE presumably contributes to indole oxidation. However, the efficiency of engineered Escherichia coli expressing YcnE for indole degradation is lower than that of GDIAS-5. To improve its efficacy, the underlying indole-degradation mechanisms in GDIAS-5 were analyzed. An ido operon that responds to a two-component indole oxygenase system was identified. In vitro experiments showed that the reductase component of YcnE, YdgI, can improve the catalytic efficiency. The reconstruction of the two-component system in E. coli exhibited higher indole removal efficiency than GDIAS-5. Furthermore, isatin, the key intermediate metabolite in indole degradation, might be degraded via a novel isatin-acetaminophen-aminophenol pathway involving an amidase whose coding gene is located near the ido operon. The two-component anaerobic oxidation system, upstream degradation pathway, and engineering strains investigated in this study provide important insights into indole degradation metabolism and offer efficient resources for achieving bacterial odor elimination.

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