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

文献类型： 外文期刊

作者： Deng, Jun-Jin 1 ; Hu, Jing-Yi 3 ; Han, Xue-ying 3 ; Li, Yang 1 ; Luo, Xiao-Chun 3 ; Wang, Zhi-Lin 1 ; Li, Jia-Zhou 2 ;

作者机构： 1.Guangdong Acad Agr Sci, Agrobiol Gene Res Ctr, State Key Lab Swine & Poultry Breeding Ind, Guangdong Key Lab Crop Germplasm Resources Preserv, 20 Jinying Rd, Guangzhou 510640, Guangdong, Peoples R China

2.Guangdong Acad Agr Sci, State Key Lab Livestock & Poultry Breeding, Key Lab Anim Nutr & Feed Sci South China, Inst Anim Sci,Minist Agr & Rural Affairs,Guangdong, 1 Dafeng St,Wushan Rd, Guangzhou 510640, Guangdong, Peoples R China

3.South China Univ Technol, Guangzhou Higher Educ Mega Ctr, Sch Biol & Biol Engn, Guangzhou 510006, Guangdong, Peoples R China

4.Guangdong Lab Lingnan Modern Agr Heyuan Subctr, Heyuan 517000, Guangdong, Peoples R China

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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