Anthracene degradation involved by antibiotic biosynthesis monooxygenase (ABM) in Comamonas testosteroni

IF 5.4 3区材料科学 Q2 CHEMISTRY, PHYSICAL ACS Applied Energy Materials Pub Date : 2024-03-28 DOI:10.1016/j.ibiod.2024.105790

Miao Xu , Yonghao Liu , Hui Li , Xiao Yang , Weijie Yue , Yu Zhang , Dong Liu , Ming Wu , Dan Wang , Guangming Xiong , Liquan Guo , Kai Song

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Abstract

It is well known that anthracene can cause serious health problems, which is why anthracene biodegradation as a method to reduce health risks has drawn the interest of researchers. However, antibiotic contamination in the environment can seriously affect the biodegradation of anthracene. In the present study, Comamonas testosteroni (CT1) had the highest degradation efficiency of anthracene (88.1%), and was still 46.6% when erythromycin concentration was 1/4MIC (8 μg mL⁻¹). Also, compared to CK, the prokaryotic transcriptome analysis of CT1 in anthracene degradation revealed an up-regulated gene that encodes antibiotic biosynthesis monooxygenase (ABM) in both anthracene and anthracene-erythromycin groups. In addition, compared to strain CT1, the CtABM knockout mutant (CT-M) showed a significant decrease in anthracene degradation efficiency. In contrast, Escherichia coli (E.coli) DH5α transformed with CtABM (EM1) exhibited a faster degradation efficiency than DH5α. Furthermore, the antimicrobial susceptibility test showed that compared to DH5α, EM1 had significant resistance to erythromycin. And the purified recombinant CtABM (rABM) had a specific activity of 2.53 μmol min⁻¹·mg⁻¹ protein based on the oxidation of anthracene at pH 7.5 and 35 °C. Additionally, compositional analysis identified 4-benzyloxy-3-methoxybenzyl alcohol and 4-methylphthalaldehyde as anthracene metabolites by EM1, suggesting a novel anthracene degradation pathway.

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Comamonas testosteroni 中的抗生素生物合成单氧化酶（ABM）参与蒽降解

众所周知，蒽会导致严重的健康问题，因此，蒽的生物降解作为一种降低健康风险的方法引起了研究人员的兴趣。然而，环境中的抗生素污染会严重影响蒽的生物降解。在本研究中，Comamonas testosteroni（CT1）对蒽的降解效率最高（88.1%），当红霉素浓度为 1/4MIC（8 μg mL-1）时，降解效率仍为 46.6%。同时，与 CK 相比，CT1 在蒽降解过程中的原核转录组分析显示，在蒽和蒽-红霉素组中，编码抗生素生物合成单加氧酶（ABM）的基因上调。此外，与 CT1 菌株相比，CtABM 基因敲除突变体（CT-M）的蒽降解效率显著下降。相比之下，转化了 CtABM 的大肠杆菌（E.coli）DH5α（EM1）的蒽降解效率比 DH5α 更快。此外，抗菌药物敏感性测试表明，与 DH5α 相比，EM1 对红霉素有明显的抗药性。纯化的重组 CtABM（rABM）在 pH 7.5 和 35 ℃条件下氧化蒽的特异活性为 2.53 μmol min-1-mg-1 蛋白。此外，成分分析还发现 EM1 的 4-苄氧基-3-甲氧基苄醇和 4-甲基邻苯二甲醛是蒽的代谢产物，这表明蒽的降解途径很新颖。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

ACS Applied Energy Materials Materials Science-Materials Chemistry

CiteScore

10.30

自引率

6.20%

发文量

1368

期刊介绍： ACS Applied Energy Materials is an interdisciplinary journal publishing original research covering all aspects of materials, engineering, chemistry, physics and biology relevant to energy conversion and storage. The journal is devoted to reports of new and original experimental and theoretical research of an applied nature that integrate knowledge in the areas of materials, engineering, physics, bioscience, and chemistry into important energy applications.