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Efficient bioremediation of multiple steroid hormones by halotolerant 17ß-hydroxysteroid dehydrogenase derived from moderately halophilic Pontibacillus chungwhensis HN14.
Yang, Haichen; Qian, Zhihui; Zhang, Shan; Peng, Tao; Li, Jin; Meng, Shanshan; Mao, Aihua; Hu, Zhong.
Afiliación
  • Yang H; Department of Biology, Shantou University, Shantou, Guangdong, 515063, P.R. China.
  • Qian Z; Department of Biology, Shantou University, Shantou, Guangdong, 515063, P.R. China.
  • Zhang S; Department of Biology, Shantou University, Shantou, Guangdong, 515063, P.R. China.
  • Peng T; Department of Biology, Shantou University, Shantou, Guangdong, 515063, P.R. China.
  • Li J; Department of Biology, Shantou University, Shantou, Guangdong, 515063, P.R. China.
  • Meng S; College of Life Sciences, China West Normal University, Nanchong, Sichuan, 637002, China.
  • Mao A; Department of Biology, Shantou University, Shantou, Guangdong, 515063, P.R. China.
  • Hu Z; Department of Biology, Shantou University, Shantou, Guangdong, 515063, P.R. China. ahmao@stu.edu.cn.
World J Microbiol Biotechnol ; 40(10): 296, 2024 Aug 10.
Article en En | MEDLINE | ID: mdl-39122994
ABSTRACT
Steroid hormones exhibit potent endocrine disrupting activity and have been shown to disrupt the equilibrium of aquatic ecosystems and pose a threat to public health through their persistent and carcinogenic effects. Pontibacillus chungwhensis HN14, a moderately halophilic bacterium with the capacity to effectively degrade various polycyclic aromatic hydrocarbons and other organic pollutants, was previously isolated. Additionally, the strain HN14 showed strong environmental adaptability under various environmental stress conditions. In this study, the steroid degradation by strain HN14 was studied for the first time. We demonstrated that strain HN14 could degrade estradiol (E2) to maintain the growth of the strain and could convert E2 to estrone. Additionally, the efficient substrate degradation efficiency of P. chungwhensis HN14 under high salinity and high substrate concentration conditions was demonstrated. Furthermore, a 17ß-hydroxysteroid dehydrogenase, 17ß-HSD(HN14), was identified in strain HN14. Comparative analysis reveals that 17ß-HSD(HN14) shares approximately 38% sequence identity with 17ß-HSDx from Rhodococcus sp. P14. In addition, 100 µg of purified 17ß-HSD(HN14) could effectively convert about 40% of 0.25 mM of E2 within 1 h period, with an enzyme activity of 17.5 U/mg, and catalyze the dehydrogenation of E2 and testosterone at the C-17 position. The characterization of purified enzyme properties reveals that 17ß-HSD(HN14) exhibits exceptional structural robustness and enzymatic efficacy even under high salinity conditions of up to 20%. Overall, this study enhances our comprehension of steroid biodegradation in strain HN14 and contributes novel ideas and theoretical underpinnings for advancing bioremediation technologies targeting steroid pollution in high-saline environments.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Biodegradación Ambiental / Salinidad / 17-Hidroxiesteroide Deshidrogenasas Idioma: En Revista: World J Microbiol Biotechnol Año: 2024 Tipo del documento: Article Pais de publicación: Alemania
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Biodegradación Ambiental / Salinidad / 17-Hidroxiesteroide Deshidrogenasas Idioma: En Revista: World J Microbiol Biotechnol Año: 2024 Tipo del documento: Article Pais de publicación: Alemania