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Effect and mechanism of Mn2+ on urease activity during anaerobic biological treatment of landfill leachate.
Liu, Hao; Huang, Jian; Zhang, Hua; Xi, Shanshan; Luo, Tao; Jiang, Xinqin.
Afiliación
  • Liu H; School of Environmental and Energy Engineering, Anhui Jianzhu University, 292, Ziyun Rd., Shushan District, Hefei, 230601, Anhui Province, China.
  • Huang J; Anhui Provincial Key Laboratory of Environment Pollution Control and Resource Reuse, Hefei, 230601, China.
  • Zhang H; Anhui Research Academy of Ecological Civilization, Hefei, 230601, China.
  • Xi S; School of Environmental and Energy Engineering, Anhui Jianzhu University, 292, Ziyun Rd., Shushan District, Hefei, 230601, Anhui Province, China.
  • Luo T; Anhui Provincial Key Laboratory of Environment Pollution Control and Resource Reuse, Hefei, 230601, China.
  • Jiang X; Anhui Research Academy of Ecological Civilization, Hefei, 230601, China.
Environ Sci Pollut Res Int ; 31(28): 41290-41300, 2024 Jun.
Article en En | MEDLINE | ID: mdl-38849617
ABSTRACT
As a crucial hydrolytic enzyme, urease plays a vital role in anaerobic biological treatment. It is well-known that manganese ions are abundant in landfill leachate, but their concentration fluctuates significantly. However, few studies have investigated the effect and mechanism of different concentrations of Mn2+ on urease activity during anaerobic biological treatment of landfill leachate. This paper aimed to investigate the effects and mechanisms of different concentrations of Mn2+ on urease activity. The results showed that an appropriate amount of Mn2+ could significantly enhance urease activity, while a high concentration of Mn2+ could inhibit it. Insight into the mechanisms behind this phenomenon, various methods such as Zeta potential, particle size, ultraviolet spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy, and statistical analysis were employed in our study. Research suggested that, on one hand, Mn2+ may form hydrogen bonds with the side chain amino or carboxyl groups of urease amino acid residues, affecting the structure of urease through hydrogen bonding. Additionally, Mn2+ also binds to urease through hydrophobic interactions. On the other hand, the C-OH and C-N functional groups in urease have a strong affinity for Mn2+, and changes in these functional groups can greatly enhance the activity of urease. Furthermore, under the action of high concentrations of Mn2+, while the structure of urease becomes more stable, there is also a steric hindrance phenomenon that affects the substrate from entering the catalytic center. Therefore, studying the mechanism of Mn2+ affecting urease activity has significant biological significance and provides a new perspective for exploring the impact of metals on anaerobic bioprocessing of landfill leachate.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ureasa / Contaminantes Químicos del Agua / Manganeso Idioma: En Revista: Environ Sci Pollut Res Int Asunto de la revista: SAUDE AMBIENTAL / TOXICOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ureasa / Contaminantes Químicos del Agua / Manganeso Idioma: En Revista: Environ Sci Pollut Res Int Asunto de la revista: SAUDE AMBIENTAL / TOXICOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China
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