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<p>Tributyl phosphate (TBP) is a solvent and plasticizer commonly used in nuclear fuel reprocessing plants. However, it poses significant environmental challenges due to its stability, persistence, and unique physicochemical properties. To address this, the present study focuses on the biodegradation of TBP by an organism isolated from soil, capable of utilizing TBP as its sole carbon source. Isolated bacteria (<i>Achromobacter sp. SM123)</i> demonstrated efficient TBP degradation, achieving 96% degradation in 29&#xa0;h following adaptation to butanol. The crude extract contains phosphatase enzyme, responsible for TBP degradation was immobilized onto hydroxyappetite matrix. Various immobilizing parameters were investigated, and storage stability study showed that the immobilized crude extract maintained 69% of its initial activity up to 65&#xa0;days however the free enzyme retained only 27% activity over 23&#xa0;days. The phosphatase activity present in crude extract was confirmed by zymogram analysis as a distinct purple band. This work highlights the potential application of isolated bacteria and its immobilized crude extract which contains phosphatase enzyme activity in the bioremediation of TBP-contaminated environment.</p>

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Isolation of Achromobacter sp. SM123 and immobilization of tributyl phosphate-degrading phosphatase enzyme for bioremediation application

  • 期刊论文

  • 发表日期：

    2026年4月2日

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  • Soumya Mukundan,
  • Jose Savio Melo,
  • Archana Mishra,
  • Kuber Chandra Bhainsa

摘要

Tributyl phosphate (TBP) is a solvent and plasticizer commonly used in nuclear fuel reprocessing plants. However, it poses significant environmental challenges due to its stability, persistence, and unique physicochemical properties. To address this, the present study focuses on the biodegradation of TBP by an organism isolated from soil, capable of utilizing TBP as its sole carbon source. Isolated bacteria (Achromobacter sp. SM123) demonstrated efficient TBP degradation, achieving 96% degradation in 29 h following adaptation to butanol. The crude extract contains phosphatase enzyme, responsible for TBP degradation was immobilized onto hydroxyappetite matrix. Various immobilizing parameters were investigated, and storage stability study showed that the immobilized crude extract maintained 69% of its initial activity up to 65 days however the free enzyme retained only 27% activity over 23 days. The phosphatase activity present in crude extract was confirmed by zymogram analysis as a distinct purple band. This work highlights the potential application of isolated bacteria and its immobilized crude extract which contains phosphatase enzyme activity in the bioremediation of TBP-contaminated environment.