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Tributyl phosphate degradation by immobilized cells of aCitrobacter sp.

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Abstract

Tributyl phosphate (TBP), a plasticizer and solvent, is used in nuclear fuel reprocessing, generating TBP wastes laden with residual uranium. ACitrobacter sp. accumulated heavy metals via a phosphohydrolase(s) that precipitated metals with inorganic phosphate liberated from an organic phosphate “donor” molecule (TBP). Mutant analysis suggested that TBP hydrolysis was not attributable to a previously documented acid phosphatase (monoesterase). Purified monoesterase had little activity against phospho di- and triesters, had no requirement for Mg2+ or Mn2+, and was EDTA-resistant. Conversely, TBP cleavage by immobilized cells was enhanced by Mg2+, and ininhibited by Mn2+ and EDTA. A separate phosphotri/diesterase was implicated.

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Authors and Affiliations

  1. Microbiology Unit, Department of Biochemistry, University of Oxford, South Parks Road, 0X1 3QU, Oxford, UK

    S. Owen & B. C. Jeong

  2. Department of Microbiology, University of Reading, London Road, Reading, RG1 5AQ, UK

    P. S. Poole

  3. School of Biological Sciences, University of Birmingham, B15 2TT, Birmingham, UK

    L. E. Macaskie

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  1. S. Owen
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  2. B. C. Jeong
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  3. P. S. Poole
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  4. L. E. Macaskie
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Owen, S., Jeong, B.C., Poole, P.S. et al. Tributyl phosphate degradation by immobilized cells of aCitrobacter sp.. Appl Biochem Biotechnol 34, 693–707 (1992). https://doi.org/10.1007/BF02920590

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