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Tributyl phosphate (TBP), a plasticizer and solvent, is used in nuclear fuel reprocessing, generating TBP wastes laden with residual uranium. A Citrobacter 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. © 1992 Humana Press Inc.

Original publication




Journal article


Applied Biochemistry and Biotechnology

Publication Date





693 - 707