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Use of thermolysin metalloprotein affinity metal chromatography in the decontamination of actinide‐bearing solutions
Author(s) -
Meier Laurel,
Terrell Katisha,
Vincent John B.
Publication year - 1995
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280640206
Subject(s) - thermolysin , chemistry , lanthanide , actinide , inorganic chemistry , aqueous solution , metal ions in aqueous solution , metal , chromatography , ion , organic chemistry , trypsin , enzyme
Thermolysin metalloprotein affinity metal chromatography (MAMC) has been shown to be effective for the removal and concentration of lanthanide and actinide ions from aqueous solution. Using solution of trivalent lanthanide ions of appropriate radii and of Th 4+ and UO 2 2+ions as models, the calciumbinding sites of immobilized thermolysin have shown appreciable potential for the decontamination of actinide‐bearing waster solutions. The zinc‐binding site of the affixed protein may also be used for the removal and concentration of divalent transition metal ions.