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Bacteria-based Chemiluminescence Sensing System Using β-galactosidase Under The Control Of The ArsR Regulatory Protein Of The Ars Operon
S. Ramanathan, Weiping Shi, B. Rosen, S. Daunert
Published 1998 · Chemistry
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Abstract A highly sensitive and selective sensing system for antimonite and arsenite was developed based on genetically engineered bacteria harboring the plasmid pBGD23. In this plasmid, arsR , the gene encoding for the ArsR regulatory protein of the ars operon, is fused to lacZ , the gene encoding for the reporter enzyme β-galactosidase. The expression of β-galactosidase in E. coli strains bearing pBGD23 is controlled by ArsR, and this can be related to the concentration of antimonite/arsenite employed to induce the production of β-galactosidase in the bacteria. ArsR has a high specificity for antimonite/arsenite, thus conferring the developed sensing system with high selectivity. This was demonstrated by evaluating several oxoanions and soft metals as potential interferents. The concentration of β-galactosidase expressed in the bacteria was monitored by chemiluminescence. Using this sensing system, antimonite can be detected at concentrations as low as 10 −15 M. The importance of the E. coli chromosomal ars operon on the observed response was evaluated by employing a strain of E. coli where the chromosomal ars operon has been deleted.
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