Bacteria-based chemiluminescence sensing system using β-galactosidase under the control of the ArsR regulatory protein of the ars operon

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^-15M. 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. Copyright (C) 1998 Elsevier Science B.V.