• Journal of Microbiology and Biotechnology
• /
• v.11 no.3
• /
• pp.355-361
• /
• 2001

A Chromate tolerant strain of Pseudomonas aeruginosa isolated from the effluent of a tannery showed significant enzymatic activity of chromate reduction. Cells grown in chromate-supplemented medium reduced 8 $\mu\textrm{g}$ chromate/mg protein/h in the presence of NADH/NADPH. The chromate reducing activity was inducible as cells pregrown in chromate showed higher chromate reduction. In contrast, the periplasmic fraction of cells gown in chromate reduce $75\%$ chromate in 4 h and the spheroplast fraction failed to do so, indicating that chromate reductase may be located in the periplasm. The presence of a 30 kDa protein in the periplasmic extracts of cells grown in the presence of chromate, but its absence of the protein in cells grown without chromate, points out a possible role of this protein in chromate reduction.

• Journal of Microbiology and Biotechnology
• /
• v.16 no.6
• /
• pp.855-862
• /
• 2006

Hexavalent chromium ($Cr^{6+}$) is a highly harmful pollutant, which can be detoxified and precipitated through reduction to $Cr^{3+}$. Bacillus megaterium TKW3 previously isolated from chromium-contaminated marine sediments was capable of reducing $Cr^{6+}$ in concomitance with metalloids ($Se^{4+}$, $Se^{6+}$, and $As^{5+}$). Notwithstanding approximately 50% inhibition, it was the first report of simultaneous bacterial reduction of $Cr^{6+}$ and $Se^{4+}$ (to elemental Se). No significant difference was observed among electron donors (glucose, maltose, and mannitol) on $Cr^{6+}$ reduction by B. megaterium TKW3. The reduction was constitutive and determined to be non-plasmid mediated. Peptide mass fingerprints (PMF) revealed a novel aerobic membrane-associated reductase with $Cr^{6+}$-induced expression and specific reductive activity (in nmol $Cr^{6+}$/mg protein/min) of 0.220 as compared with 0.087 of the soluble protein fraction. Respiratory inhibitor $NaN_3$ did not interfere with the reductase activity. Transmission electron microscopy with energy dispersive X-ray (TEM-EDX) analysis confirmed the aggregation of reduced chromium along the intracellular membrane region. Future identification of the N-terminal amino acid sequence of this reductase will facilitate purification and understanding of its enzymatic action.

• Journal of Microbiology and Biotechnology
• /
• v.22 no.4
• /
• pp.547-554
• /
• 2012

Chromium is generated from several industrial processes. It occurs in different oxidation states, but Cr(III) and Cr(VI) are the most common ones. Cr(VI) is a toxic, soluble environmental contaminant. Some bacteria are able to reduce hexavalent chromium to the insoluble and less toxic Cr(III), and thus chromate bioremediation is of considerable interest. An indigenous chromium-reducing bacterial strain, Rb-2, isolated from a tannery water sample, was identified as Ochrobactrum intermedium, on the basis of 16S rRNA gene sequencing. The influence of factors like temperature of incubation, initial concentration of Cr, mobility of bacteria, and different carbon sources were studied to test the ability of the bacterium to reduce Cr(VI) under variable environmental conditions. The ability of the bacterial strain to reduce hexavalent chromium in artificial and industrial sewage water was evaluated. It was observed that the mechanism of resistance to metal was not due to the change in the permeability barrier of the cell membrane, and the enzyme activity was found to be inductive. Intracellular reduction of Cr(VI) was proven by reductase assay using cell-free extract. Scanning electron microscopy revealed chromium precipitates on bacterial cell surfaces, and transmission electron microscopy showed the outer as well as inner distribution of Cr(VI). This bacterial strain can be useful for Cr(VI) detoxification under a wide range of environmental conditions.