Bioremediation of chromium in tannery effluent by microbial consortia

Chromium is the most toxic and common among the heavy metal pollutants of industrial effluents. In the present work the chromium remediation ability of Bacillus subtilis, Pseudomonas aeruginosa and Saccharomyces cerevisiae in consortia and in their immobilized forms was studied and their efficiencies were compared. Flame Atomic Absorption Spectroscopy and diphenyl carbazide method was used to quantify chromium in the effluent. The chromium content of the effluent was around 770 mg/l before remediation, after which it reduced to 5.2 – 5.7 mg/l. The best activity was observed by S.cerevisiae - P. aeruginosa consortia, followed by immobilized beads of S. cerevisiae and S. cerevisiae - B. subtilis consortia

Successful data recovery from oscillation photographs containing strong polycrystalline diffraction rings from an unknown small-molecule contaminant: preliminary structure solution of Salmonella typhimurium pyridoxal kinase (PdxK)

Pyridoxal kinase (PdxK; EC 2.7.1.35) belongs to the phosphotransferase family of enzymes and catalyzes the conversion of the three active forms of vitamin B-6, pyridoxine, pyridoxal and pyridoxamine, to their phosphorylated forms and thereby plays a key role in pyridoxal 5 `-phosphate salvage. In the present study, pyridoxal kinase from Salmonella typhimurium was cloned and overexpressed in Escherichia coli, purified using Ni-NTA affinity chromatography and crystallized. X-ray diffraction data were collected to 2.6 angstrom resolution at 100 K. The crystal belonged to the primitive orthorhombic space group P2(1)2(1)2(1), with unitcell parameters a = 65.11, b = 72.89, c = 107.52 angstrom. The data quality obtained by routine processing was poor owing to the presence of strong diffraction rings caused by a polycrystalline material of an unknown small molecule in all oscillation images. Excluding the reflections close to powder/polycrystalline rings provided data of sufficient quality for structure determination. A preliminary structure solution has been obtained by molecular replacement with the Phaser program in the CCP4 suite using E. coli pyridoxal kinase (PDB entry 2ddm) as the phasing model. Further refinement and analysis of the structure are likely to provide valuable insights into catalysis by pyridoxal kinases