Biocatalytic lipoprotein bioamphiphile induced treatment of recalcitrant hydrocarbons in petroleum refinery oil sludge through transposon technology.

The present investigation employed transposon technology to enhance the degradation of recalcitrant petroleum hydrocarbons present in petroleum oil sludge by using biosurfactant hyper-producing strain Enterobacter xiangfangensis STP-3. Out of 2500 transposon induced mutants, mutants M and M hyper-produce biocatalytic lipoprotein biosurfactant by1.98 and 2.

Genomic characterization of Enterobacter xiangfangensis STP-3: Application to real time petroleum oil sludge bioremediation.

Sustainable treatment of petroleum oil sludge still remains as a major challenge to petroleum refineries. Bioremediation is the promising technology involving bacteria for simultaneous production of biosurfactant and followed by degradation of petroleum compounds. Complete genomic knowledge on such potential microbes could accentuate its successful exploitation.

Recombinant l-Asparaginase II from subsp. ATCC 393 and Its Anticancer Activity.

l-asparaginases from bacterial origin are employed extensively in leukemic treatment and food industry. The present study focuses on the characterization of the recombinant l-asparaginase II from subsp. ATCC 393 cloned into expression system and purified using Ni-NTA chromatography.

In silico analysis, molecular cloning, expression and characterization of l-asparaginase gene from DSM 20016.

l-Asparaginase is employed in leukaemic treatment and in processing starchy foods. The in silico analysis of DSM 20016 reveals the presence of an l-asparaginase gene with theoretical pI value of 4.99.

Expression and characterization of alkaline protease from the metagenomic library of tannery activated sludge.

Metagenomics has the potential to facilitate the discovery of novel enzymes; however, to date, only a few alkaline proteases have been characterized from environmentally-sourced DNA. We report the identification and characterization of an alkaline serine protease designated as Prt1A from the metagenomic library of tannery activated sludge. Sequence analysis revealed that Prt1A is closely related to S8A family subtilisins with a catalytic triad of Asp, His and Ser.

Direct utilization of waste water algal biomass for ethanol production by cellulolytic Clostridium phytofermentans DSM1183.

Direct bioconversion of waste water algal biomass into ethanol using Clostridium phytofermentans DSM1183 was demonstrated in this study. Fermentation of 2% (w/v) autoclaved algal biomass produced ethanol concentration of 0.52 g L(-1) (solvent yield of 0.

Turning the RING domain protein MdmX into an active ubiquitin-protein ligase.

The related RING domain proteins MdmX and Mdm2 are best known for their role as negative regulators of the tumor suppressor p53. However, although Mdm2 functions as a ubiquitin ligase for p53, MdmX does not have appreciable ubiquitin ligase activity. In this study, we performed a mutational analysis of the RING domain of MdmX, and we identified two distinct regions that, when replaced by the respective regions of Mdm2, turn MdmX into an active ubiquitin ligase for p53.

Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2.

Mdm2 is a member of the RING finger family of ubiquitin ligases and is best known for its role in targeting the tumor suppressor p53 for ubiquitination and degradation. Mdm2 can bind to itself and to the structurally related protein MdmX, and these interactions involve the RING finger domain of Mdm2 and MdmX, respectively. In this study, we performed a mutational analysis of the RING finger domain of Mdm2, and we identified several amino acid residues that are important for Mdm2 to exert its ubiquitin ligase function.