Biomedical subjects

W Bae

Publications and source records attributed to W Bae.

12 recordsLinked to original sources

PubMed2005

Comparison of influence of free ammonia and dissolved oxygen on nitrite accumulation between suspended and attached cells.

The shortcut biological nitrogen removal (SBNR) hybrid (suspended cells combined with attached cells) process is an innovative technology that nitrosofies ammonium to nitrite and then denitrifies nitrite to nitrogen gas. Theoretically, this results in a 25% savings of the oxygen needed for nitrification and a 40% of savings in carbon source needed for denitrification. In this study, the influences of free ammonia (FA) and dissolved oxygen (DO) concentrations on nitrite accumulation were investigated to find the optimal operational factors for stable nitrite accumulation over a long period. The maximum specific utilization rates for ammonium (qa) and nitrite (qn) were determined for suspended and attached cells taken from a bench-scale SBNR reactor and a pilot-scale livestock wastewater treatment plant reactor. For the ammonium and nitrite oxidations in both reactors, the attached cells were more resistant to the FA concentration, but were more significantly influenced by the DO concentration than the suspended cells. In addition, the effect of the DO concentration was more significant than that of the FA concentration for both types of cells from both reactors. In this SBNR hybrid system, a simultaneous manipulation of DO concentration (<1.5 mg l(-1)) and FA concentration (10-20 mg l(-1)) was required for maintaining high levels of nitrite accumulation.

Ammonia↗

PubMed2004

Evaluation of predominant reaction mechanisms for the Fenton process in textile dyeing wastewater treatment.

This research quantitatively evaluated the predominant reactions in a large-scale Fenton process that treated dyeing wastewaters and suggested an economical and effective treatment process. Through plant analysis, it was found that a great part of the COD was removed by ferric coagulation. The comparative evaluation of Fenton oxidation and ferric coagulation revealed that ferric coagulation was the predominant mechanism to remove COD and colour. In Fenton oxidation, the removal efficiencies of SCOD and colour were 67.7% and 84.7%, respectively. In ferric coagulation, those of SCOD and colour were 60.8% and 62.0%, respectively. A combined process with iron coagulation/precipitation and Fenton oxidation reduced the hydrogen peroxide dosage by over 40% compared to a conventional dosage.

Coloring Agents↗

PubMed2002

Application of membrane-coupled anaerobic volatile fatty acids fermentor for dissolved organics recovery from coagulated raw sludge.

To investigate the treatment performance of membrane-coupled anaerobic volatile fatty acids fermentor system, the effects of operational parameters for volatile fatty acids production were evaluated through experiments and a mathematical model. The volatile fatty acids recovery ratio was largely affected by the change of hydraulic retention time, reaching its maximum value at 12 hrs. Over the range of hydraulic retention time 8 to 96 hrs, the volatile fatty acids recovery ratio decreased with the increase of hydraulic retention time above 12 hrs, while the ratio of mineralization and gasification increased. Hydraulic retention time and membrane filtration ratio should be maintained less than 1 day and above 0.9, respectively, to attain over 40% of organic materials recovery ratio at 10 days of solids retention time. When the hydrolysis rate constant was 0.01 hr-1, the organic loading rate should be maintained at above 1.0 (kgC/m3/day) to attain over 45% of volatile fatty acids recovery ratio. Based on experimental and simulated results, membrane-coupled anaerobic volatile fatty acids fermentor system was thought to be effective for dissolved organics recovery from coagulated sewage sludge.

Bacteria, Anaerobic↗

PubMed2001

Optimal operational factors for nitrite accumulation in batch reactors.

The environmental factors that affected the accumulation of nitrite in nitrifying reactors were investigated using a mixed culture. A batch reactor with 50 mg-N/l of ammonia was used. The pH, temperature and dissolved oxygen concentration were varied. The concentration of unionized free ammonia also changed with the oxidation of ammonia and the variation of pH and temperature. The accumulation of nitrite was affected sensitively by pH and temperature. A higher nitrite concentration was observed at pH 8-9 or temperature around 30 degrees C. The dissolved oxygen also affected, giving the highest nitrite accumulation at around 1.5 mg/l. These were the favored conditions for nitrite production. The free ammonia concentration influenced the nitrite accumulation also, by inhibiting nitrite oxidation. The inhibition became apparent at a concentration of approximately 4 mg/l or above, but insignificant at below 1 mg/l. Thus, simultaneously high free ammonia concentration and maximum specific ammonia-oxidation rate (above 15 x 10(-3) mg-N/mg-VSS x h) were needed for a significant nitrite accumulation. When the two conditions were met, then the highest accumulation was observed when the ratio of the maximum specific oxidation rate of ammonia to the maximum specific oxidation rate of nitrite (ka/kn) was highest. Under the optimal operating conditions of pH 8, 30 degrees C and 1.5 mg/l of dissolved oxygen, as much as 77% of the removed ammonia accumulated in nitrite.

Algorithms↗

PubMed2001

Genetic engineering of Escherichia coli for enhanced uptake and bioaccumulation of mercury.

Synthetic phytochelatins (ECs) are a new class of metal-binding peptides with a repetitive metal-binding motif, (Glu-Cys)(n)Gly, which were shown to bind heavy metals more effectively than metallothioneins. However, the limited uptake across the cell membrane is often the rate-limiting factor for the intracellular bioaccumulation of heavy metals by genetically engineered organisms expressing these metal-binding peptides. In this paper, two potential solutions were investigated to overcome this uptake limitation either by coexpressing an Hg(2+) transport system with (Glu-Cys)(20)Gly (EC20) or by directly expressing EC20 on the cell surface. Both approaches were equally effective in increasing the bioaccumulation of Hg(2+). Since the available transport systems are presently limited to only a few heavy metals, our results suggest that bioaccumulation by bacterial sorbents with surface-expressed metal-binding peptides may be useful as a universal strategy for the cleanup of heavy metal contamination.

Chelating Agents↗

PubMed2000

Enhanced bioaccumulation of heavy metals by bacterial cells displaying synthetic phytochelatins.

A novel strategy using synthetic phytochelatins is described for the purpose of developing microbial agents for enhanced bioaccumulation of toxic metals. Synthetic genes encoding for several metal-chelating phytochelatin analogs (Glu-Cys)(n)Gly (EC8 (n = 8), EC11 (n = 11), and EC20 (n = 20)) were synthesized, linked to a lpp-ompA fusion gene, and displayed on the surface of E. coli. For comparison, EC20 was also expressed periplasmically as a fusion with the maltose-binding protein (MBP-EC20). Purified MBP-EC20 was shown to accumulate more Cd(2+) per peptide than typical mammalian metallothioneins with a stoichiometry of 10 Cd(2+)/peptide. Cells displaying synthetic phytochelatins exhibited chain-length dependent increase in metal accumulation. For example, 18 nmoles of Cd(2+)/mg dry cells were accumulated by cells displaying EC8, whereas cells exhibiting EC20 accumulated a maximum of 60 nmoles of Cd(2+)/mg dry cells. Moreover, cells with surface-expressed EC20 accumulated twice the amount of Cd(2+) as cells expressing EC20 periplasmically. The ability to genetically engineer ECs with precisely defined chain length could provide an attractive strategy for developing high-affinity bioadsorbents suitable for heavy metal removal.

Bacterial Outer Membrane Proteins↗

PubMed2000

Escherichia coli CspA-family RNA chaperones are transcription antiterminators.

CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone, which is thought to facilitate translation at low temperature by destabilizing mRNA structures. Here we demonstrate that CspA, as well as homologous RNA chaperones CspE and CspC, are transcription antiterminators. In vitro, the addition of physiological concentrations of recombinant CspA, CspE, or CspC decreased transcription termination at several intrinsic terminators and also decreased transcription pausing. In vivo, overexpression of cloned CspC and CspE at 37 degrees C was sufficient to induce transcription of the metY-rpsO operon genes nusA, infB, rbfA, and pnp located downstream of multiple transcription terminators. Similar induction of downstream metY-rpsO operon genes was observed at cold shock, a condition to which the cell responds by massive overproduction of CspA. The products of nusA, infB, rbfA, and pnp-NusA, IF2, RbfA, and PNP-are known to be induced at cold shock. We propose that the cold-shock induction of nusA, infB, rbfA, and pnp occurs through transcription antitermination, which is mediated by CspA and other cold shock-induced Csp proteins.

Adaptation, Biological↗

PubMed1999

Glutathione as a matrix for the synthesis of CdS nanocrystallites

GSH-capped CdS nanocrystallites were synthesized by reacting Cd(II)-GSH with aqueous sodium sulfide using specific initial sulfide/Cd(II) ratios. Spectroscopic analyses of fractions obtained from a size exclusion column showed varying absorption spectra indicating a significant dispersion in size-distribution of nanocrystallites at lower sulfide/Cd(II) ratios. However, size distribution of the nanocrystallites was narrower at initial sulfide/Cd(II) ratios that exceeded 1.0. An ethanol precipitation procedure was used to remove free Cd(II)-GSH complexes and selectively isolate GSH-capped nanocrystallites in a very narrow size range. Size exclusion chromatography indicated similar chemical compositions and overlapping spectral profiles of ethanol-precipitated samples suggesting apparent uniformity in both the size and the cap content. All of the GSH-capped CdS nanocrystallites with varying cap contents degraded p-nitrophenol upon irradiation at 366 nm. However, photocatalytic degradation of p-nitrophenol was significantly higher in samples with higher sulfide/Cd ratio and less capping material. The addition of H2O2 enhanced levels of photo-oxidation of p-nitrophenol.

Journal Article↗

PubMed1999

Characterization of Escherichia coli cspE, whose product negatively regulates transcription of cspA, the gene for the major cold shock protein.

Escherichia coli contains nine members of the CspA protein family from CspA to Cspl. To elucidate the cellular function of CspE, we constructed a delta cspE strain. CspE is highly produced at 37 degrees C. The synthesis level of CspE transiently increased during the growth lag period after dilution of stationary-phase cells into the fresh medium at 37 degrees C. This is consistent with the delta cspE phenotype of the longer growth lag period after dilution. The protein synthesis patterns of the delta cspE strain and the wild-type strain were compared using two-dimensional gel electrophoresis. In the delta cspE strain, the synthesis of a number of proteins at 37 degrees C was found to be altered and cspA was derepressed. The derepression of cspA in the delta cspE strain was at the level of transcription in a promoter-independent fashion but was not caused by stabilization of the cspA mRNA, which was shown to be a major cause of CspA induction after cold shock. In vitro transcription assays demonstrated that both CspE and CspA enhanced transcription pause at the region immediately downstream of the cold box, a putative repressor binding site on the cspA mRNA. In a cell-free protein synthesis system using S-30 cell extracts, CspA production was specifically inhibited by the addition of CspE. These results indicate that CspE functions as a negative regulator for cspA expression at 37 degrees C, probably by interacting with the transcription elongation complex at the cspA cold box region.

Bacterial Proteins↗

PubMed1997

Characteristics of glutathione-capped ZnS nanocrystallites.

The titration of increasing equivalents of inorganic sulfide into preformed Zn-glutathione led to the appearance of UV/VIS spectral features attributable to ZnS nanocrystallites. Glutathione-ZnS complexes upon irradiation caused reduction of methylviologen confirming their semiconductor properties. Size-fractionation of glutathione-ZnS samples on a gel filtration column showed the formation of a range of complexes whose spectral properties were correlated with the sulfide content. The stoichiometry of Zn:glutathione increased from 1:2 to a maximum of about 7:1 as the sulfide/Zn ratios increase from 0 to approximately 1.0 in Zn-glutathione complex indicating up to 14-fold increase in the Zn-binding capacity of glutathione upon sulfide incorporation. Spectral characteristics of GSH-capped ZnS nanocrystallites were significantly influenced by pH and by the stoichiometry of Zn, sulfide and glutathione in the complex. Samples containing least glutathione and highest sulfide showed maximal luminescence at pH 6, whereas those with higher glutathione and lower sulfide content showed maximal luminescence at pH 11.

Chromatography, Gel↗

PubMed1997

Promoter-independent cold-shock induction of cspA and its derepression at 37 degrees C by mRNA stabilization.

The gene for CspA, the major cold-shock protein of Escherichia coli is known to be dramatically induced upon temperature downshift. Here, we report that three-base substitutions around the Shine-Dalgarno sequence in the 159-base 5'-untranslated region of the cspA mRNA stabilizes the mRNA 150-fold, resulting in constitutive expression of cspA at 37 degrees C. This stabilization was found to be at least partially due to resistance against RNase E degradation. The cold-shock induction of cspA was also achieved by exchanging its promoter with the non-cold-shock Ipp promoter. The results presented indicate that the cspA gene is efficiently transcribed even at 37 degrees C. However, the translation of the cspA mRNA is blocked because of its extreme instability at 37 degrees C. The presented results also demonstrate that the cspA gene is constitutively transcribed at all temperatures; however, its expression at 37 degrees C is prevented by destabilizing its mRNA.

Bacterial Proteins↗

PubMed1997

CspA, the major cold shock protein of Escherichia coli, negatively regulates its own gene expression.

When the gene for CspA, the major cold shock protein of Escherichia coli, was disrupted by a novel positive/negative selection method, the deltacspA cells did not show any discernible growth defect at either 37 or 15 degrees C. By two-dimensional gel electrophoresis, total protein synthesis was analyzed after temperature downshift in the deltacspA strain. The production of the CspA homologs CspB and CspG increased, and the duration of their expression was prolonged, suggesting that both CspB and CspG compensate for the function of CspA in the absence of CspA during cold shock adaptation. Interestingly, the production of the 159-base 5'-untranslated region (5'-UTR) of cspA from the chromosomal cspA::cat gene, detected by primer extension, failed to be repressed after cold shock. When an independent system to produce CspA was added to the deltacspA strain, the 5'-UTR production for the cspA::cat gene was significantly reduced compared to that of the deltacspA strain. By examining the expression of translationally fused cspA and cspB genes to lacZ in the deltacspA strain, it was found that cspA is more strongly regulated by CspA than cspB is. We showed that the increased expression of the 5'-UTR of the cspA mRNA in the deltacspA strain occurred mainly at the level of transcription and, to a certain extent, at the level of mRNA stabilization. The mRNA stabilization in the deltacspA strain was observed for other mRNAs, supporting the notion that CspA functions as an mRNA chaperone to destabilize secondary structures in mRNAs.

Artificial Gene Fusion↗