ABSTRACT
Textile dyeing industries are regarded as one of the most polluting by virtue of the chemicals used and wastewater released. A great deal of chemicals, fasteners, dispersing agents is employed in the stages of dyeing and finishing. The aim of the study was to evaluate scaling and corrosion tendency of polyester textile dyeing effluent using Langelier saturation index (LSI), Ryznar stability index (RSI), and aggressiveness index (AI). The estimation of water stability indices helps in assessing the scaling and corrosive nature of wastewater which in turn facilitates evaluating the condition of the pipelines and valves. Wastewater released from textile dyeing units contains high levels of color (892 ± 20Pt-Co), chemical oxygen demand (2461 ± 48.45 mg/L), electrical conductivity (2906 ± 5.77 µS/cm), and sulfate (6620 ± 7.22 mg/L). The LSI ranged from 2.12 to 3.45, RSI varied from 2.84 to 5.62, and AI varied from 13.67 to 14.99. It was found from the results that the polyester textile dyeing effluent was scaling and non-aggressive. Also, the pipes containing this effluent have to undergo regular maintenance so that they are not blocked by scales which can render financial losses to the industry.
Subject(s)
Wastewater , Water Pollutants, Chemical , Waste Disposal, Fluid/methods , Water Pollutants, Chemical/analysis , Corrosion , Textiles , Textile Industry , Coloring AgentsABSTRACT
Due to high augmentation in population and low availability of land, the quantum of wastewater production has surged resulting in advancements in wastewater treatment systems. To cope under such stressful circumstances, moving bed biofilm reactor (MBBR) proves to be an upgraded treatment technology for industrial and municipal wastewater treatment. The present startup study has been carried out using a laboratory-scale aerobic MBBR with working volume of 25L for textile dye wastewater treatment having AnoxKaldnes K3 media at filling percentage of 50%. In order to acclimatize the microorganisms on textile dye wastewater, the startup of the reactor was carried out using lactose as readily degradable co-substrate with textile dye wastewater in different ratios at hydraulic retention time (HRT) of 24 h. The biofilm on the media was developed in 63 days duration and the reactor attained pseudo-steady state (PSS) in 185 days period. During PSS condition of the MBBR, the maximum chemical oxygen demand (COD) removal efficiency of 92% with mixed liquor suspended solids (MLSS) concentration of 4224 ± 22 mg/L has been achieved. The kinetic study for biodegradation of textile dye wastewater has also been carried out using the Monod growth kinetics. The values of bio-kinetic coefficients of yield of heterotrophic biomass (Y) and endogenous decay coefficient for heterotrophic biomass (Kd) recorded are 0.394 mgVSS/mgCOD.d and 0.087 day-1, respectively. The values of specific substrate removal rate (k), Monod half saturation constant (Ks), and maximum specific growth rate for heterotrophic biomass (µmax) are 0.024 mgCOD/mgVSS.d, 53.203 mg/L, and 0.0095 day-1, respectively, demonstrating the suitability and healthy performance of MBBR for textile dye wastewater treatment.
Subject(s)
Waste Disposal, Fluid , Wastewater , Waste Disposal, Fluid/methods , Biofilms , Kinetics , Bioreactors , TextilesABSTRACT
Several intracellular pathogens have developed diverse strategies to avoid targeting to lysosomes. However, they universally recruit lysosome-associated membrane protein 1 (LAMP1); the mechanism of LAMP1 recruitment remains unclear. Here, we report that a Salmonella effector protein, SipC, specifically binds with host Syntaxin6 through its C terminus and thereby recruits Syntaxin6 and other accessory molecules like VAMP2, Rab6, and Rab8 on Salmonella-containing phagosomes (SCP) and acquires LAMP1 by fusing with LAMP1-containing Golgi-derived vesicles. In contrast, sipC knock-out:SCP (sipC(-):SCP) or sipC(M398K):SCP fails to obtain significant amounts of Syntaxin6 and is unable to acquire LAMP1. Moreover, phagosomes containing respective knock-out Salmonella like sipA(-), sipB(-), sipD(-), sopB(-), or sopE(-) recruit LAMP1, demonstrating the specificity of SipC in this process. In addition, depletion of Syntaxin6 by shRNA in macrophages significantly inhibits LAMP1 recruitment on SCP. Additionally, survival of sipC(-):Salmonella in mice is found to be significantly inhibited in comparison with WT:Salmonella. Our results reveal a novel mechanism showing how Salmonella acquires LAMP1 through a SipC-Syntaxin6-mediated interaction probably to stabilize their niche in macrophages and also suggest that similar modalities might be used by other intracellular pathogens to recruit LAMP1.
Subject(s)
Bacterial Proteins/metabolism , Golgi Apparatus/metabolism , Lysosomal-Associated Membrane Protein 1/metabolism , Phagosomes/metabolism , Phagosomes/microbiology , Qa-SNARE Proteins/metabolism , Salmonella typhimurium/metabolism , Animals , Bacterial Proteins/genetics , Cell Line , Golgi Apparatus/microbiology , Intracellular Space/metabolism , Intracellular Space/microbiology , Macrophages/cytology , Macrophages/metabolism , Macrophages/microbiology , Mice , Mutation , Protein Transport , Salmonella typhimurium/genetics , Salmonella typhimurium/physiology , Substrate SpecificityABSTRACT
Initial characterizations of live-Salmonella-containing early (LSEP) and late phagosomes (LSLP) in macrophages show that both phagosomes retain Rab5 and EEA1. In addition, LSEP specifically contain transferrin receptor whereas LSLP possess relatively more rabaptin-5. In contrast to LSLP, late-Salmonella-containing vacuoles in epithelial cells show significantly reduced levels of Rab5 and EEA1. Subsequent results demonstrate that both phagosomes efficiently fuse with early endosomes (EE). In contrast to LSEP, fusion between LSLP and EE is insensitive to ATPgammaS treatment. Furthermore, LSLP fuses with EE in absence of NEM-sensitive fusion factor (NSF) as well as in the presence of NSF:D1EQ mutant demonstrating that LSLP fusion with EE is NSF independent.
Subject(s)
Endosomes/metabolism , Phagosomes/metabolism , Salmonella/metabolism , Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins/physiology , Adenosine Triphosphate/metabolism , Adenosine Triphosphate/physiology , Cells, Cultured , Endosomes/pathology , Endosomes/physiology , Guanosine 5'-O-(3-Thiotriphosphate)/metabolism , HeLa Cells , Humans , Hydrolysis , Membrane Fusion/physiology , Mutant Proteins/metabolism , Mutant Proteins/physiology , Phagocytosis/physiology , Phagosomes/pathology , Phagosomes/physiology , Salmonella Infections/metabolism , Salmonella Infections/pathology , Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins/genetics , Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins/metabolism , Time FactorsABSTRACT
Phagocytosis is a process by which invading organisms are taken up by macrophages and targeted to the lysosomes, where they are degraded. However, many pathogens modulate this central process of macrophage-mediated killing by inhibiting their transport to the lysosomes through a variety of pathogen-derived mechanisms. Given the importance of Rab proteins in the regulation of intracellular transport pathways, we investigated the role of different host endocytic Rabs on the maturation of Salmonella-containing phagosomes in macrophages. Initially, we have developed a ligand mixing assay to measure the transport of the Salmonella-containing phagosomes to lysosomes. Using this assay we have shown that Salmonella decline their transport to the lysosomes. In order to determine whether inhibition of Salmonella transport to lysosomes is due to their sustained fusion with early endosomes, we have developed an in vitro fusion assay between Salmonella-containing phagosomes and early endosomes. Here, we have discussed how these methodologies are helpful to determine the mechanism of evasion of Salmonella transport to the lysosomes.
Subject(s)
Bacterial Proteins/physiology , Lysosomes/metabolism , Phagosomes/metabolism , Salmonella/metabolism , rab5 GTP-Binding Proteins/metabolism , Animals , Bacterial Proteins/metabolism , Biological Transport/physiology , Endosomes/metabolism , Lysosomes/microbiology , Membrane Fusion , Mice , Salmonella/growth & developmentABSTRACT
Recent studies have shown that phagosome maturation depends on the balance between pro-inflammatory and anti-inflammatory cytokines, indicating that cytokine modulates phagosome maturation. However, the mechanism of cytokine-mediated modulation of intracellular trafficking remains to be elucidated. Here, we have shown that treatment of macrophages with IL-6 specifically induce the expression of Rab5 through the activation of extracellular signal-regulated kinase, whereas IL-12 exclusively upregulate the expression of Rab7 through the activation of p38 MAPK. We have cloned the 5'-flanking regions of the rab5c or rab7 into the promoterless reporter vector. Our results have shown that cells transfected with rab5c chimera are transactivated by IL-6, and IL-12 specifically transactivates cells containing rab7 chimera. Moreover, our results also show that IL-12 induces lysosomal transport, whereas IL-6 stimulates the fusion between early compartments in macrophages and accordingly modulates Salmonella trafficking and survival in macrophages. This is the first demonstration showing that cytokine differentially regulates endocytic trafficking by controlling the expression of appropriate Rab GTPase, and provides insight into the mechanism of cytokine-mediated regulation of intracellular trafficking.