scholarly journals Indole Pulse Signalling Regulates the Cytoplasmic pH ofE. coliin a Memory-Like Manner

2018 ◽  
Author(s):  
Ashraf Zarkan ◽  
Santiago Caño Muñiz ◽  
Jinbo Zhu ◽  
Kareem Al Nahas ◽  
Jehangir Cama ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Ph Regulation ◽  
Critical Role ◽  
Bacterial Cells ◽  
Cytoplasmic Ph ◽  
E Coli ◽  
Degree Of Protection ◽  
Bacterial Cell Membrane ◽  
Ph Range ◽  
Phase Entry

SUMMARYBacterial cells are critically dependent upon pH regulation. Most proteins function over a limited pH range and the pH gradient across the bacterial cell membrane is central to energy production and transduction1. Here we demonstrate that indole plays a critical role in the regulation of the cytoplasmic pH ofE. coli. Indole is an aromatic molecule with diverse signalling roles that in bacteria is produced from tryptophan by the enzyme tryptophanase (TnaA)2. Two modes of indole signalling have been described: persistent and pulse signalling. The latter is illustrated by the brief but intense elevation of intracellular indole during stationary phase entry3,4. We show thatE. colicells growing under conditions where no indole is produced maintain their cytoplasmic pH at 7.8 ± 0.2. In contrast, under conditions permitting indole production, pH is maintained at 7.2 ± 0.2. Experiments where indole was added experimentally to non-producing cultures showed that pH regulation results from pulse, rather than persistent, indole signalling. Furthermore, the application of an artificial pulse of either of two non-biological proton ionophores (DNP or CCCP) caused a similar effect, suggesting that the relevant property of indole in this context is its ability to conduct protons across the cytoplasmic membrane5. Additionally, we show that the effect of the indole pulse that occurs normally during stationary phase entry in rich medium remains as a “memory” to maintain the correct cytoplasmic pH until entry into the next stationary phase. The indole-mediated reduction in cytoplasmic pH may explain why indole providesE. coliwith a degree of protection against stresses, including some bactericidal antibiotics.

scholarly journals Studies on the disinfection efficiency of hoa sen medical instrument sterilizing equipment at the general, obstetrics and paediatrics hospitals in TraVinh Province

2019 ◽  
Vol 41 (3) ◽  
Author(s):  
Pham Hoang Long ◽  
Nguyen Hoai Chau ◽  
Nguyen Chi Thanh ◽  
Ngo Quoc Buu
Keyword(s):  
Cell Membrane ◽  
Removal Efficiency ◽  
Medical Instrument ◽  
Culture Method ◽  
Aerobic Bacteria ◽  
Bacterial Cells ◽  
E Coli ◽  
Before And After ◽  
Microbiological Criteria ◽  
Bacterial Cell Membrane

This research aims to study on the disinfection efficiency of Hoa Sen medical instrument sterilizing equipment based on the application of ECA technology at General Hospital and Obstetrics and Paediatrics Hospitals in Tra Vinh. Disinfection using ECA technology is a method that does not require the introduction of special oxidizing agents except of water and salt. ECA solution - Anolyte solution has very strong oxidants, which oxidize components such as protein, lipid, etc. (usually of the bacterial cell membrane) that make the cell membrane decomposed, reducing 77−93% of the respiratory ability of bacterial cells, weakening them and eventually being destroyed. Hoa Sen medical instrument sterilizing equipment has a similar construction form as a regular double washing table with two wash basins, wherein one sink with a faucet which produces purified water, while other one has a faucet that gives anolyte solution for sterilization. Both faucets are based on a touch support. At the bottom of the sink an anolyte solution production system was installed. Valorization of the disinfection ability of the Hoa Sen medical instrument sterilizing equipment was based on the determination of the number of microorganisms on the surface of the instrument before and after being soaked with an antiseptic washing table. Microbiological criteria are the number of aerobic bacteria, E. Coli and Coliforms. Analytical samples were quantified by culture method on agar plates. Analysis of total aerobic bacteria, E. Coli and Coliforms bacteria according to Vietnam Standard TCVN 4884:2015, TCVN 6846:2007 and TCVN 6848:2007, respectively. The results showed that bacterial removal efficiency was elevated with a novel Hoa Sen sterilizing equipment anolyte. In laboratory scale, E. Coli and Coliforms bacteria with a density of 105 CFU/mL were completely removed in 30 sec contact with an anolyte solution of 300 mg/L active chlorine concentration. In hospital scale, the removal efficiency of total aerobic bacteria on the surface of medical instruments after surgery was 99% for one minute disinfection time. For E. Coli and Coliforms bacteria, the results of the analysis were not detected in both cases before and after sterilization. 

Synthesis and structure-activity study of quaternary ammonium functionalized β-cyclodextrin-carboxymethylcellulose polymers

2011 ◽  
Vol 63 (12) ◽  
pp. 2827-2832 ◽  
Author(s):  
Danielle Bonenfant ◽  
François-René Bourgeois ◽  
Murielle Mimeault ◽  
Frédéric Monette ◽  
Patrick Niquette ◽  
...  
Keyword(s):  
Quaternary Ammonium ◽  
Antimicrobial Activities ◽  
Bacterial Cells ◽  
Experimental Conditions ◽  
E Coli ◽  
Antimicrobial Efficiency ◽  
Disinfection Process ◽  
Didecyldimethylammonium Chloride ◽  
Low Toxicity ◽  
Bacterial Cell Membrane

Carboxymethylcellulose (CMC) and β-cyclodextrin (β-CD)-based polymers functionalized with two types of quaternary ammonium compounds (QACs), the alkaquat DMB-451 (N-alkyl (50% C14, 40% C12, 10% C10) dimethylbenzylammonium chloride) (DMD-451) named polymer DMB-451, and FMB 1210-8 (a blend of 32 w% N-alkyl (50% C14, 40% C12, 10% C10) dimethylbenzylammonium chloride and 48 w% of didecyldimethylammonium chloride) named polymer FMB 1210-8, were synthethized and characterized by Fourier transform infrared spectroscopy. The antimicrobial activities of these polymers against Eschericia coli were also evaluated at 25 °C in wastewater. The results have indicated that the polymer FMB 1210-8 possesses a high-affinity binding with bacterial cells that induces a rapid disinfection process. Moreover, in the same experimental conditions of disinfection (mixture of 1.0 g of polymer and 100 mL of wastewater), the polymer FMB 1210-8 has a higher antimicrobial efficiency (99.90%) than polymer DMB-451 (92.8%). This phenomenon might be associated to a stronger interaction with bacterial cells due to stronger binding affinity for E. coli cells and greater killing efficiency of the C10 alkyl chains QAC of polymer FMB 1210-8 to disrupt the bacterial cell membrane as compared to N-alkyl (50% C14, 40% C12, 10% C10) dimethylbenzylammonium chloride. Together, these results suggest that the polymer FMB 1210-8 could constitute a good disinfectant against Escherichia coli, which could be advantageously used in wastewater treatments due to the low toxicity of β-CD and CMC, and moderated toxicity of FMB 1210-8 to human and environment.

scholarly journals Modifying TIMER, a slow-folding DsRed derivative, for optimal use in quickly-dividing bacteria

2021 ◽  
Author(s):  
Pavan Patel ◽  
Brendan J. O’Hara ◽  
Emily Aunins ◽  
Kimberly M. Davis
Keyword(s):  
Nitric Oxide ◽  
Cell Division ◽  
Stationary Phase ◽  
Yersinia Pseudotuberculosis ◽  
Fluorescent Protein ◽  
Bacterial Species ◽  
Bacterial Cells ◽  
E Coli ◽  
Slow Growing ◽  
Host Tissues

AbstractIt is now well appreciated that members of pathogenic bacterial populations exhibit heterogeneity in growth rates and metabolic activity, and it is known this can impact the ability to eliminate all members of the bacterial population during antibiotic treatment. It remains unclear which pathways promote slowed bacterial growth within host tissues, primarily because it has been difficult to identify and isolate slow growing bacteria from host tissues for downstream analyses. To overcome this limitation, we have developed a novel variant of TIMER, a slow-folding fluorescent protein, to identify subsets of slowly dividing bacteria within host tissues. The original TIMER folds too slowly for fluorescence accumulation in quickly replicating bacterial species (Escherichia coli, Yersinia pseudotuberculosis), however this TIMER42 variant accumulates signal in late stationary phase cultures of E. coli and Y. pseudotuberculosis. We show TIMER42 signal also accumulates during exposure to sources of nitric oxide (NO), suggesting TIMER42 signal detects growth-arrested bacterial cells. In a mouse model of Y. pseudotuberculosis deep tissue infection, TIMER42 signal is clearly detected, and primarily accumulates in bacteria expressing markers of stationary phase growth. There was not significant overlap between TIMER42 signal and NO-exposed subpopulations of bacteria within host tissues, suggesting NO stress was transient, allowing bacteria to recover from this stress and resume replication. This novel TIMER42 variant represents a new faster folding TIMER that will enable additional studies of slow-growing subpopulations of bacteria, specifically within bacterial species that quickly divide.Author SummaryWe have generated a variant of TIMER that can be used to mark slow-growing subsets of Yersinia pseudotuberculosis, which has a relatively short division time, similar to E. coli. We used a combination of site-directed and random mutagenesis to generate the TIMER42 variant, which has red fluorescent signal accumulation in post-exponential or stationary phase cells. We found that nitric oxide (NO) stress is sufficient to promote TIMER42 signal accumulation in culture, however within host tissues, TIMER42 signal correlates with a stationary phase reporter (dps). These results suggest NO may cause an immediate arrest in bacterial cell division, but during growth in host tissues exposure to NO is transient, allowing bacteria to recover from this stress and resume cell division. Thus instead of indicating a response to host stressors, TIMER42 signal accumulation within host tissues appears to identify slow-growing cells that are experiencing nutrient limitation.

Recruitment of the TolA protein to cell constriction sites in Escherichia coli via three separate mechanisms, and a critical role for FtsWI activity in recruitment of both TolA and TolQ.

2021 ◽  
Author(s):  
Cynthia A. Hale ◽  
Logan Persons ◽  
Piet A. J. de Boer
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Cell Envelope ◽  
Critical Role ◽  
Gram Negative Bacteria ◽  
Bacterial Cells ◽  
Future Studies ◽  
E Coli ◽  
Middle Domain ◽  
Fundamental Biological Process

The Tol-Pal system of Gram-negative bacteria helps maintain integrity of the cell envelope and ensures that invagination of the envelope layers during cell fission occurs in a well-coordinated manner. In E. coli , the five Tol-Pal proteins (TolQ, R, A, B and Pal) accumulate at cell constriction sites in a manner that normally requires the activity of the cell constriction initiation protein FtsN. While septal recruitment of TolR, TolB and Pal also requires the presence of TolQ and/or TolA, each of the the latter two can recognize constriction sites independently of the other system proteins. What attracts TolQ or TolA to these sites is unclear. We show that FtsN attracts both proteins in an indirect fashion, and that PBP1A, PBP1B and CpoB are dispensable for their septal recruitment. However, the β-lactam aztreonam readily interferes with septal accumulation of both TolQ and TolA, indicating that FtsN-stimulated production of septal peptidoglycan by the FtsWI synthase is critical to their recruitment. We also discovered that each of TolA's three domains can recognize division sites in a separate fashion. Notably, the middle domain (TolAII) is responsible for directing TolA to constriction sites in the absence of other Tol-Pal proteins and CpoB, while recruitment of TolAI and TolAIII requires TolQ and a combination of TolB, Pal, and CpoB, respectively. Additionally, we describe the construction and use of functional fluorescent sandwich fusions of the ZipA division protein, which should be more broadly valuable in future studies of the E. coli cell division machinery. IMPORTANCE Cell division (cytokinesis) is a fundamental biological process that is incompletely understood for any organism. Division of bacterial cells relies on a ring-like machinery called the septal ring or divisome that assembles along the circumference of the mother cell at the site where constriction will eventually occur. In the well-studied bacterium Escherichia coli , this machinery contains over thirty distinct proteins. We studied how two such proteins, TolA and TolQ, which also play a role in maintaining integrity of the outer-membrane, are recruited to the machinery. We find that TolA can be recruited by three separate mechanisms, and that both proteins rely on the activity of a well-studied cell division enzyme for their recruitment.

scholarly journals Identification of a Dithiazoline Inhibitor of Escherichia colil,d-Carboxypeptidase A

2005 ◽  
Vol 49 (11) ◽  
pp. 4500-4507 ◽  
Author(s):  
Ellen Z. Baum ◽  
Steven M. Crespo-Carbone ◽  
Barbara Foleno ◽  
Sean Peng ◽  
Jamese J. Hilliard ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stationary Phase ◽  
Phase Behavior ◽  
High Throughput Screening ◽  
Deletion Mutant ◽  
Inhibitory Concentration ◽  
Bacterial Cells ◽  
Carboxypeptidase A ◽  
E Coli ◽  
Bacterial Peptidoglycan

ABSTRACT The enzyme l,d-carboxypeptidase A is involved in the recycling of bacterial peptidoglycan and is essential in Escherichia coli during stationary phase. By high-throughput screening, we have identified a dithiazoline inhibitor of the enzyme with a 50% inhibitory concentration of 3 μM. The inhibitor appeared to cause lysis of E. coli during stationary phase, behavior that is similar to a previously described deletion mutant of l,d-carboxypeptidase A (M. F. Templin, A. Ursinus, and J.-V. Holtje, EMBO J. 18:4108-4117, 1999). As much as a one-log drop in CFU in stationary phase was observed upon treatment of E. coli with the inhibitor, and the amount of intracellular tetrapeptide substrate increased by approximately 33%, consistent with inhibition of the enzyme within bacterial cells. Stationary-phase targets such as l,d-carboxypeptidase A are largely underrepresented as targets of the antibiotic armamentarium but provide potential opportunities to interfere with bacterial growth and persistence.

scholarly journals Tombusvirus p19 captures RNase III-cleaved double-stranded RNAs formed by overlapping sense and antisense transcripts in E. coli

2019 ◽  
Author(s):  
Linfeng Huang ◽  
Padraig Deighan ◽  
Jingmin Jin ◽  
Yingxue Li ◽  
Elaine Lee ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Ectopic Expression ◽  
Antisense Transcription ◽  
Bacterial Cells ◽  
Rnase Iii ◽  
Antisense Transcripts ◽  
E Coli ◽  
Physiological Importance ◽  
Protein Levels ◽  
Bacterial Genes

AbstractAntisense transcription is widespread in bacteria. By base pairing with overlapping sense RNAs, antisense RNAs (asRNA) can form long double-stranded RNAs (dsRNA), which are cleaved by RNase III, a dsRNA endoribonuclease. Ectopic expression of plant tombusvirus p19 in E. coli stabilizes ~21 bp dsRNA RNase III decay intermediates, which enabled us to characterize otherwise highly unstable asRNA by deep sequencing of p19-captured dsRNA and total RNA. dsRNA formed at most bacterial genes in the bacterial chromosome and in a plasmid. The most abundant dsRNA clusters were mostly formed by divergent transcription of sense and antisense transcripts overlapping at their 5’-ends. The most abundant clusters included small RNAs, such as ryeA/ryeB, 4 toxin-antitoxin genes, and 3 tRNAs, and some longer coding genes, including rsd and cspD. The sense and antisense transcripts in abundant dsRNA clusters were more plentiful and had longer half-lives in RNase III mutant strains, suggesting that formation of dsRNAs promoted RNA decay at these loci. However, widespread changes in protein levels did not occur in RNase III mutant bacteria. Nonetheless, some proteins involved in antioxidant responses and glycolysis changed reproducibly. dsRNAs accumulated in bacterial cells lacking RNase III, increasing in stationary phase, and correlated with increased cell death in RNase III mutant bacteria in late stationary phase. The physiological importance of widespread antisense transcription in bacteria remains unclear but it may become important during environmental stress. Ectopic expression of p19 is a sensitive method for identifying antisense transcripts and RNase III cleavage sites in bacteria.

scholarly journals Abstract OR-1: Condensed DNA Architecture in a Nucleoid of Escherichia coli

2021 ◽  
Vol 11 (Suppl_1) ◽  
pp. S7-S7
Author(s):  
Yurii Krupyanskii ◽  
Nataliya Loiko ◽  
Olga Sokolova
Keyword(s):  
Stationary Phase ◽  
Liquid Crystalline ◽  
Environmental Changes ◽  
Dna Condensation ◽  
Bacterial Cells ◽  
E Coli ◽  
Flexible Response ◽  
Bacterial Nucleoid ◽  
As Stress ◽  
Condensed Dna

Background: Bacterial genomic DNA interacts with nucleoid-associated proteins (NAPs) and is located in a highly condensed and functional organized form in the nucleoid of the cell. The structure of the bacterial nucleoid is still awaiting its determination in high resolution. However, recent intensive research showed that condensed DNA in the bacterial nucleoid has a complex, hierarchically organized structure. Such architecture may only exist as a result of dynamic structural rearrangements, which characterize actively growing bacteria. Changes in environmental conditions are perceived by bacteria as stress. In the stationary phase caused by nutrient depletion, energy production processes become inefficient. Bacteria in the stationary phase use an energy-independent mechanism for maintaining an order to protect the DNA: the creation of stable structures, like those in inanimate nature. Cells develop into dormant forms that differ significantly in the structural organization from growing cells. Methods: Electron microscopy and synchrotron radiation diffraction studies were used to reveal distinct forms of DNA condensation in dormant E. coli cells. Results: The study made it possible to find the intracellular nanocrystalline, liquid crystalline, and folded nucleosome-like DNA structures, which were observed and described for the first time. Conclusion: The results of experiments made it possible to visualize the structures of the lower hierarchical tier of DNA compaction in the nucleoid of dormant cells. We hypothesized that the heterogeneity of bacterial cells allows for a flexible response to environmental changes and to surviving stress situations. Multiple types of DNA condensation in the same dormant E. coli cell increase the chances for rapid resumption of growth when conditions turn back to favorable.

scholarly journals Roles of NhaA, NhaB, and NhaD Na+/H+ Antiporters in Survival of Vibrio cholerae in a Saline Environment

2003 ◽  
Vol 185 (4) ◽  
pp. 1236-1244 ◽  
Author(s):  
Katia Herz ◽  
Sophie Vimont ◽  
Etana Padan ◽  
Patrick Berche
Keyword(s):  
Stationary Phase ◽  
Vibrio Cholerae ◽  
Ph Regulation ◽  
Molecular System ◽  
Specific Inhibitor ◽  
Ion Pump ◽  
Quinone Oxidoreductase ◽  
Saline Environment ◽  
E Coli ◽  
Wide Range

ABSTRACT Vibrio cholerae, the causative agent of cholera, is a normal inhabitant of aquatic environments, where it survives in a wide range of conditions of pH and salinity. In this work, we investigated the role of three Na+/H+ antiporters on the survival of V. cholerae in a saline environment. We have previously cloned the Vc-nhaA gene encoding the V. cholerae homolog of Escherichia coli. Here we identified two additional antiporter genes, designated Vc-nhaB and Vc-nhaD, encoding two putative proteins of 530 and 477 residues, respectively, highly homologous to the respective antiporters of Vibrio species and E. coli. We showed that both Vc-NhaA and Vc-NhaB confer Na+ resistance and that Vc-NhaA displays an antiport activity in E. coli, which is similar in magnitude, kinetic parameters, and pH regulation to that of E. coli NhaA. To determine the roles of the Na+/H+ antiporters in V. cholerae, we constructed nhaA, nhaB, and nhaD mutants (single, double, and triple mutants). In contrast to E. coli, the inactivation of the three putative antiporter genes (Vc-nhaABD) in V. cholerae did not alter the bacterial exponential growth in the presence of high Na+ concentrations and had only a slight effect in the stationary phase. In contrast, a pronounced and similar Li+-sensitive phenotype was found with all mutants lacking Vc-nhaA during the exponential phase of growth and also with the triple mutant in the stationary phase of growth. By using 2-n-nonyl-4-hydroxyquinoline N-oxide, a specific inhibitor of the electron-transport-linked Na+ pump NADH-quinone oxidoreductase (NQR), we determined that in the absence of NQR activity, the Vc-NhaA Na+/H+ antiporter activity becomes essential for the resistance of V. cholerae to Na+ at alkaline pH. Since the ion pump NQR is Na+ specific, we suggest that its activity masks the Na+/H+ but not the Li+/H+ antiporter activities. Our results indicate that the Na+ resistance of the human pathogen V. cholerae requires a complex molecular system involving multiple antiporters and the NQR pump.

scholarly journals Introduction of a Carboxyl Group in the First Transmembrane Helix of Escherichia coliF1Fo ATPase Subunit c and Cytoplasmic pH Regulation

2001 ◽  
Vol 183 (5) ◽  
pp. 1524-1530 ◽  
Author(s):  
Phil C. Jones
Keyword(s):  
Ph Regulation ◽  
Transmembrane Helix ◽  
Binding Pocket ◽  
Side Chain ◽  
Ion Binding ◽  
Cytoplasmic Ph ◽  
Wild Type ◽  
Atpase Subunit ◽  
Subunit C ◽  
E Coli

ABSTRACT The multicopy subunit c of the H+-transporting F1Fo ATP synthase of Escherichia coli folds across the membrane as a hairpin of two hydrophobic α helices. The subunits interact in a front-to-back fashion, forming an oligomeric ring with helix 1 packing in the interior and helix 2 at the periphery. A conserved carboxyl, Asp61 in E. coli, centered in the second transmembrane helix is essential for H+ transport. A second carboxylic acid in the first transmembrane helix is found at a position equivalent to Ile28 in several bacteria, some the cause of serious infectious disease. This side chain has been predicted to pack proximal to the essential carboxyl in helix 2. It appears that in some of these bacteria the primary function of the enzyme is H+pumping for cytoplasmic pH regulation. In this study, Ile28was changed to Asp and Glu. Both mutants were functional. However, unlike the wild type, the mutants showed pH-dependent ATPase-coupled H+ pumping and passive H+ transport through Fo. The results indicate that the presence of a second carboxylate enables regulation of enzyme function in response to cytoplasmic pH and that the ion binding pocket is aqueous accessible. The presence of a single carboxyl at position 28, in mutants I28D/D61G and I28E/D61G, did not support growth on a succinate carbon source. However, I28E/D61G was functional in ATPase-coupled H+transport. This result indicates that the side chain at position 28 is part of the ion binding pocket.

scholarly journals Studies on the disinfection efficiency of hoa sen medical instrument sterilizing equipment at the general, obstetrics and paediatrics hospitals in TraVinh Province

2019 ◽  
Vol 41 (3) ◽  
Author(s):  
Pham Hoang Long ◽  
Nguyen Hoai Chau ◽  
Nguyen Chi Thanh ◽  
Ngo Quoc Buu
Keyword(s):  
Cell Membrane ◽  
Removal Efficiency ◽  
Medical Instrument ◽  
Culture Method ◽  
Aerobic Bacteria ◽  
Bacterial Cells ◽  
E Coli ◽  
Before And After ◽  
Microbiological Criteria ◽  
Bacterial Cell Membrane

This research aims to study on the disinfection efficiency of Hoa Sen medical instrument sterilizing equipment based on the application of ECA technology at General Hospital and Obstetrics and Paediatrics Hospitals in Tra Vinh. Disinfection using ECA technology is a method that does not require the introduction of special oxidizing agents except of water and salt. ECA solution - Anolyte solution has very strong oxidants, which oxidize components such as protein, lipid, etc. (usually of the bacterial cell membrane) that make the cell membrane decomposed, reducing 77−93% of the respiratory ability of bacterial cells, weakening them and eventually being destroyed. Hoa Sen medical instrument sterilizing equipment has a similar construction form as a regular double washing table with two wash basins, wherein one sink with a faucet which produces purified water, while other one has a faucet that gives anolyte solution for sterilization. Both faucets are based on a touch support. At the bottom of the sink an anolyte solution production system was installed. Valorization of the disinfection ability of the Hoa Sen medical instrument sterilizing equipment was based on the determination of the number of microorganisms on the surface of the instrument before and after being soaked with an antiseptic washing table. Microbiological criteria are the number of aerobic bacteria, E. Coli and Coliforms. Analytical samples were quantified by culture method on agar plates. Analysis of total aerobic bacteria, E. Coli and Coliforms bacteria according to Vietnam Standard TCVN 4884:2015, TCVN 6846:2007 and TCVN 6848:2007, respectively. The results showed that bacterial removal efficiency was elevated with a novel Hoa Sen sterilizing equipment anolyte. In laboratory scale, E. Coli and Coliforms bacteria with a density of 105 CFU/mL were completely removed in 30 sec contact with an anolyte solution of 300 mg/L active chlorine concentration. In hospital scale, the removal efficiency of total aerobic bacteria on the surface of medical instruments after surgery was 99% for one minute disinfection time. For E. Coli and Coliforms bacteria, the results of the analysis were not detected in both cases before and after sterilization. 

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