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At least 199 records · Page 11Linked to original sources
PubMed1976

Physiological characteristics of chemostatically grown Citrobacter freundii as a function of the specific growth rate and type of nutrient limitation.

Citrobacter freundii was grown aerobically in a chemostat on a mineral medium with galactose or glucose as carbon and energy sources under limitation by carbon or nitrogen source respectively. At various specific growth rates ranging from 7 to 95% mumax the culture in steady state was analysed and growth yield, specific metabolic rate of substrate utilization, intracellular concentration of pyruvate, ATP, ADP, AMP and energy charge were determined and plotted as functions of dilution rate. In all four types of experiments the physiological state of cells remained practically independent of dilution rate up to D=0.6 mumax, and at a given specific growth rate nearly independent on mumax and type of limitation. At approximately D=0.6 mumax, which is close to the maximum output dilution rate Dm, the physiological state of the cells changed: growth yields decreased and intr cellular pyruvate and adenylates concentrations increased. Consequently, in a given medium two dilution rates exist at which growth rate dx/dt is the same but the physiology of the population is quite different.

Adenosine Diphosphate↗
PubMed1978

Instability of the tetrathionate respiratory chain of Citrobacter freundii.

The formate--tetrathionate reductase redox pathway of Citrobacter freundii is associated with the cytoplasmic membrane fraction. A high concentration of phosphate in the buffer used for cell disintegration assists in the preparing of membrane particles capable of efficient tetrathionate respiration. A part of this effect at least may be attributed to the high ionic strength of the buffer.

Cell Fractionation↗
PubMed2001

Cloning, sequence analysis, and characterization of the astA gene encoding an arylsulfate sulfotransferase from Citrobacter freundii.

Arylsulfate sulfotransferase (ASST) transfers a sulfate group from a phenolic sulfate ester to a phenolic acceptor substrate. In the present study, the gene encoding ASST was cloned from a genomic library copy of Citrobacter freundii, subcloned into the vector pGEM3Zf(-) and sequenced. Sequencing revealed two contiguous open reading frames (ORF1 and ORF2) on the same strand and based on amino acid sequence homology, they were designated as astA and dsbA, respectively. The amino acid sequence of astA deduced from C. freundii was highly similar to that of the Salmonella typhimurium, Enterobacter amnigenus, Klebsiella, Pseudomonas putida, and Campylobacter jejuni, encoded by the astA genes. However, the ASST activity assay revealed different acceptor specificities. Using p-nitrophenyl sulfate (PNS) as a donor substrate, alpha-naphthol was found to be the best acceptor substrate, followed by phenol, resorcinol, p-acetaminophen, tyramine and tyrosine.

Amino Acid Sequence↗
PubMed2004

Utilization of aminoaromatic acids by a methanogenic enrichment culture and by a novel Citrobacter freundii strain.

Following incubation of mesophilic methanogenic floccular sludge from a lab-scale upflow anaerobic sludge bed reactor used to treat cattle manure wastewater, a stable 5-aminosalicylate-degrading enrichment culture was obtained. Subsequently, a Citrobacter freundii strain, WA1, was isolated from the 5-aminosalicylate-degrading methanogenic consortium. The methanogenic enrichment culture degraded 5-aminosalicylate completely to CH4, CO2 and NH4+, while C. freundii strain WA1 reduced 5-aminosalicylate with simultaneous deamination to 2-hydroxybenzyl alcohol during anaerobic growth with electron donors such as pyruvate, glucose or serine. When grown on pyruvate, C. freundii WA1 converted 3-aminobenzoate to benzyl alcohol and also reduced benzaldehyde to benzyl alcohol. Pyruvate was fermented to acetate, CO2, H2 and small amounts of lactate, succinate and formate. Less lactate (30%) was produced from pyruvate when C. freundii WA1 grew with 5-aminosalicylate as co-substrate.

Ammonia↗
PubMed1998

Purification and characterization of acid-type phosphatases from a heavy-metal-accumulating Citrobacter sp.

An acid phosphatase from a heavy-metal-accumulating strain of a Citrobacter sp. was resolved into two forms on the basis of their nonbinding (phosphatase I) or binding (phosphatase II) behaviour on the cation-exchange resin SP-Sephadex C50. Both holoenzymes had a molecular mass of 103-108 kDa as determined by Superose Q-6 column chromatography in the presence of 150 mM KCl and a subunit molecular mass of 27 kDa as determined by SDS-PAGE; the enzyme was tetrameric. Both enzymes had a pI approximately 9.0 and were immunologically cross-reactive. There were minor differences in amino acid composition and in peptide maps following tryptic digest. The pH optimum for phosphatases I and II was 5.5 and 6.25, respectively; phosphatase II alone retained activity at pH values up to 9.0. Phosphatase I was more resistant to mechanical shear, gamma-irradiation, high temperature, and toxins (F- and formaldehyde). Glycerol increased the thermostability of both enzymes, particularly the more thermosensitive phosphatase II. Phosphatase II had a lower Km and a lower Vmax for glycerol 2-phosphate hydrolysis. The production of enzyme isoforms is a phenomenon similar to that described previously for the alkaline phosphatase of Escherichia coli, where the isoforms relate to precursive and final processed forms of the enzyme. Acid phosphatase is physiologically distinct, with a role that is still obscure but that may relate to cellular stress responses.

Acid Phosphatase↗
PubMed2001

Nitrate reduction by Citrobacter diversus under aerobic environment.

A new aerobic denitrifier, Citrobacter diversus, was isolated from both nitrification and denitrification sludge. To monitor the variation in the concentration of nitrogen oxides, aerobic denitrification by C. diversus was carried out in a batch reactor. When the nitrate concentration was greater than 180 mg N l(-1), the nitrate reduction rate became stable. The effect of the C/N ratio on the denitrification activity was also investigated. The results showed that the optimum denitrification activity was obtained when the C/N ratio was 4-5. The range of the C/N ratio was higher than that for traditional anoxic denitrification. The effect of the dissolved oxygen concentration was further studied; and it was found that the range of dissolved oxygen concentrations, both for specific growth rates and for specific denitrification rates, was 2-6 mg(-1). From these results, it can be concluded that both the concentration of dissolved oxygen and the C/N ratio are key factors in the aerobic denitrification by C. diversus.

Aerobiosis↗
PubMed1998

Cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002.

The gene coding for 3-methylaspartate ammonia-lyase (3-methylaspartase, MAL, EC 4.3.1.2) from Citrobacter amalonaticus strain YG-1002 (TPU 6323) was cloned onto plasmid pBluescript II KS(+), and the nucleotide sequence of the 1239-bp open reading frame (ORF), consisting of 413 codons, was identified as the mal gene coding for MAL. The predicted polypeptide has 62.5% identity with MAL from the obligate anaerobe, Clostridium tetanomorphum NCIMB 11547. ORF1, which showed 58.6% and 58.8% identities with subunit E of the glutamate mutases of C. tetanomorphum and Clostridium cochlearium respectively, was found in the upstream region of the mal gene. An expression plasmid pMALCA3 (5.4 kb), in which the mal gene was expressed under control of the lac promoter on the vector, was constructed. With feeding of 1 mM isopropyl beta-D-thiogalactopyranoside, the amount of the enzyme in a cell-free extract of the transformant, E. coli JM109/pMALCA3, was elevated to 51,800 units/l culture, which is about 50-fold that of C. amalonaticus strain YG-1002. It was calculated that the enzyme comprised over 40% of the total extractable cellular proteins. The enzyme produced by the E. coli transformant was purified in a crystalline form and shown to be identical to that of the wild-type strain with respect to specific activity, molecular mass, subunit structure, enzymological properties, and N-terminal amino acid sequences.

Amino Acid Sequence↗
PubMed2004

Isolation and characterization of Citrobacter strain HPC255 for broad-range substrate specificity for chlorophenols.

This study aims at development of an approach for selection of strain, which has capability for oxidation of broad-range of chloro-substitute phenols. A multiplex PCR was optimized targeting loci involved in phenol and chlorophenol degradation, which was used to select activated sludge samples and also to assess the degradative genotype of isolates. The isolated strains were screened on the basis of RAPD analysis. In parallel, physiological experiments were carried out with activated sludge samples and isolated bacteria by respirometric analysis. Based on cluster analysis of RAPD pattern and respirometric data, the isolate G20 was selected and identified by using 16S rDNA sequence analysis as Citrobacter freundii strain HPC255. The strain could oxidize different substituted chlorophenol molecules. Such strains could provide the pool of intermediates, which can further be degraded by the associated population, thus helping in maintaining the synergistic association of catabolic activity in activated sludge.

Biodegradation, Environmental↗
PubMed2005

Acid hydrolysis and quantitative determination of total hexosamines of an exopolysaccharide produced by Citrobacter sp.

During the hydrolysis of an exopolysaccharide (EPS) produced by Citrobacter sp., the maximum liberation of hexosamine was obtained with 6 M HCl at 115 degrees C in an autoclave for 1 h. The glycosidic bond energy and degree of acetylation of the hexosamine in EPS were approximately 77 kJ mol(-1) and 61%, respectively. Thermal destruction of the hexosamines and the effect of salt on the hexosamine determination could be minimized under the optimized hydrolytic conditions. Using a modified Elson-Morgan method, maximum total hexosamine concentration was determined to be 3.2 g l(-1) (29% of crude EPS) after 96 h of fed-batch culture.

Acids↗
PubMed2006

Polymeric and compositional properties of novel extracellular microbial polyglucosamine biopolymer from new strain of citrobacter sp. BL-4.

A novel polyglucosamine polymer, PGB-2, was produced extracellularly from a new strain Citrobacter sp. BL-4 using pH-stat fed batch cultivation. It was composed of 97.3% glucosamine and 2.7% rhamnose; its average molecular weight, solubility in 2% acetic acid and viscosity were 20 kDa, 5 g l(-1) and 2.9 cps, respectively. FT-IR and 1H NMR spectra of PGB-2 revealed a close identity with chitosan from crab shells.

Amino Acid Sequence↗
PubMed2006

Molecular cloning of the phytase gene from Citrobacter braakii and its expression in Saccharomyces cerevisiae.

The gene, appA, encoding phytase was cloned from a size-selected genomic library of Citrobacter braakii YH-15 by Southern hybridization using a degenerate probe based on the N-terminal amino acid sequence of the phytase. The deduced amino acid sequence of appA contained the N-terminal RHGXRXP motif and the C-terminal HD motif, which are common in histidine acid phosphatases. It also had significant homology (60% identity) with phytase from Escherichia coli, while the physical mapping analysis of appA revealed that gene organization near appA in C. braakii was similar to that in Salmonella typhimurium genome. C. braakii AppA contained five putative N-glycosylation sites. The recombinant phytases, rAppAEc and rAppASc, were produced in E. coli and Saccharomyces cerevisiae, respectively, with both being fused with C-terminal His-tag. After purification, rAppASc was shown to be hyperglycosylated by Endo-H treatment. It had greater thermostability than the wild type phytase and rAppAEc.

6-Phytase↗
PubMed2001

Long-Term outcome of neonatal Citrobacter koseri (diversus) meningitis treated with imipenem/meropenem and surgical drainage.

Neonatal Citrobacter koseri (diversus) meningitis is often complicated by the formation of brain abscesses and has a poor neurological outcome with seizures, mental retardation and paresis as sequelae in 50% of the cases. As there is emerging resistance to ampicillin, gentamicin and third-generation cephalosporins, we attempted to treat this infection with carbapenems. Carbapenems in combination with cefotaxime and surgical drainage may play an important role in treating C. koseri meningitis.

Carbapenems↗
PubMed2003

Resistance to extended-spectrum cephalosporins and mortality in patients with Citrobacter freundii bacteremia.

BACKGROUND: This study was performed to characterize the clinical features and to identify the risk factors for resistance to extended-spectrum cephalosporins (ESCs) and for mortality in patients with Citrobacter freundii bacteremia. PATIENTS AND METHODS: 105 patients (aged > or = 15 years) with C. freundii bacteremia in 1991-2000 were retrospectively analyzed. RESULTS: Nosocomial acquisition was identified in 78.1% of the patients. Hepatic, biliary and pancreatic disease was the most common underlying disease (65.7%) and the biliary tract was the most common site of infection (50.5%). The overall resistance rate to ESCs was 59.0% and was significantly associated with hepatic, biliary and pancreatic disease, recent surgery and procedure, biliary drainage catheter and previous antibiotic therapy in univariate analysis. However, only previous antibiotic therapy with ESCs (OR = 5.0, 95% CI 1.6-15.7, p = 0.006) and recent surgery or procedure (OR = 3.1, 95% CI 1.1-8.4, p = 0.03) were strong, independent risk factors in multivariate analysis. Mortality directly related to C. freundii bacteremia was 21.9% and there was no difference between cases with resistance and susceptibility to ESCs (19.4% vs 25.6%; p = 0.45). Mortality was significantly associated with rapidly fatal or ultimately fatal underlying disease, a solid tumor, septic shock and polymicrobial bacteremia in univariate analysis. Among patients who had therapeutic surgical procedures, mortality was lower (4.5%, p = 0.04). Multivariate analysis revealed rapidly or ultimately fatal disease, septic shock and polymicrobial bacteremia as independent prognostic factors. CONCLUSION: Biliary infection was the leading cause of C. freundii bacteremia. Previous antibiotic therapy, especially with ESCs, frequently predisposed for resistance to these antibiotics. However, resistance to ESCs was not associated with increased mortality.

Adolescent↗
PubMed1977

L-Asparagainases from Citrobacter freundii.

Three enzymes which catalyze the hydrolysis of L-asparagine have been identified in extracts of Citrobacter freundii. One of these (asparaginase-glutaminase (EC 3.5.1.1) also shows substantial glutaminase activity. This enzyme is extremely labile, is sensitive to inactivation by p-chloromercuribenzoate, and is not protected by dithiothreitol. A second enzyme (asparaginase B) is also sensitive to mercurials but is protected from inactivation by dithiothreitol. This enzyme has a relatively low affinity for L-asparagine (Km = 1.7-10(-3) M). The third enzyme (asparaginase A) is insensitive to inactivation by mercurials, is stable upon long term storage and has a relatively high affinity for L-asparagine (Km = 2.9-10(-5) M). This enzyme has been purified to homogeneity and has a molecular weight of approx. 140 000; the subunit weight being approx. 33 000. The C. freundii asparaginase A produced significant increases in the survival time of C3H/HE mice carrying the 6C3HED lymphoma tumor.

Amino Acids↗
PubMed1979

Resolution of the coenzyme B-12-dependent dehydratases of Klebsiella sp. and Citrobacter freundii.

Diol dehydratase (1,2-propanediol hydro-lyase, EC 4.2.1.28) and glycerol dehydratase (glycerol hydro-lyase, EC 4.2.1.30) are shown to be distinct, separable enzymes that occur individually or together in different strains of Klebsiella sp. Anaerobic growth with propan-1,2-diol induces diol dehydratase alone, whereas glycerol fermentation induces both enzymes in K. pneumoniae ATCC 25955 and in Citrobacter freundii NCIB 3735. The dehydratases can be resolved by polyacrylamide-gel electrophoresis or separated by anion-exchange chromatography alone. Sucrose density gradient centrifugation failed to distinguish the enzymes and indicated a molecular weight of 1.9 . 10(5) for both. The enzymes can be assayed individually, even when present in the same crude extract, using the 67-fold difference in their Km values for coenzyme B-12. For both enzymes inactivation kinetics are observed with glycerol as substrated, and monovalent cations influence both the inactivation rate and catalytic rate of the reaction.

Chromatography, Ion Exchange↗
PubMed1976

A specific cephalosporin-binding protein of Citrobacter freundii.

1. A cephalosporin-binding protein obtained from a strain of Citrobacter freundii was purified to the extent of a single band in analytical and sodium dodecyl sulfate-containing disc electrophoresis. 2. The molecular weight determined by disc electrophoresis was 53 000. 3. The binding protein did not show any beta-lactamase activity at substrate concentrations examined: 6 mM to 100 muM of penicillins and 12 mM to 100 muM of cephalosporins. 4. In gel filtration, [14C]benzylpenicillin was found not to bind to the binding protein. 5. In fluorescence titration, all cephalosporins tested quenched the fluorescence. Association constants of cephalosporins were in the range of 0.8-12-103 M-1, and one binding site was calculated for all cephalosporins tested.

Amino Acids↗
PubMed1988

The structure of the O-specific polysaccharide chain from Citrobacter O23-lipopolysaccharide.

The structure of Citrobacter O23-specific polysaccharide has been shown by sugar and methylation analyses of the native and chemically degraded polysaccharide and by 1H- and 13C-n.m.r. spectroscopy to consist of the tetrasaccharide repeating-units: ----4)-alpha-D-Man-(1----2)-alpha-D-Man-(1----2)-beta-D-Man- (1----3)-alpha-D-GalNAc-(1----, 80% of which are substituted by O-acetyl groups.

Antigens, Bacterial↗
PubMed1983

A new site-specific endodeoxyribonuclease from Citrobacter freundii.

Cfr10 I, a site-specific endonuclease from Citrobacter freundii strain RFL10, was isolated. It recognizes and cleaves the family of related sequences: 5'Pu decreases CCGGPy to generate DNA fragments with 5' tetranucleotide extensions. Cfr10 I may be useful in molecular cloning experiments, especially in conjunction with other enzymes which generate the same terminal extensions.

Base Sequence↗