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PubMed1988

Identification of Pseudomonas, Flavobacterium, and Alcaligenes with the API 20 NE system.

The API 20 NE system is designed for the rapid identification of Gram negative rods other than Enterobacteriaceae. It has been compared to conventional methods in the characterization of 404 strains representative of 23 species belonging to 3 genera: Pseudomonas (236 strains), Flavobacterium (133 strains) and Alcaligenes (35 strains). The system consists of 9 enzymatic tests and 12 carbohydrate assimilation tests. A 7-digit numerical profile is obtained by an octal coding of the test results. The strains are identified by comparing the numerical profile to those of species listed in a profile index. The API 20 NE tests showed 99-100% correlation with corresponding conventional methods except in indole production (96.5%) for which we observed 14 false negative reactions in testing F. meningosepticum and CDC groups IIb and IIf. The API 20 NE system presented 94.1% identification to the species level and 96.3% to the genus level in agreement with conventional biochemical methods. Among the correctly identified strains, 7.4% (30) gave an erroneous or unlisted numerical profile in the first version of the Profile Index and required the use of the computer. Among the misidentified strains 2%, (8) were assigned to the right genus but wrong species, 0.7% (3) were placed in the wrong genus and 1% (4) gave a doubtful profile with one or more tests compared to the profiles listed.

Alcaligenes↗
PubMed1987

Comparison of Flavobacterium and Sphingobacterium species by enzyme profiles, with use of pattern recognition of two-dimensional fluorescence data.

Enzyme profiles of eight Flavobacterium species and one Sphingobacterium species were compared after using a two-dimensional fluorescence technique. Enzyme contents and corresponding activities were rapidly determined for whole-cell preparations after incubation with a mixture of preselected fluorogenic substrates. A two-dimensional fluorescence spectrum of the resulting product mixture, measured with a video fluorometer, provided a characteristic "fingerprint" for each organism. Comparison of fluorescent spectra was facilitated by a Fourier-transform-based pattern-recognition algorithm and by a clustering technique involving the Pearson product-moment correlation coefficient. F. multivorum, F. thalpophilum, and S. mizutae formed one cluster; F. indologenes, F. spiritivorum, F. odoratum, and F. balustinum formed a second. F. meningosepticum was intermediate between the first and second cluster, whereas F. breve was different from all other strains examined, based on their spectral dissimilarity indices and correlation coefficients.

Flavobacterium↗
PubMed1985

Purification and characterization of heparinase from Flavobacterium heparinum.

Heparinase (EC 4.2.2.7) isolated from Flavobacterium heparinum was purified to homogeneity by a combination of hydroxylapatite chromatography, repeated gel filtration chromatography, and chromatofocusing. Homogeneity was established by the presence of a single band on both sodium dodecyl sulfate and acid-urea gel electrophoretic systems. Amino acid analysis shows that the enzyme contains relatively high amounts of lysine residues (9%) consistent with its cationic nature (pI 8.5) but contains only 4 cysteine residues/polypeptide. The molecular weight of heparinase was estimated to be 42,900 +/- 1,000 daltons by gel filtration and 42,700 +/- 1,200 daltons by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is very specific, acting only on heparin and heparan monosulfate out of 12 similar polysaccharide substrates tested. It has an activity maximum at pH 6.5 and 0.1 M NaCl and a stability maximum at pH 7.0 and 0.15 M NaCl. The Arrhenius activation energy was found to be 6.3 kcal/mol. However, the enzyme is very sensitive to thermal denaturation and loses activity very rapidly at temperatures over 40 degrees C. Kinetic studies of the heparinase reaction at 37 degrees C gave a Km of 8.04 X 10(-6) M and a Vm of 9.85 X 10(-5) M/min at a protein concentration of 0.5 microgram/ml. By adapting batch procedures of hydroxylapatite and QAE (quaternary aminoethyl)-Sephadex chromatography, gram quantities of heparinase that is nearly free of catalytic enzyme contaminants can be purified in 4-5 h.

Amino Acids↗
PubMed1985

Purification and properties of creatinine iminohydrolase from Flavobacterium filamentosum.

Creatinine iminohydrolase (EC 3.5.4.21), which catalyzes hydrolysis of creatinine to N-methylhydantoin and ammonia, was purified from Flavobacterium filamentosum. The average molecular weight of the purified enzyme was 272,480, and the subunit molecular weight was 44,300. Extensive specificity studies indicated that the enzyme utilized cytosine (Km, 0.62 mM; Vm, 20.1 units/mg) as well as creatinine (Km, 5.00 mM; Vm, 40.4 units/mg) as a substrate. Each was a competitive inhibitor toward hydrolysis of the other compound. Dialysis of creatinine iminohydrolase in the presence of 0.01 M Tris phosphate buffer, pH 7.5, containing 1,10-phenanthroline decreased activity by 98%. Reactivation was accomplished by incubating the apoenzyme in the presence of certain divalent metal chlorides, listed in decreasing order of effectiveness: iron(II), zinc, cobalt(II), cadmium, and nickel. The extent of reactivation depended on the substrate and on which metal ion was added to the apoenzyme. Creatinine to cytosine activity ratios varied from 1:3.75 (iron(II) chloride), to 1:0.9 (zinc chloride), to 1:0.06 (nickel chloride). For different preparations of the holoenzyme that ratio ranged from 1:0.45 to 1:1.10. Variable but significant quantities of zinc and iron were present in all preparations of the purified enzyme.

Aminohydrolases↗
PubMed1979

[Six new serotypes of "Flavobacterium meningosepticum" (author's transl)].

Six new serotypes (G to L) of Flavobacterium meningosepticum are described herein. Cross-reactions between the 12 serotypes, A to L (including the 6 serotypes A to F of Owen and Lapage, 1974) are described. Sixty-six strains isolated in France (61 from Strasbourg) belong to the following serotypes (with number of strains): A (1), F (4), G (51), H (1), I (1), J (6), K (1) and L (1). Use of meningosepticum serotyping is recommended as an epidemiological tool.

Flavobacterium↗
PubMed1983

[An in vitro study of susceptibility of Flavobacterium meningosepticum to antibiotics].

The present study concern in vitro observation on the susceptibility to 20 antibacterial agents of the strains of Flavobacterium meningosepticum from clinical specimens at Juntendo University Hospital during the 1 year period of 1981. The tests for susceptibility of the 144 strains to the drugs were all performed by the serial 2-fold agar plate dilution method on Mueller Hinton agar (Difco), standardized by the Japan Society of Chemotherapy using the Microplanter apparatus with one loop of approximately 10(8) cells/ml. The antibacterial agents tested were as follows: ampicillin, sulbenicillin, piperacillin, mezlocillin, cefazolin, cefmetazole, cefoperazone, cefotaxime, ceftizoxime, kanamycin, gentamicin, tobramycin, amikacin, tetracycline, doxycycline, minocycline, nalidixic acid, pipemidic acid, erythromycin and clindamycin. 1. Thirty-seven per cent of the strains were isolated from sputum, 23% from urine (greater than or equal to 10(5) ml), and 18% from pus and exudate. Only 3 and 2 strains were isolated from cerebrospinal fluid and blood, respectively. 2. A large number of the strains tested were highly resistant to ABPC, SBPC, CEZ, KM, TOB, AMK, PPA and EM, and moderately resistant to PIPC, MZPC, CMZ, CPZ, CTX, CZX, GM, TC and NA. The most of the strains were highly sensitive to MINO, CLDM and DOXY in this order. There was no strain resistant to MINO in this study. 3. The yearly change of the antibacterial activities of DOXY, MINO, CLDM was not significant and 9% of the strains in 1981 were highly resistant to CLDM. The strains resistant to EM were more frequently seen in 1981 than in 1974--1976.

Cephalosporins↗
PubMed1980

[Growth inhibition by phenylalanine and tyrosine--metabolism of phenylalanine in Flavobacterium devorans (author's transl)].

Growth of a chloramphenicol-resistant mutant of Flavobacterium devorans (F. devorans r) was inhibited by L-phenylalanine and L-tyrosine and furthermore by L-tryptophan, 4-amino-benzoate, anthranilate and homogentisate. The inhibitionwas reversed partially by simultaneous addition of aromatic amino acids and 4-amino-benzoate. After cultivating F. devorans r in a glucose-minimal medium containing L-phenylalanine, the metabolites L-tyrosine, 4-hydroxyphenylpyruvate, 4-hydroxyphenylacetate, 4-hydroxybenzaldehyd, 4-hydroxybenzoate, homogentisate and anthranilate were found. Growth inhibition and a hypothetical degrading pathway of phenylalanine are discussed.

Aminobenzoates↗
PubMed1980

[A prephenate dehydratase from Flavobacterium devorans stimulated by aromatic amino acids (author's transl)].

Isolation and properties of prephenate dehydratase from Flavobacterium devorans r are described. The enzyme was enriched 43-fold by ammonium sulfate precipitation, by gel chromatography on ultrogel ACA-34 and by hydrophobic chromatography on decylagarose. The molecular weight was estimated to be 1.35 x 10(5). The enzyme was activated in 1mM solutions of L-tyrosine 4,4-fold, of L-phenylalanine 3.9fold and by L-tryptophan 1.9-fold in 0.02M Tris/HCl buffer at pH 7.7. The Km values were, when adding the activator, at L-tyrosine 1.5 x 10(-5) M, at L-phenylalanine 1.3 x 10(-5) M and at L-tryptophan 1 x 10(-5) M. Regulation of aromatic amino acid is discussed in connection with the prephenate dehydratase.

Chorismate Mutase↗
PubMed1995

Plasmid mediated organophosphate pesticide degradation by Flavobacterium balustinum.

A bacterium capable of degrading methyl parathion, an organophosphorus insecticide into paranitrophenol (as evidenced by TLC) and other metabolites, was isolated from the agricultural soils of Anantapur district, Andhra Pradesh, India. This bacterium, identified as Flavobacterium balustinum was found to harbour an indigenous plasmid of approximately 86 kb in size. The degradative enzyme, parathion hydrolase, was found to be encoded by this plasmid. No enzyme activity was observed in plasmid cured strain.

Biodegradation, Environmental↗
PubMed1994

[Antibiotic treatment for pneumonia caused by Flavobacterium meningosepticum].

Two cases of critical nosocomial pneumonia caused by flavobacterium meningosepticum (FM) were reported and both of them were successfully cured. There were 2 other cases of FM pneumonia reported in Chinese literature previously, but none of them survived. It has been found that the treatment for FM respiratory infection was very difficult because of its resistance to majority of antibiotics, including the third generation cephalosporins. The symptoms of FM pneumonia are similar to those of other gram-negative bacillus pneumonias, such as Klebsiella pneumoniae pneumonia. Definite diagnosis depends principally on etiological examination and clinical manifestations of pneumonia. Cefoperazone, Cefsulodin, Astreonam and Ciprofloxacin are valuable drugs in saving the lives of patients with FM Pneumonia.

Aged↗
PubMed1995

[Studies on elastase from Flavobacterium. I. Strain screening and enzyme purification].

132 strains bacteria secreting extracellular elastase were isolated from soil samples, 5 of them possessed considerably high elastiolytic activity of more than 100 u/ml. The highest-yield strain No. 17-87 was characterized as Flavobacterium odoratum, studies on the condition of elastase production revealed that its optimum carbohydrate and nitrogen source were glucose and casein respectively, and that it could utilize fowl ferther meal and wheat bran to give 80% relative yield. The culture exhibited maximum elastase activity at 26 degrees C for 21 hours, the productivity could be increased when the aeration was improved. The PAGE-homogenous elastase preparation was obtained from the culture broth by (NH4)2SO4 fractionation, DEAE-cellulose column chromatography and gel filtration on Sephadex G-75. The molecular weight was determined to be 21380 by SDS-PAGE, the elastiolytic activity was optimal at pH7.4 and 50 degrees C. The enzyme was stable over the range of pH4.5-9.5 and below 40 degrees C, but the activity was inhibited completely by Fe3+, Zn2+, Cu2+, Cr3+, Co2+, Ni2+, Hg2+, Ag+.

Flavobacterium↗
PubMed1993

Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression.

The genes for Flavobacterium meningosepticum Endo (endoglycosidase) F2 and Endo F3 were cloned, and their nucleotide sequences were determined. The deduced amino acid sequences were verified independently to a large extent by direct peptide microsequencing of 66 and 84% of native Endo F2 and Endo F3, respectively. Structurally, the Endo F2 and Endo F3 genes code for a typically long leader sequence of 45 and 39 amino acids, respectively, and, in both cases, a mature protein of 290 amino acids. Comparative structural analysis demonstrated minimum overall homology (15-30%) between Endo F1, Endo F2, and Endo F3, but revealed distinct clusters of identical residues distributed throughout the entire sequence, which represent motifs for binding and hydrolysis of beta 1,4-di-N-acetylchitobiosyl linkages in complex carbohydrates. The mobility of native Endo F2 and Endo F3 on SDS-polyacrylamide gel electrophoresis, unlike Endo F1, did not correlate with the molecular weights determined from the coding region of the corresponding genes. Mass spectrometry confirmed that Endo F2 and Endo F3 were heterogeneous and contained approximately 4000 and 1200 daltons of mass not accounted for in the gene structure. We presume that Endo F2 and Endo F3 are variably post-translationally modified during secretion by possible linkage to the hydroxyl of serine.

Amino Acid Sequence↗
PubMed1997

[The effect of cefepime on ceftazidime, cefotaxime and imipenem resistant strains of Acinetobacter, Xanthomonas, Pseudomonas, Flavobacterium, Sphingobacterium and on producers of extended spectrum beta-lactamases (ESBL) with resistance transfer].

BACKGROUND: The new cephalosporins with heterocyclic positively charged substituent at position C3 belong to the 4th generation cephalosporins. It is not evident, whereas these antibiotics are effective against cefotaxime-ceftazidime-resistant bacteria. We investigated the efficiency of the cefepime (Maxipime, BMS) against Acinetobacter sp., X. maltophilia, Pseudomonas sp., Flavobacterium sp., Sphingobacterium sp. and against strains with production of ESBL (Extended Spectrum beta-Lactamases) (Enterobacter sp., Citrobacter sp., Klebsiella sp.). METHODS AND RESULTS: We determined the susceptibility of the 54 strains resistant to 50 mg/l and more of ceftazidime. The majority of the strains (35) are susceptible to cefepime and MIC is the range 1.65-3.15 mg/l of cefepime. 17 strains have MIC = 6.25 mg/l. Two strains (one strain P. aeruginosa a one strain K. pneumoniae) were resistant to cefepime and MIC = 12.5 mg/l. The activity of beta-lactamases was determined by quantitative macroiodometric method in one strain of P. cepacia and two strains of Sphingobacterium multivorum. They hydrolyse actively imipenem (they produce metallo-beta-lactamase) and ceftazidime (they are highly resistant to this antibiotic), but cefepime is more slowly hydrolysed than ceftazidime. CONCLUSIONS: At the present time cefepime is effective against ceftazidime-resistant strains in so-called "problematic" species of bacteria. However, it is important to protect its efficiency in the future, this requires its rational use.

Acinetobacter↗
PubMed2004

Psychroflexus tropicus sp. nov., an obligately halophilic Cytophaga-Flavobacterium-Bacteroides group bacterium from an Hawaiian hypersaline lake.

A Gram-negative bacterium designated LA1(T) was isolated from water collected in hypersaline Lake Laysan on Laysan Island in the Northwestern Hawaiian Islands. Cells occurred singly as fine rods to short filaments. Growth in 50 % strength marine broth occurred optimally when the medium contained 7.5-10 % (w/v) NaCl. The major fatty acids in LA1(T) grown at 15 and 30 degrees C were 12-methyl tetradecanoic acid and 13-methyl tetradecanoic acid, respectively. The nucleotide sequence of the 16S rRNA gene showed that LA1(T) belonged in the Cytophaga-Flavobacterium-Bacteroides (CFB) group in the domain Bacteria. The closest described neighbour in terms of 16S rRNA gene sequence identity was Psychroflexus torquis ACAM 623(T) (94.4 % over 1423 bases), an obligate psychrophile from Antarctic sea-ice. The G+C content of 35.0 mol% was consistent with this affiliation. Phenotypic and genotypic analyses, including DNA hybridization, indicated that LA1(T) could be assigned to the genus Psychroflexus but, based on significant differences, including growth at 43 degrees C, it constitutes a novel species, Psychroflexus tropicus sp. nov., for which LA1(T) (=ATCC BAA-734(T)=DSM 15496(T)) is the type strain.

Base Composition↗
PubMed1980

Production of l-Glutamine by a Penicillin-Resistant Mutant of Flavobacterium rigense.

To establish a practical method for the fermentative production of l-glutamine, cultural conditions for the accumulation of a large amounts of l-glutamine were investigated by using Flavobacterium rigense 703, which was previously reported by us as a l-glutamine-producing mutant. As a result, a yield of 25 mg of l-glutamine per ml was obtained after a 48-h cultivation in a medium containing glucose, yeast extract, (NH(4))(2)-fumarate, KH(2)PO(4), K(2)HPO(4), MgSO(4).7H(2)O, and CaCO(3) (pH 6.4). Accumulation of l-glutamine was dependent upon the concentration of (NH(4))(2)-fumarate, and a suboptimum growth at a relatively high concentration of (NH(4))(2)-fumarate was essential for the maximum production of l-glutamine. At the optimum conditions, glutamic acid was formed as a by-product at a concentration of less than 1 mg/ml, but accumulation of the other amino acids was negligible. The product was isolated from the culture broth and readily purified by anion-exchange chromatography. The pure crystals of l-glutamine obtained in an 80% yield were optically and chromatographically pure.

Journal Article↗
PubMed1981

Influence of Nutritional Conditions on Production of l-Glutamine by Flavobacterium rigense.

The nutritional conditions for the production of l-glutamine by Flavobacterium rigense strain 703 were investigated. The optimum concentration of ammonia for achieving the highest yield of l-glutamine (25 mg/ml of broth) was relatively broad, from 0.9 to 1.6%, whereas fumaric acid had a narrow optimum range, near 5.5%. High concentration of inorganic ions such as chloride or sulfate ion clearly inhibited cell growth. Therefore, ammonium salts other than (NH(4))(2)-fumarate were unsuitable for the highest production. The optimum concentration of (NH(4))(2)-fumarate was 7%. To reduce the concentration of fumaric acid in the medium, many substances were evaluated as substitutes. The fumaric acid concentration required for highest l-glutamine yield could not be replaced by any one of the compounds tested. However, part of fumaric acid could be replaced with succinic acid and cupric ion; 4% (NH(4))(2)-fumarate plus 2.5% succinic acid or 5% (NH(4))(2)-fumarate plus 1 mM cupric ion produced results similar to 7% (NH(4))(2)-fumarate in the fermentation medium.

Journal Article↗
PubMed1981

Mechanism of l-Glutamine Production by an l-Glutamine-Producing Mutant of Flavobacterium rigense.

Properties of some enzymes involved in l-glutamine biosynthesis in an l-glutamine-producing mutant of Flavobacterium rigense were examined. Glutamate-oxaloacetate transaminase in the mutant was nearly at the same level as that in the parent strain and was the most active among the enzymes participating in glutamate biosynthesis from alpha-ketoglutarate. Glutamine synthetase formation in the mutant was enhanced by increasing the concentration of (NH(4))(2)-fumarate in the medium, but the activity of this enzyme in the parent strain was very low, and its formation was not influenced by the concentration of (NH(4))(2)-fumarate. Glutaminase formation by both strains was similar and was not influenced by the levels of (NH(4))(2)-fumarate. Glutaminase activity of the mutant was inhibited by ammonia and fumarate. Intracellular amino acids and extracellular free amino acids in the mutant were compared with those of the parent strain. It seems reasonable to conclude that l-glutamine leaks out specifically through the cell membrane of strain 703 and that this specific excretion of l-glutamine probably allows a continuous conversion of l-glutamate to l-glutamine inside the cell.

Journal Article↗