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PubMed1990

Optimized deglycosylation of glycoproteins by peptide-N4-(N-acetyl-beta-glucosaminyl)-asparagine amidase from Flavobacterium meningosepticum.

Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F(PNGase F) from Flavobacterium meningosepticum is a highly useful enzyme for the structural analysis of N (asparagine)-linked carbohydrate chains derived from glycoproteins. The enzyme was enriched using a published procedure [Tarentino AL, Gomez CM, Plummer TH, Jr (1984) Biochemistry 1985:4665-71; Tarentino AL, Plummer TH, Jr (1987) Methods Enzymol 138:770-78] and further purified by hydrophobic interaction HPLC on a weak hydrophobic TSK-Ether column from which it was eluted by a decreasing gradient of 1.7 M ammonium sulphate in 100 mM sodium phosphate, pH 7.0, containing 5 mM EDTA. To determine the optimal conditions for a complete deglycosylation of glycoproteins by PNGase F, experiments were performed with human alpha 1-acid glycoprotein, because the five complex type carbohydrate chains are quite resistant to enzymic hydrolysis. The influence of different detergents on the enzyme reaction was studied. Complete deglycosylation of human alpha 1-acid glycoprotein was achieved by the use of 60 mU/ml PNGase F in 0.25 M sodium phosphate buffer, pH 8.6, containing 0.2% (w/v) SDS, 20 mM mercaptoethanol and 0.5% Mega-10.

Amidohydrolases↗

PubMed1997

Studies on mercury-detoxicating enzymes from a broad-spectrum mercury-resistant strain of Flavobacterium rigense.

Flavobacterium rigense strain PR2, a broad-spectrum mercury-resistant bacterium abundantly present in soil exhibited multiple metal resistance properties. Mercury resistance was due to the sequential action of two mercury-detoxicating enzymes, organomercurial lyase and mercuric reductase. The levels of these enzyme activities were determined using different mercury compounds as inducers and substrates. Mercuric reductase was partially purified from the bacterium and the physicochemical properties of the enzyme were studied. The effect of several enzyme inhibitors and heavy metal ions on the enzyme activity was also studied.

Bacterial Proteins↗

PubMed1991

The release of heparinase from the periplasmic space of Flavobacterium heparinum by three-step osmotic shock.

Heparinase was released from the periplasmic space of Flavobacterium heparinum by three-step osmotic shock procedure. The procedure involves resuspending exponentially growing cells consecutively into (1) 40% sucrose, (2) 10 mM sodium phosphate, 2 mM magnesium chloride, pH 7, and (3) 10 mM sodium phosphate, 300 mM sodium chloride, 2 mM magnesium chloride, pH 7. Typically, 50-75% of the total heparinase activity is recovered by this procedure with an observed 7-15-fold increase in purity. The majority of heparinase activity is released in the final step of the procedure allowing for resolution from cytoplasmic and nonspecific periplasmic material. F. heparinum cells can be stored in 40% sucrose at 4 degrees C for up to one week without significant losses in recovery yields.

Biotechnology↗

PubMed2005

Survival of Lost River suckers (Deltistes luxatus) challenged with Flavobacterium columnare during exposure to sublethal ammonia concentrations at ph 9.5.

The Lost River sucker (Deltistes luxatus) is a federally listed, endangered species inhabiting the hypereutrophic waters of Upper Klamath Lake in southern Oregon, USA. High pH (> or =10) and elevated ammonia concentrations (> or =1 mg NH(3)-N/L) often occur during blooms of cyanobacteria (Aphanizomenon flos-aquae) in the lake, with major fish kills sometimes following a mid- or late-summer "crash" of the cyanobacterial population. Previous histopathology analyses and bacterial sampling indicated that infections of the pathogenic bacterium Flavobacterium columnare might contribute to the fish kills. We hypothesized that prior exposure to adverse water quality conditions increases the susceptibility of Lost River suckers to F. columnare infections. To test this, we exposed juvenile Lost River suckers to four sublethal ammonia concentrations at pH 9.4 for 62 d. On day 31, fish in half of the aquaria were exposed to F. columnare. As expected, survival of the Lost River suckers decreased in aquaria inoculated with F. columnare. Ninety-four percent of the fish that died were infected by F. columnare in the gills, kidney, or skin, whereas none of the survivors or unexposed control fish was infected. However, contrary to our hypothesis, survival of the fish exposed to F. columnare increased significantly (p < 0.05) as unionized ammonia concentrations increased. Our results suggest that complex interactions can complicate prediction of the responses of fish to concurrent chemical stressors and bacterial pathogens.

Ammonia↗

PubMed1998

Properties of a cold-active protease from psychrotrophic Flavobacterium balustinum P104.

Protease activity was detected in the culture medium of Flavobacterium balustinum P104 grown at 10 degrees C, which was isolated from salmon (Oncorhynchus keta) intestine. The enzyme, designated as CP-70 protease, was purified to homogeneity from the culture broth by ion exchange and gel filtration chromatographyies. The molecular mass of the protease was 70 kDa, and its isoelectric point was close to 3.5. Maximal activity toward azocasein was observed at 40 degrees C and from pH 7.0 to 9.0. The activity was strongly inhibited by phenylmethylsulfonyl fluoride, suggesting that the enzyme is a serine protease. The N-terminal amino acid sequence was Asp-Thr-Arg-Gln-Leu-Leu-Asn-Ala-Asn-Ser-Asp-Leu-Leu- Asn-Thr-Thr-Gly-Asn-Val-Thr-Gly-Leu-Thr-Gly-Ala-Phe-Asn-Gly-Gly-Asn. A search through the database for sequence homology yielded no significant match. The initial cleavage sites for oxidized insulin B-chain were found to be the Glu13-Ala14 and Phe24-Phe25 bonds. The result of the cleavage pattern of oxidized insulin B-chain suggests that CP-70 protease has a broader specificity than the other cold-active proteases against the peptide substrate.

Amino Acid Sequence↗

PubMed2006

Isolation and characterization of a cold-active xylanase enzyme from Flavobacterium sp.

Xylan is the major component of hemicellulose, and xylan should be fully utilized to improve the efficiencies of a biobased economy. There are a variety of industrial reaction conditions in which an active xylanase enzyme would be desired. As a result, xylanase enzymes with different activity profiles are of great interest. We isolated a xylanase gene (xyn10) from a Flavobacterium sp. whose sequence suggests that it is a glycosyl hydrolase family 10 member. The enzyme has a temperature optimum of 30 degrees C, is active at cold temperatures, and is thermolabile. The enzyme has an apparent Km of 1.8 mg/ml and kcat of 100 sec-1 for beechwood xylan, attacks highly branched native xylan substrates, and does not have activity against glucans.

Amino Acid Sequence↗

PubMed2006

Genome and proteome characterization of the psychrophilic Flavobacterium bacteriophage 11b.

Virion DNA of bacteriophage 11b (Phi11b), which infects a psychrophilic Flavobacterium isolate from Arctic sea-ice, was determined to consist of 36,012 bp. With 30.6% its GC content corresponds to that of host-genus species and is the lowest of all phages of Gram-negative bacteria sequenced so far. Similarities of several of 65 predicted ORFs, genome organization and phylogeny suggest an affiliation to 'mesophilic' nonmarine siphoviruses, e.g. to bacteriophages SPP1 and HK97. Early genes presumably encode an essential recombination factor (ERF), a single strand binding (SSB) protein, an endonuclease, and a DNA methylase. The late gene segment is likely to contain a terminase, portal, minor head, protease and a major capsid gene. Five ORFs exhibited similarities to Bacteroidetes species and seem to reflect the host specificity of the phage. Among PAGE-separated virion proteins that were identified by MALDI-ToF mass spectrometry are the portal, the major capsid, and a putative conserved tail protein. The Phi11b genome is the first to be described of a cultivated virus infecting a psychrophilic host as well as a Bacteroidetes bacterium.

Arctic Regions↗

PubMed2006

A cold-active and thermostable alcohol dehydrogenase of a psychrotorelant from Antarctic seawater, Flavobacterium frigidimaris KUC-1.

An NAD(+)-dependent alcohol dehydrogenase of a psychrotorelant from Antarctic seawater, Flavobacterium frigidimaris KUC-1 was purified to homogeneity with an overall yield of about 20% and characterized enzymologically. The enzyme has an apparent molecular weight of 160k and consists of four identical subunits with a molecular weight of 40k. The pI value of the enzyme and its optimum pH for the oxidation reaction were determined to be 6.7 and 7.0, respectively. The enzyme contains 2 gram-atoms Zn per subunit. The enzyme exclusively requires NAD(+) as a coenzyme and shows the pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of NAD(+). F. frigidimaris KUC-1 alcohol dehydrogenase shows as high thermal stability as the enzymes from thermophilic microorganisms. The enzyme is active at 0 to over 85 degrees C and the most active at 70 degrees C. The half-life time and k (cat) value at 60 degrees C were calculated to be 50 min and 27,400 min(-1), respectively. The enzyme also shows high catalytic efficiency at low temperatures (0-20 degrees C) (k(cat)/K(m) at 10 degrees C; 12,600 mM(-1)min(-1)) similar to other cold-active enzymes from psychrophiles. The alcohol dehydrogenase gene is composed of 1,035 bp and codes 344 amino acid residues with an estimated molecular weight of 36,823. The sequence identities were found with the amino acid sequences of alcohol dehydrogenases from Moraxella sp. TAE123 (67%), Pseudomonas aeruginosa (65%) and Geobacillus stearothermophilus LLD-R (56%). This is the first example of a cold-active and thermostable alcohol dehydrogenase.

Alcohol Dehydrogenase↗

PubMed2004

Beta-carotene production by Flavobacterium multivorum in the presence of inorganic salts and urea.

Flavobacterium multivorum, a non-fermenting Gram-negative bacteria, normally produces zeaxanthin (3R, 3' R-beta, beta-carotene-3, 3' diol) as its main carotenoid. The effect of supplementation of various inorganic salts and urea on the growth, total carotenoid production, and proportion of beta-carotene (beta, beta-carotene), beta-cryptoxanthin (beta, beta-caroten-3-ol), and zeaxanthin produced by F. multivorum was investigated. Urea and several salts, such as calcium chloride, ammonium chloride, lithium chloride, and sodium carbonate, improved total carotenoid production by 1.5- to 2.0-fold. Urea and sodium carbonate had an unexpectedly strong positive effect on beta-carotene production at the expense of zeaxanthin formation. The effect was found to be independent of incubation time, and beta-carotene represented 70% (w/w) of the total carotenoid content. The cumulative effect of urea and sodium carbonate was further studied using response surface methodology. An optimum medium was found to contain 4,000 and 4,070 mg l(-1) urea and sodium carbonate, respectively. The maximum beta-carotene level was 7.85 microg ml(-1) culture broth, which represented 80% (w/w) of the total carotenoid produced. Optimization resulted in 77- and 88-fold improvements in the volumetric and specific beta-carotene levels, respectively, accompanied by a simultaneous decrease in the zeaxanthin level as compared to the control medium. The carotenoid production profile in the optimized medium indicated that beta-carotene was produced maximally during the late exponential phase at 0.41 microg ml(-1) h(-1). It is possible that this organism could be an excellent commercial source of either beta-carotene or zeaxanthin, depending on initial culture conditions.

Culture Media↗

PubMed2005

Production of deuterated zeaxanthin by Flavobacterium multivorum and its detection by resonance Raman and mass spectrometric methods.

Flavobacterium multivorum, a zeaxanthin-producing organism, was grown aerobically in a medium prepared with deuterated water. Atmospheric pressure chemical ionization mass spectrometry (APCI-MS) and resonance Raman spectroscopy (RRS) analysis revealed approximately 75% replacement of hydrogen by deuterium atoms as indicated by the molecular mass cluster at around m/z 600. Deuterated zeaxanthin upon excitation with a 488 nm laser exhibited characteristic resonance Raman vibrational modes at 1,161 and 1,504 cm(-1) as compared to 1,007, 1,159 and 1,525 cm(-1 )for undeuterated zeaxanthin. HPLC/APCI-MS and HPLC/RRS were specific and sensitive with limits of detection of 2.5 pg and 50 ng, respectively.

Deuterium Oxide↗

PubMed1983

Purification and characterization of an extracellular protease from Flavobacterium arborescens.

An extracellular protease from Flavobacterium arborescens has been purified to an apparent homogeneity and characterized. The enzyme is most active at pH 8-10.5, requires no metal cofactor, and is inhibited by diisopropyl fluorophosphate. The protease is nonspecific, is active at temperatures up to 60 degrees C, and is completely free of nucleases. The ease of purification and freedom from nucleolytic contaminants make the protease a useful deproteinizing agent in DNA and RNA manipulations.

Centrifugation, Density Gradient↗

PubMed1975

Purification and properties of a beta-1,6-clucosidase from Flavobacterium.

An intracellular beta-1,6-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) was produced semiconstitutively by Flavobacterium M64. This enzyme was purified 180-fold by fractionation with ammonium sulfate followed by chromatographies on carboxymethylcellulose, hydroxyapatite and Sephadex G-100. The final preparation appeared homogeneous on disc electrophoresis on polyacrylamide gel. The molecular weight of the enzyme was determined to be ca. 59 000 by Sephadex G-100 gel filtration and sodium dodecylsulfate-polyacrylamide gel electrophoresis. The optimum pH of the enzyme was 5.8 and the optimum temperature was 40 degrees C. The enzyme readily hydrolyzed oligomers with beta-a,6-glucosidic linkages, converting them to glucose. The Km values for gentio-biose, -triose, -tetraose and -pentaose were 2.8, 3.0, 4.2 and 4.6 times 10- minus 4 M, respectively. The rates of their hydrolyses decreased with increase in their chain lengths. The enzyme was concluded to be a beta-1,6-glucosidase from its substrate specificity, production of glucose, transferring ability and inhibition by glucono-delta-lactone. The enzyme activity was inhibited by Hg-2+, Cu-2+, Ag-+, Fe-3+, p-chloromercuribenzoate, N-ethylmaleimide, glucose and trishydroxyaminomethane (Tris) but not by ethylenediaminetetraacetic acid.

Chromatography↗

PubMed1996

Platelet lysis and functional perturbation by 13-methyl myristate. The major fatty acid in Flavobacterium ranacida.

Flavobacterium ranacida consisted of 75% of 13-methyl myristate in total fatty acids. The acid at > 60 microM caused the lysis of gel-filtered platelets (GFP) in both time- and concentration-dependent manners. Scanning electron microscopy showed that: 1). GFP in 40 microM of the acid changed the morphology to speculate discoid shape at 15 sec, and to ellipsoids after 30 sec; and 2), the cells gradually swelled to spherical forms as the concentration of the acid increased. At nonlytic concentration, the acid inhibited platelet responses to various agonists with differential concentrations. The order of inhibitory potency was U46619 > low dose collagen > ADP-fibrinogen > phorbol ester > high dose collagen. The results demonstrated that 13-methyl myristate exhibited both cell lytic activity and perturbation on membrane function.

15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5↗

PubMed1983

Meningitis caused by Flavobacterium meningosepticum after transsphenoidal hypophysectomy with recovery.

Adult meningitis caused by Flavobacterium meningosepticum is rare. Five cases have been reported in the literature. The case reported herein developed in a woman after a transsphenoidal hypophysectomy. The isolate was resistant to erythromycin. Treatment with oral rifampicin combined with intravenous chloramphenicol and cefoperazone resulted in complete recovery.

Anti-Bacterial Agents↗

PubMed1989

Peptide: N-glycosidase F: studies on the glycoprotein aminoglycan amidase from Flavobacterium meningosepticum.

Peptide: N-glycosidase from Flavobacterium meningosepticum was isolated in a homogeneous state and its physico-chemical characterization was accomplished. The reliability of the previously recorded assay procedures was assessed. Using an octaglycopeptide derived from ovomucoid a rapid and sensitive FPLC method was developed for the assay of enzymatic activity. Peptide: N-glycosidase was found to effect deglycosylation of glycoproteins bearing complex and/or multiantennary glycans even in their native state. In contrast, glycoproteins with high mannose and/or hybrid carbohydrates required denaturation to become susceptible to deglycosylation by the enzyme.

Amidohydrolases↗

PubMed1992

Flavobacterium meningosepticum peptide:N-glycosidase: influence of ionic strength on enzymatic activity.

Flavobacterium meningosepticum peptide:N-glycosidase-mediated deglycosylation of N-linked glycan strands of glycoproteins has been found to be strongly influenced by the ionic strength of the assay medium. By use of a modification of a previously published assay procedure for quantitative analysis of glycan release we have been able to improve reproducibility and thus to compare the extent of deglycosylation achieved under a variety of conditions of ionic strength. We have observed that enzyme activity is adversely affected by high ionic strength buffers such as those recommended for deglycosylation of various glycoproteins and recommend the use of low ionic strength buffers for routine use.

Amidohydrolases↗

PubMed1988

Mechanism of proline-specific proteinases: (I) Substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum.

The substrate specificity of dipeptidyl peptidase IV (dipeptidyl peptide hydrolase, EC 3.4.14.5) from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum, was investigated with a series of N-terminal unprotected (dipeptidyl peptidases IV) and succinylated dipeptidyl-p-nitroanilides (proline-specific endopeptidase). Both enzymes are specific for the S configuration of the amino-acid residue in P1 and P2 position if the penultimate residue is proline. In the case of alanine substrates (Ala in P1, dipeptidyl peptidase IV hydrolyzes such compounds where the configuration of the P2 residue is R. The penultimate residue with dipeptidyl peptidase IV can be, beside proline and alanine, dehydroproline, hydroxyproline and pipecolic acid. Proline substrates (Pro in P1) with an R configuration in P2 are inhibitors of the hydrolysis of proline substrates with an S,S configuration in an uncompetitive (dipeptidyl peptide IV) or mixed inhibition type (proline-specific endopeptidase). Derivatives of Gly-Pro-pNA where the N-terminal amino group is methylated are hydrolyzed by dipeptidyl peptidase IV.

Amino Acid Sequence↗

PubMed1989

Outbreak of nosocomial Flavobacterium meningosepticum respiratory infections associated with use of aerosolized polymyxin B.

Flavobacterium meningosepticum is an uncommon cause of adult nosocomial infection. On a medical/surgical intensive care unit we recently encountered an adult outbreak of respiratory colonization and infection caused by this organism, which was associated with the prophylactic use of aerosolized polymyxin B that had been used in an attempt to abort an outbreak of infection caused by highly resistant strains of Pseudomonas aeruginosa. Twenty isolates (95% from respiratory secretions) of F. meningosepticum from nine persons were identified during a 2 1/2-month period. No environmental source has been identified to date. Pneumonia developed in five patients, and two deaths associated with this organism occurred. All isolates were sensitive to ciprofloxacin; none were sensitive to other antibiotics tested, including third-generation cephalosporins, aminoglycosides, erythromycin, trimethoprim-sulfamethoxazole, antipseudomonal penicillins, aztreonam, and imipenem/cilastatin. Two patients with nosocomial pneumonia were successfully treated with oral ciprofloxacin. F. meningosepticum may emerge as an important pathogen if prophylactic use of polymyxin B becomes more widespread. Ciprofloxacin may become the agent of choice for treatment of this organism.

Administration, Inhalation↗