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PubMedDate not supplied

Alcaligenes faecalis rhinotracheitis in Manitoba turkeys.

An outbreak of alcaligenes rhinotracheitis occurred on one premises housing five turkey flocks totaling 25,000 poults. Prominent findings were severe respiratory difficulty resulting from excess mucus in the nasopharynx, lachrimation, and tracheal collapse. Sinus and tracheal cultures consistently yielded Alcaligenes faecalis. An adenovirus was isolated and four flocks became positive for CELO virus by agar-gel-precipitin (AGP) tests. Mortality by flocks ranged from 4% to 48%. Treatment was unsuccessful and appeared to increase the mortality rate. The course of the disease was about 6 weeks, and recovered turkeys were marketed 1 week later than the usual date.

Alcaligenes↗
PubMed2002

Purification and characterization of alkaline protease from Alcaligenes faecalis.

Extracellular alkaline protease from the alkalophilic bacterium Alcaligenes faecalis was purified by a combination of ion-exchange and size-exclusion chromatographic methods, and its properties were examined. The purified enzyme had a specific activity of 563.8 micromol of tyrosine/min per mg of protein and gave a single band on native PAGE and SDS/PAGE with a molecular mass of 67 kDa. Gelatin zymogram also revealed one clear zone of proteolytic activity which corresponded to the band obtained with native PAGE and SDS/PAGE. The enzyme had an optimal pH of 9.0 and exhibited its highest activity at 55 degrees C. The enzyme activity was inhibited by PMSF, suggesting the presence of serine residues at the active site. The enzyme had a K(m) of 1.66 mg/ml and a V(max) of 526 units/min per mg of protein with casein as the substrate.

Acetone↗
PubMed1997

Structure and function of poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1.

Poly(3-hydroxybutyrate) (PHB) depolymerase from Alcaligenes faecalis T1 is composed of three domains: the catalytic (C) domain, the fibronectin type III-like (F) domain, and the substrate-binding (S) domain. We constructed domain deletion, inversion, chimera, and extra-F-domain mutants and examined their enzyme activity and PHB-binding ability. In addition, we performed substitution of 214Asp and 273His with glycine and aspartate, respectively, to examine their participation in a catalytic triad together with 139Ser. The mutant with both the F and S domains deleted and the trypsin-digested enzyme showed no PHB-hydrolyzing activity and less PHB-binding ability than that of the wild-type enzyme but retained D-(-)-3-hydroxybutyrate trimer-hydrolyzing activity at a level similar to that of the wild-type enzyme. The mutant with the F domain deleted and the mutant which had the order of the F and S domains inverted retained PHB-binding ability and trimer-hydrolyzing activity at levels similar to those of the wild-type enzyme but lost PHB-hydrolyzing activity. The chimera mutant, in which the F domain was substituted with a Thr-rich domain of PHB depolymerase A from Pseudomonas lemoignei, and the extra-F-domain mutant, with an additional F domain, retained trimer- and PHB-hydrolyzing activities and PHB-binding ability at levels similar to those of the wild-type enzyme. Two mutants (D214G and H273D) showed no enzymatic activity toward trimer and PHB, and they were not labeled with [3H]diisopropylfluorophosphate.

Alcaligenes↗
PubMed2005

Pancreatic abscess secondary to Alcaligenes faecalis.

We report a patient with pancreatic abscesses and necrosis secondary to Alcaligenes faecalis infection. He initially presented with alcohol-induced acute pancreatitis. Twenty days after the initial presentation, he re-presented with increasing pain and was found to have pancreatic necrosis and abscesses. Treatment was initiated with meropenem. Because of persistent fevers, computed tomography-guided drainage was performed. The fluid grew A faecalis resistant to meropenem and the patient continued to be febrile. He recovered only after adequate surgical intervention and appropriate antibiotic coverage. Although this is the first case of A faecalis reported to cause pancreatic abscess, we believe selection of this organism occurred because surgical drainage was delayed while the patient was on the recommended treatment with meropenem. This case emphasizes the need for early surgical drainage of pancreatic abscesses to avoid the selection of such resistant pathogens.

Abscess↗
PubMed2005

Alcaligenes faecalis kw-a biofilm for denitrification of nitrate-rich effluent.

Alcaligenes faecalis kw-A selected for possessing good denitrification efficiency was used for biofilm development. The biofilm could be developed on a glass surface within 12 hr when 5%, Ix 10(8) cells/ml was used as inoculum. The microcolonies were seen in 6 hr and glycocalyx in 9 hr stage. At 24 hr the biofilm was developed fully and hence was visualised as dense mass. The biofilm protein content showed 48.5% increase in shake flask than in static condition. The exopoplymer is produced in larger amounts in biofilm as compared to the suspended cells. Also, its amount was more by 43% in the biofilm produced in shake flask condition than in static condition. The biofilm could remove 95% nitrate from nitrate-rich effluent in a bench-scale process in 36 hr. The attached growth technique demonstrated here can be utilised to study the effect of favourable as well as adverse conditions on the denitrification efficiency of a culture. The ultimate application of a denitrifying biofilm would be in attached growth or biofilm reactor.

Alcaligenes faecalis↗
PubMed2003

Purification and characterization of Alcaligenes faecalis penicillin G acylase expressed in Bacillus subtilis.

The Alcaligenes faecalis PGA gene encoding heterodimeric penicillin G acylase (PGA) was cloned and successfully expressed in Escherichia coli and Bacillus subtilis respectively. In contrast to E.coli hosts where the enzymes were retained in the periplasm, B. subtilis cell secreted the recombinant enzyme into the medium. Contrary to limited expression yield of E. coli (pETAPGA), PGA extracellularly expressed by B. subtilis (pBAPGA) and B. subtilis (pMAPGA) reached the highest yield of 653 u/L. This yield increased 109-fold higher than the native expression of A. faecalis CICC AS1.767. The enzyme was fractionated with (NH(4))(2)SO(4) and purified by DEAE-Sepharose CL-6B with a yield of 81%. The purified enzyme had a specific activity of 1.469 u/mg. Furthermore, some enzyme characteristics, such as the pH and temperature optimum, the stability against organic solvent and the ratio of cepholexin synthesis to hydrolysis were determined. By overexpressing A. faecalis PGA in B. subtilis and purifying secreted enzyme from culture medium one could readily obtain a large amount of an alternative source of PGA.

Alcaligenes↗
PubMedDate not supplied

[Attempt to establish genome similarity between Alcaligenes faecalis and several Gram-negative bacteria using the method of molecular hybridization of DNA to DNA].

The technique of DNA-DNA molecular hybridization was used to demonstrate the absence of genome similarity between Alcaligenes faecalis and gram-negative bacteria belonging to the genera Pseudomonas, Enterobacterium, Comamonas producing alkalis, and vibrions. Some similarity in the polynucleotide sequences was found between the DNA of the reper strain of Alcaligenes faecalis 45 (5--10% of homology) and the DNA of the culture belonging to the Achromobacter genus; therefore, the two genera may belong to one and the same family.

Alcaligenes↗
PubMed1990

Microbial metabolism of quinoline and related compounds. IV. Degradation of isoquinoline by Alcaligenes faecalis Pa and Pseudomonas diminuta 7.

From sewage and soil isoquinoline-degrading organisms were enriched. Two strains could be isolated which were able to utilize isoquinoline as sole carbon source. The bacteria were tentatively identified as Alcaligenes faecalis and Pseudomonas diminuta with respect to their morphological and physiological characters. When growing on isoquinoline both strains excrete a metabolite into the medium which was identified as 1-oxo-1,2-dihydroisoquinoline. Alcaligenes faecalis was cultivated in continuous culture on 1-oxo-1,2-dihydroisoquinoline to improve growth on isoquinoline and degradative activity.

Alcaligenes↗
PubMed1989

Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis.

The extracellular poly(3-hydroxybutyrate) depolymerase gene from Alcaligenes faecalis T1 was cloned into Escherichia coli DH1 by using the plasmid pUC8. An A. faecalis T1 genomic library was prepared in E. coli from a partial Sau3AI digest and screened with antibody against the depolymerase. Of the 29 antibody-positive clones, 1 (pDP14), containing about 4 kilobase pairs of A. faecalis T1 DNA, caused expression of a high level of depolymerase activity in E. coli. The enzyme purified from E. coli was not significantly different from the depolymerase of A. faecalis in molecular weight, immunological properties, peptide map, specific activity, or substrate specificity. Most of the expressed enzyme was found to be localized in the periplasmic space of E. coli, although about 10% of the total activity was found in the culture medium. Results of a deletion experiment with pDP14 showed that a large SalI fragment of about 2 kilobase pairs was responsible for expression of the enzyme in E. coli. The nucleotide sequence of the large SalI fragment has been determined. Comparison of the deduced amino terminus with that obtained from sequence analysis of the purified protein indicated that poly(3-hydroxybutyrate) depolymerase exists as a 488-amino-acid precursor with a signal peptide of 27 amino acids.

Alcaligenes↗
PubMed1988

Size of diffusion pore of Alcaligenes faecalis.

The diffusion pore of the outer membrane of Alcaligenes faecalis was shown to be substantially smaller than the Escherichia coli porin pore. In experiments with intact cells, pentoses and hexoses penetrated into the NaCl-expanded periplasm, whereas saccharides of Mr greater than 342 did not. Cells treated with 0.5 M saccharides of Mr greater than 342 weighed 33 to 38% less than cells treated with isotonic solution, suggesting that these saccharides do not permeate through the outer membrane. The diffusion rates of various solutes through the liposome membranes reconstituted from the Mr-43,000 outer membrane protein showed the following characteristics. (i) The relative diffusion rates of pentoses, hexoses, and methylhexoses appeared to be about 1.0, 0.6, and negligibly small, respectively. (ii) The diffusion rate of glucose appeared to be about 1/10th that with the E. coli B porin. (iii) The diffusion rate of gluconic acid was five to seven times higher than that of glucose. (iv) The diffusion rates of beta-lactam antibiotics appeared to be 40 to less than 10% of those with the E. coli B porin.

Alcaligenes↗
PubMed1973

Evidence for the existence of an aerobic pathway for synthesis of monounsaturated fatty acids by Alcaligenes faecalis.

Studies on the composition of total fatty acids of Alcaligenes faecalis harvested at different growth phases have been carried out. Ability of the organism to desaturate palmitic and stearic acid has also been tested. The organism contained palmitic (16:0), stearic (18:0), palmitoleic (16:1), cis-vaccenic (18:1), cyclopropane (17: big dn tri, open and 19: big dn tri, open), and three hydroxy acids. Increase in cyclopropane acids and corresponding decrease in monounsaturated acids in direct proportion to the age of the culture were observed, whereas other fatty acids remained relatively unaltered. A growing culture of the organism was found to desaturate [1-(14)C]palmitic acid supplied in the medium to hexadecanoic acid. Resting cells desaturated [1-(14)C]palmitic and [1-(14)C]stearic acid giving rise to about 50% of (14)C in the COOH group of corresponding monounsaturated fatty acids.

Acetates↗
PubMed1986

Degradation of poly(3-hydroxybutyrate) by poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1.

The extracellular poly(3-hydroxybutyrate) depolymerase purified from Alcaligenes faecalis T1 has two disulfide bonds, one of which appears to be necessary for the full enzyme activity. This depolymerase hydrolyzed not only hydrophobic poly(3-hydroxybutyrate) but also water-soluble trimer and larger oligomers of D-(-)-3-hydroxybutyrate, regardless of their solubilities in water. Kinetic analyses with oligomers of various sizes indicated that the substrate cleaving site of the enzyme consisted of four subsites with individual affinities for monomer units of the substrate. Analyses of the hydrolytic products of oligomers, which had labeled D-(-)-3-hydroxybutyrate at the hydroxy terminus, showed that the enzyme cleaved only the second ester linkage from the hydroxy terminus of the trimer and tetramer, and acted as an endo-type hydrolase toward the pentamer and higher oligomers. The enzyme appeared to have a hydrophobic site which interacted with poly(3-hydroxybutyrate) and determined the affinity of the enzyme toward the hydrophobic substrate.

Alcaligenes↗
PubMedDate not supplied

The efficacy of a temperature-sensitive mutant vaccine against Northwest Arkansas isolates of Alcaligenes faecalis.

The efficacy of a commercially produced temperature-sensitive mutant Alcaligenes faecalis vaccine was evaluated in turkeys contact-challenged with one of three strains of A. faecalis. In the vaccinated control group, the vaccine strain of A. faecalis colonized the nasal turbinates but not the trachea, caused no clinical signs of turkey coryza, and induced humoral antibodies. In the vaccinated challenged groups, the vaccine reduced both the severity of lesions and the number of birds exhibiting lesions compared with unvaccinated challenged groups, but it did not prevent colonization of challenge strains of A. faecalis.

Alcaligenes↗