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PubMed1982

An extracellular poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis.

A strain of Alcaligenes faecalis T1, which was isolated from activated sludge, excreted an extracellular poly(3-hydroxybutyrate) depolymerase as it grew in a medium containing poly(3-hydroxybutyrate) as the sole carbon source. The molecular weight of the enzyme, purified from the culture medium to electrophoretic homogeneity, was 48 000 as determined by Sephadex G-100 filtration, and 50 000 by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate. The pH optimum for the enzyme reaction was 7.5. The purified enzyme depolymerized poly(3-hydroxybutyrate) purified from Zoogloea ramigera 1-16-M, but did not attack the bacterial native poly(3-hydroxybutyrate)-containing granules. Km values were 13.3 micrograms/ml (= 0.78 microM, based on an estimated average molecular weight of 17 000) for poly(3-hydroxybutyrate) and 5.4 mM for the trimeric ester of D(--)-3-hydroxybutyric acid. Analysis of hydrolytic products of poly(3-hydroxybutyrate), several oligomeric esters of D(--)-3-hydroxybutyric acid, and the methyl ester of the trimeric ester indicated that the enzyme hydrolyzed these substrates from the free hydroxyl terminus, releasing D(--)-3-hydroxybutyrate dimer units one at a time.

Alcaligenes↗
PubMed1997

Strains of Alcaligenes faecalis from clinical material.

Six strains of Alcaligenes faecalis, unusually isolated from clinical material, are described. Alcaligenes faecalis is a Gram-negative catalase- and oxidase-positive, motile rod. It is commonly found in a watery environment and is rarely isolated from humans. The clinical and laboratory characteristics of the clinical A. faecalis isolates are presented.

Adult↗
PubMed2004

[Constitutive expression and purification of Alcaligenes faecalis penicillin G acylase in Escherichia coli].

Considering Alcaligenes faecalis pencillin G acylase(AfPGA), which possesses the attractive characteristics for beta-lactam antibiotics conversions, the gene of PGA was cloned into an expressing vector pKKFPGA. The recombinant plasmid contained multicopy replicon(COLE 1), trc promoter, AfPGA gene, rrnB transcript terminator and ampicillin marker transformed Escherichia coli DH5alpha. As both the recombinant plasmid and the host DH5alpha had no laclq gene, the trc promoter was always active and the AfPGA could be constitutively expressed without IPTG induction in the host DH5alpha. In the shaking flask, the recombinant cell was inoculated into the fermentation medium (tryptone 10g/L, yeast extract 5g/L, MgSO4 x 7 H2O 1g, KH2 PO4 2g/L, K2HPO4 x 3H2O 5g/L, Na2HPO4 x 12H2O 7g/L, (NH4)2SO4 1.2g/L, NH4Cl 0.2 g/L, NaCl 0.1g/L, dextrin 30g/L) and cultured at 28 degrees C for 20h. The production of AfPGA reached 2,590u/L(NIPAB method), with a cell-density-specific activity of more than 300(u/L)/A600, this yield increased 432 fold higher than the native expression of Alcaligenes faecalis . Without ammonium sulphate fractionation and dialysis, the supernatant of crude extract was directly loaded on DEAE-Sepharose CL 6B column equilibrated by phosphate buffer (50mmol/L, pH7.8), and the enzyme fraction was not absorbed on the column but impurities were absorbed. Subsequently the effluent was added ammonium sulphate to 1mol/L and loaded on Butyl-Sepharose CL 4B column equilibrated by 50mmol/L phosphate buffer pH7.8-1mol/L ammonium sulphate. The enzyme was eluted as concentration of ammonium sulphate in phosphate buffer decreased to 0, PGA was eluted. After these two column chromatography, the enzyme was enriched 20 times with a 91% activity recovery. The purified enzyme had a specific activity of 68.6u/mg protein. However, the overproduction of PGA was often limited by translocation and/or periplasmic processing steps, subsequently resulted in intracellular accumulation of various types of PGA precursors and then formed inclusion bodies in the cytoplasm and/or periplasm. In this study, 5% PGA precursors formed as inclusion bodies in the cytoplasm while no inclusion bodies formed in the periplasm. It suggested most PGA precursors were transported to the periplasm and matured to active PGA and also explained why PGA gene was highly expressed in the host DH5alpha. On the other hand, inclusion bodies in the cytoplasm indicated that the maturation of PGA in the host DHSalpha was limited by the translocation step.

Alcaligenes faecalis↗
PubMed1985

An Alcaligenes faecalis isolate from turkeys: pathogenicity in selected avian and mammalian species.

An Alcaligenes faecalis isolate of known pathogenicity for turkeys was examined for adherence and cytotoxicity in tracheal organ cultures of turkeys, chickens, Japanese quail, guinea pigs, hamsters, and mice, and for colonization and pathogenicity in these 6 species. Adherence and colonization were detected by fluorescent antibody staining. Infected and noninfected tracheal rings were examined by phase-contrast microscopy for cytotoxicity (ciliostasis, blebing of the cell membrane, and sloughing of the ciliated epithelium). Alcaligenes faecalis adhered to the tracheal rings of all species examined. Cytotoxicity was apparent in the tracheal rings of turkeys, quail, and chickens. Cytotoxicity was not detected in tracheal rings from the mammalian species. Alcaligenes faecalis colonization of turbinates and tracheas of intact turkeys and quail was detected. Clinical signs of alcaligenes rhinotracheitis were observed and histopathologic characteristics of the disease were detected. Chickens, guinea pigs, hamsters, and mice were refractory to infection with this isolate of A faecalis.

Adhesiveness↗
PubMed1976

Alcaligenes faecalis septicaemia.

A case of Alcaligenes faecalis septicaemia occurring after appendicectomy is described, and previous reports of this condition are briefly reviewed. Alcaligenes is frequently found in the faeces of healthy people and systemic infections appear to be very uncommon. Nevertheless, if the organism is cultured from the blood it should not be dismissed as a contaminant without careful investigation.

Adolescent↗
PubMed2000

[Tn5 mutagenesis and the characteristics of indole-3-acetic acid biosynthesis in Alcaligenes faecalis A1501].

The IAA production of Alcaligenes faecalis wild type strain A1501 depended on addition of L-tryptopham(trp). A1501 could grow well in minimal medium without Trp, but could not produce IAA. The results indicated that there was Trp-dependent IAA biosynthesis pathway in A. faecalis A1501. A1501 shows a characteristic of cell density-dependent IAA biosynthesis. The Tn5-induced mutant bank of A1501 was constructed using Tn5 mutagenesis and one Trp auxotrophic mutant AT63 was selected and identified. The Tn5-induced mutant AT63 could synthesis 2.24 micrograms/mL IAA in minimal medium without L-Trp. It indicated there were at least two IAA biosynthesis pathways in A. faecalis, one needed Trp, the other needed IGP as precursor. The results of southern hybridization also suggested that the Tn5-insertion might locate in gene locus encoded IAA synthetase.

Alcaligenes faecalis↗
PubMed2001

Alcaligenes faecalis subsp. parafaecalis subsp. nov., a bacterium accumulating poly-beta-hydroxybutyrate from acetone-butanol bioprocess residues.

The authors have previously isolated a solvent tolerant bacterium, strain G(T), (T = type strain) capable to convert acetone-butanol bioprocess residues into poly-beta-hydroxybutyrate. Strain G(T) was initially identified as Alcaligenes spp by standard bacteriological tests. In this study the taxonomic position of the bacterium was investigated in detail. The 165 rDNA sequence analysis, the G + C content of DNA (56 mol%) and the presence of ubiquinone Q-8 confirmed strain G(T) as a representative of the genus Alcaligenes. In the polyamine pattern of the bacterium putrescine and cadaverine were detected, but only trace amounts of 2-hydroxyputrescine. The extremely low content of 2-hydroxyputrescine is remarkable, since this unique diamine is a common marker for beta-proteobacteria. Phylogenetic analyses of 16S rDNA demonstrated that Alcaligenes sp. G(T) is most closely related to the species Alcaligenes faecalis (99.6% sequence similarity to A. faecalis HR4 and 98.7% sequence similarity to A. faecalis [ATCC 8750T = DSM 30030T]. On the basis of DNA-DNA relatedness (56% similarity), the unique polyamine pattern, the physiological and biochemical differences strain G(T) could be distinguished from the species A. faecalis. Therefore, a new subspecies for the species Alcaligenes faecalis is proposed; Alcaligenes faecalis subsp. parafaecalis subsp. nov.

Acetone↗
PubMed2005

Alcaligenes faecalis subsp. phenolicus subsp. nov. a phenol-degrading, denitrifying bacterium isolated from a graywater bioprocessor.

A Gram (-) coccobacillary bacterium, J(T), was isolated from a graywater bioprocessor. 16S rRNA and biochemical analysis has revealed strain J(T) closely resembles Alcaligenes faecalis ATCC 8750T and A. faecalis subsp. parafaecalis DSM 13975T, but is a distinct, previously uncharacterized isolate. Strain J(T), along with the type strain of A. faecalis and its previously described subspecies share the ability to aerobically degrade phenol. The degradation rates of phenol for strain J(T) and reference phenol degrading bacteria were determined by photometrically measuring the change in optical density when grown on 0.1% phenol as the sole carbon source, followed by addition of Gibb's reagent to measure depletion of substrate. The phenol degradation rates of strain J(T) was found to exceed that of the phenol hydroxylase group III bacterium Pseudomonas pseudoalcaligenes, with isolate J(T) exhibiting a doubling time of 4.5 h. The presence of the large subunit of the multicomponent phenol hydroxylase gene in strain J(T) was confirmed by PCR. The presence of the nirK nitrite reductase gene as demonstrated by PCR as well as results obtained from nitrite media indicated denitrification at least to N2O. Based on phenotypic, phylogenetic, fatty acid analysis and results from DNA DNA hybridization, we propose assigning a novel subspecies of Alcaligenes faecalis, to be named Alcaligenes faecalis subsp. phenolicus with the type strain J(T) (= DSM 16503) (= NRRL B-41076).

Alcaligenes faecalis↗
PubMedDate not supplied

Immunization against turkey coryza by colonization with mutants of Alcaligenes faecalis.

Temperature-sensitive mutants of Alcaligenes faecalis that exhibited reduced growth at 42 C but grew well at 30 C were induced by N-methyl-N'-nitro-N-nitrosoguanidine. Four of the 5 mutants that were studied readily colonized the nasal mucosa of turkeys when given intranasally or in drinking water. Several mutants caused no signs of coryza or depression and produced minimal colonization of the trachea. Colonization of the nasal mucosa lasted 3 to 4 weeks and induced moderate levels of serum antibodies. When challenged with virulent isolates of A. faecalis 4 to 6 weeks after having been exposed to the mutants, unstressed turkeys were protected; turkeys subjected to water deprivation exhibited some colonization with the virulent strain and showed slight signs of coryza.

Alcaligenes↗
PubMed1986

The purification and characterization of a beta-glucosidase from Alcaligenes faecalis.

The beta-glucosidase from Alcaligenes faecalis has been purified to homogeneity (880-fold purification, 11% yield) using a combination of classical techniques and medium pressure ion-exchange chromatography. It is a dimeric enzyme of monomer molecular weight 50,000 and has no specific requirement for divalent metal ions. It has a high specificity for beta-glucosides and hydrolyses a wide variety of different chemical types wit retention of configuration at the anomeric centre. It has no exo-beta-1,4-glucanase activity. It is reversibly inhibited by a variety of sugars which have been shown previously to be very active against glucosidases, suggesting a normal mechanism of action. Measured Km values for cellobiose and p-nitrophenyl beta-D-glucopyranoside are quite low (0.70 and 0.08 mM, respectively), making this a good choice for cocloning into a cellulase system optimized for glucose production.

Alcaligenes↗
PubMed1979

Isolation and properties of a particulate fraction for the desaturation of palmitic acid from Alcaligenes faecalis.

A particulate fraction obtained from Alcaligenes faecalis could desaturate palmitic acid to palmitoleic acid. NADPH, ATP, CoA, Fe2+ and Mg2+ were essential cofactors for the reaction. The desaturation showed an absolute requirement for O2. Metal ions like Mn2+, Mo6+ and Cu2+ did not affect the desaturation, while Zn2+ was inhibitory. Sulfhydryl agents such as cysteine, glutathione and beta-mercaptoethanol had no effect, but SH-blocking agents like HgCl2 and p-hydroxymercuribenzoate inhibited the reaction. Azide and cyanide strongly inhibited the reaction while CO had no effect. The presence of a b-type cytochrome in the enzyme preparation was confirmed by the spectral studies on the reaction of enzyme with NADPH. Involvement of b-type cytochrome in the desaturation reaction was demonstrated by the reoxidation of b-type cytochrome initially reduced with NADPH, by the addition of palmitic acid and other cofactors. The pH optimum for the enzyme activity was 7.4. The optimum temperature for enzyme activity was 25 degrees C and maximum activity was obtained at the end of 45 min.

Adenosine Triphosphate↗
PubMedDate not supplied

Effect of humidity on infection of turkeys with Alcaligenes faecalis.

Turkeys maintained at 75% to 80% relative humidity were more adversely affected by Alcaligenes faecalis infection than turkeys maintained at 20 to 35% relative humidity. Alcaligenes faecalis was reisolated earlier and more often from turkeys maintained at the higher humidity. Clinically, the turkeys maintained at high humidity exhibited both sinusitis and conjunctivitis earlier than the turkeys at low humidity. In both groups, antibody titers as determined by a microagglutination test developed by 2 weeks postinoculation and started to decline after the third week, lymphocytosis was demonstrated at 1 week postinoculation, and a lymphopenia developed at 5 weeks postinoculation.

Agglutination Tests↗