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At least 19 recordsLinked to original sources
PubMed1992

Molecular cloning of a specific DNA probe for the identification of Bacillus licheniformis.

Bacillus licheniformis has been found to be one of the dominant nosocomial species of Bacillus: laboratories dealing with nosocomial infections must be able to identify Bacillus up to the species level. To date, no DNA probes have been isolated for B. licheniformis although there is a clear need for a direct detection by polymerase chain reaction. The isolation of a B. licheniformis-specific DNA probe, as described in this paper, represents the first step toward accomplishing this goal.

Bacillus↗
PubMed1993

Two glucose transport systems in Bacillus licheniformis.

Bacillus licheniformis NCIB 6346 showed active accumulation of glucose which was inhibited by agents which affect the transmembrane proton gradient. Phosphotransferase (PTS) activity, identified as phosphoenolpyruvate-dependent phosphorylation of glucose, was found in cell extracts but could not be demonstrated in cells permeabilized with toluene when assays were conducted at pH 6.6. The same was true for mannitol and fructose phosphotransferase activities. Cells grown on fructose accumulated glucose at a slower rate than glucose-grown cells, and extracts prepared from them did not contain glucose PTS activity. Examination of the effects of analogs on glucose uptake and phosphorylation showed that 2-deoxyglucose was not a PTS substrate, but did markedly inhibit glucose uptake, with stronger inhibition in cells grown on fructose. Glucose accumulation by whole cells grown on glucose became less sensitive to the uncoupler tetrachlorosalicylanilide (TCS) as the pH was raised from 6.6 to 8.0, while in fructose-grown cells TCS was equally effective across this pH range. PTS activity was exhibited by toluene-treated cells at pH 7.5 and above, although the system itself in extracts was not affected by pH in the range of 5.0 to 8.0. The results are consistent with the presence of two glucose transport systems, one a PTS and the other operating by an alternative mechanisms, and suggest that the PTS in B. licheniformis may be regulated in a pH-dependent manner.

Bacillus↗
PubMed1982

The influence of glucose, ammonium and magnesium availability on the production of protease and bacitracin by Bacillus licheniformis.

Bacillus licheniformis was cultivated in a range of defined media varying in both the nature of the growth-limiting component and the concentration of excess nutrients. The compositions of the media were such as to ensure that the final absorbance (A430) of the culture was the same in each case. Samples taken during the stationary phase were assayed for their content of extracellular serine protease and bacitracin. The nature of the growth-limiting nutrient had a profound effect on the amounts of these products formed while those components which were present in excess also exerted an influence in proportion to their concentration. Thus, for example, a four-fold increase in serine protease production occurred when ammonium replaced glucose as the growth-limiting nutrient. Serine protease and bacitracin production responded differently to these varying cultural conditions suggesting they are subject to separate control mechanisms. The results are discussed in relation to the need for rigorously controlled cultural conditions during physiological studies of this nature.

Ammonia↗
PubMed1995

Contribution of a disulfide bridge to the stability of 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis.

Bacillus 1,3-1,4-beta-glucanases possess a highly conserved disulfide bridge connecting a beta-strand with a solvent-exposed loop lying on top of the extended binding site cleft. The contribution of the disulfide bond and of both individual cysteines (Cys61 and Cys90) in the Bacillus licheniformis enzyme to stability and activity has been evaluated by protein engineering methods. Reduction of the disulfide bond has no effect on kinetic parameters, has only a minor effect on the activity-temperature profile at high temperatures, and destabilizes the protein by less than 0.7 kcal/mol as measured by equilibrium urea denaturation at 37 degrees C. Replacing either of the Cys residues with Ala destabilizes the protein and lowers the specific activity. C90A retains 70% of wild-type (wt) activity (in terms of Vmax), whereas C61A and the double mutant C61A-C90A have 10% of wt Vmax. A larger change in free energy of unfolding is seen by equilibrium urea denaturation for the C61A mutation (loop residue, 3.2 kcal/mol relative to reduced wt) as compared with the C90A mutation (beta-strand residue, 1.8 kcal/mol relative to reduced wt), while the double mutant C61A-C90A is approximately 0.8 kcal/mol less stable than the single C61A mutant. The effects on stability are interpreted as a result of the change in hydrophobic packing that occurs upon removal of the sulfur atoms in the Cys to Ala mutations.

Bacillus↗
PubMed1983

Comparative studies on extracellular penicillinases of the same structural gene, penP, expressed in Bacillus licheniformis and Bacillus subtilis.

Extracellular penicillinases produced by Bacillus licheniformis ATCC 9945A and Bacillus subtilis from the same structural gene, penP, were compared. The two strains secreted the same exo-large penicillinase (mol. wt, 305000; isoelectric point, pI = 5.00-5.04; NH2-terminal amino acid, Ser). In contrast, the exo-small enzyme from Bacillus subtilis (mol. wt, 29500; pI = 5.00-5.04; NH2-terminal amino acid, Glu or Asn) was slightly different from that of Bacillus licheniformis (mol. wt, 29500; pI = 5.13; NH2-terminal amino acid, Lys). The difference in the NH2-terminal residue is most probably due to differences in degradation by host-specific proteolytic enzymes.

Amino Acid Sequence↗
PubMed1963

TRANSDUCTION OF BACILLUS LICHENIFORMIS AND BACILLUS SUBTILIS BY EACH OF TWO PHAGES.

Taylor, Martha J. (U.S. Army Biological Laboratories, Fort Detrick, Frederick, Md.) and Curtis B. Thorne. Transduction of Bacillus licheniformis and Bacillus subtilis by each of two phages. J. Bacteriol. 86:452-461. 1963.-A second transducing bacteriophage, designated SP-15, was isolated from the same soil-sample culture filtrate that supplied the Bacillus subtilis transducing phage, SP-10, reported earlier from this laboratory. SP-10 and SP-15 differ serologically and in several other respects, but share the ability to propagate on B. subtilis W-23-S(r) (streptomycin-resistant) and B. licheniformis ATCC 9945a, and to mediate general transduction in either species when propagated homologously. Attempts to transduce between the species have failed. SP-10 forms plaques readily on both W-23-S(r) and 9945a; SP-15 forms minute plaques on W-23-S(r) and has shown no evidence of any lytic activity on 9945a. Maximal recoveries of prototrophic colonies from mixtures of SP-10 with auxotrophs of either W-23-S(r) or 9945a were obtained only when excess phage was neutralized by post-transduction treatment with specific phage antiserum. Such treatment was not necessary for maximal recovery of transductants effected by SP-15. Unlike SP-10, SP-15 propagated on W-23-S(r) did not transduce B. subtilis 168 (indole(-)). SP-15 transduced B. licheniformis more efficiently than did SP-10. Neither phage was able to transduce B. licheniformis as efficiently as it transduced B. subtilis. The differing influences of multiplicity of infection were compared for the two phages in both species.

Bacillus↗
PubMed1975

Estimates of the porosity of Bacillus licheniformis and Bacillus subtilis cell walls.

The maximum porosity of Bacillus subtilis and Bacillus licheniformis cell walls was estimated by two independent and relatively simple methods. Peptidoglycan was isolated from Bacillus subtilis cell wall preparations and used as an insoluble support for exclusion chromatography of dextrans of known average molecular size. In an alternative approach the leakage of radioactively labelled proteins from Bacillus licheniformis cells incubated in butanol-saline mixtures was measured and their size estimated by exclusion chromatography on Sephadex G-100. Under these conditions the permeability barrier of the cytoplasmic membrane was destroyed with preservation of the structural integrity of the outer cell wall. The apparent exclusion threshold of the cell wall of either organism as determined by these means corresponded to molecules with a diffusional radius of not more than 2.5 nm.

Alanine↗
PubMed2006

Effect of Bacillus licheniformis and Bacillus subtilis supplementation of ewe's feed on sheep milk production and young lamb mortality.

The purpose of this pilot study was to evaluate under field conditions the effect of a probiotic containing Bacillus licheniformis and Bacillus subtilis on young lamb mortality and sheep milk production when administered in the late pregnancy and lactation feed of ewes. In a sheep farm, two groups of milking ewes with identical genetic material, management, nutrition, health status and similar production characteristics were formed. One group (46 ewes) served as control, while the other one (48 ewes) served as a probiotic-treated group. Both groups of ewes received a similar feeding regiment, but the ewes of the second group were additionally offered a probiotic product containing B. licheniformis and B. subtilis (BioPlus 2B, Chr. Hansen, Denmark) at the approximate dose of 2.56 x 10(9) viable spores per ewe per day. Lamb mortality during the 1.5 months suckling period, and milk yield during the 2 months of milk collection for commercial purposes have been recorded. In the non-treated control group, 13.1% mortality was observed versus 7.8% in the probiotic-treated group (P = 0.33), with mortality being mainly due to diarrhoea. Microbiological examination of diarrhoeic faeces from some of the dead lambs in both groups revealed the presence of Escherichia coli. The average daily milk yield per ewe was significantly lower in the control group (0.80 l) than that in the probiotic-treated group (0.93 l) (P < 0.05). Fat and protein content of milk in ewes that received probiotics was significantly (P < 0.05) increased compared with untreated ewes. It was concluded that supplementing ewe's feed with probiotics may have beneficial effect on subsequent milk yields, fat and protein content.

Animal Feed↗
PubMed2004

Field evaluation of the efficacy of a probiotic containing Bacillus licheniformis and Bacillus subtilis spores, on the health status and performance of sows and their litters.

The aim of this study was to assess the efficacy of BioPlus 2B, a probiotic containing Bacillus licheniformis and Bacillus subtilis spores, on the health status and productivity of sows and their litters. A total of 109 gilts and sows were allocated into two experimental groups, as follows: untreated controls (UC) and BioPlus 2B (same feeding as the UC group plus BioPlus 2B) at a dose of 400 g/ton of feed (equal to 1.28 x 10(6) viable spores/g of feed). Treatment started from the day of allocation (14 days prior to the expected farrowing) up to the weaning day. Homogeneity of the groups was satisfied with regard to the parity. From the results it was evident that BioPlus 2B supplementation of the feed improved gilt/sow performance as shown by: (i) the increase of sow feed consumption during the first 14 days postpartum and (ii) the decrease of sow weight loss during the suckling period. Certain blood and milk parameters were significantly improved, as shown by higher serum cholesterol and total lipids concentrations and higher milk fat and protein content at mid-suckling period. As a consequence, a positive effect was also noticed as regard litter health and performance characteristics in terms of: (i) decrease in piglet diarrhoea score, (ii) decrease in pre-weaning mortality thus leading to increase in the number of weaned piglets per litter and (iii) increase in piglet body weight at weaning. Moreover, BioPlus 2B tended to improve the health status and fertility of sows demonstrating: (i) tendency to a lower proportion of sows with Mastitis-Metritus-Agalactia (MMA) problems and (ii) lower proportion of sows returning to oestrus.

Animal Feed↗
PubMed1975

Peptidoglycan synthesis in L-phase variants of Bacillus licheniformis and Bacillus subtilis.

Stable L-phase variants isolated from Bacillus licheniformis and Bacillus subtilis, when grown in osmotically stabilized media, do not synthesize peptidoglycan but have been found to accumulate the nucleotide precursors of this polymer. The enzymes involved in the synthesis of these precursors and the later membrane-bound stages of peptidoglycan synthesis have been investigated, and the L-phase variants have been shown to contain lesions, which provide a rational explanation for the absence of peptidoglycan and for the nature of the precursor accumulated. The majority of the L-phase variants contained a single enzymic defect, but two strains were isolated with double lesions. Five out of seven strains examined accumulated uridine 5'-diphosphate (UDP)-MurAc-L-ala-D-glu and were unable to synthesize diaminopimelic acid as a consequence of a defect in aspartate-beta-semialdehyde dehydrogenase activity. Two strains were deficient in UDP-MurAc: L-alanine ligase and accumulated UDP-MurAc. One strain accumulated the complete nucleotide precursor UDP-MurAc-L-ala-D-glu-mA2pm-D-ala-D-ala and was deficient in phospho-N-acetylmuramyl pentapeptide translocase. A second strain also had this lesion, together with defective aspartate-beta-semialdehyde dehydrogenase activity. The other enzymes of peptidoglycan synthesis were present in the L-phase variants, with activities similar to those found in the parent bacilli grown under identical conditions. Membrane preparations from certain of the L-phase variants were also capable of synthesizing the secondary polymers poly(glycerol phosphate) teichoic acid and teichuronic acid and also a polymer of N-acetylglucosamine.

Alanine↗
PubMed1977

DNA polymerase from mesophilic and thermophilic bacteria. III. Lack of fidelity in the replication of synthetic polydeoxyribonucleotides by DNA polymerase from Bacillus licheniformis and Bacillus stearothermophilus.

1. DNA polymerase from the mesophile Bacillus licheniformis and the thermophile Bacillus stearothermophilus has been used to study the replication of poly(dA-dT)-poly(dA-dT) and poly(dC)-poly(dG) templates at 37, 45, and 55 degrees C. 2. Incorporation of non-complementary deoxyribonucleoside triphosphates (misincorporation) occurred with both enzymes and both templates. Non-specific incorporation (de novo polynucleotide synthesis, random attachment to existing strands, and tritium exchange of nucleotides) accounted for, at most, a small fraction of the total observed misincorporation. The error rates at 37 degrees C for the complete system were as follows:: B. licheniformis: dATP, 1/61; dCTP, 1/830; dGTP, 1/360; dTTP, 1/65; B. stearothermophilus: dATP, 1/68; dCTP, 1/1430; dGTP, 1/440; dTTP, 1/67. For both organisms, the error rate for dCTP and dGTP was independent of incubation temperature; the error rate for dATP and dTTP was 5-50-fold greater than that for dCTP or dGTP and increased significantly from 37 to 55 degrees C. 3. The ratio of dATP to dTTP incorporation with the poly(dA-dT)-poly-(dA-dT) template was independent of temperature and close to unity. The ratio of dCTP to dGTP incorporation with the poly(dC)-poly(dG) template decreased from approx. 0.2 to 0.05 for the mesophile and from approx. 0.06 to 0.03 for the thermophile as the temperature increased from 37 to 55 degrees C.

Bacillus↗
PubMed2001

Regulation of polyglutamic acid synthesis by glutamate in Bacillus licheniformis and Bacillus subtilis.

The synthesis of polyglutamic acid (PGA) was repressed by exogenous glutamate in strains of Bacillus licheniformis but not in strains of Bacillus subtilis, indicating a clear difference in the regulation of synthesis of capsular slime in these two species. Although extracellular gamma-glutamyltranspeptidase (GGT) activity was always present in PGA-producing cultures of B. licheniformis under various growth conditions, there was no correlation between the quantity of PGA and enzyme activity. Moreover, the synthesis of PGA in the absence of detectable GGT activity in B. subtilis S317 indicated that this enzyme was not involved in PGA biosynthesis in this bacterium. Glutamate repression of PGA biosynthesis may offer a simple means of preventing unwanted slime production in industrial fermentations using B. licheniformis.

Bacillus↗
PubMed2002

Co-linear scaffold of the Bacillus licheniformis and Bacillus subtilis genomes and its use to compare their competence genes.

We have established the co-linear regions of Bacillus licheniformis, an industrially important bacterium, and Bacillus subtilis, a model bacterium. In the co-linear regions, revealed by PCR, gene content and order are presumed to be conserved. These regions constitute approximately 60% of the compared chromosomes. Sequencing of the competence genes of B. licheniformis allowed us to validate the approach, and to demonstrate how it can be used for the comparative analysis of complex genetic systems. A new insertion sequence, designated IS3Bli1, was discovered in the competence region of the analyzed B. licheniformis strain.

Bacillus↗
PubMed1987

Characterization of the sacQ genes from Bacillus licheniformis and Bacillus subtilis.

The sacQ gene from Bacillus licheniformis was cloned and expressed in Bacillus subtilis. Deletion analysis shows that it encodes a 46-amino-acid polypeptide homologous to the B. subtilis sacQ gene product. The polypeptide, when it is overexpressed, activates the expression of a number of target genes in B. subtilis, all encoding secreted enzymes: alkaline protease, levansucrase, beta-glucanase(s), xylanase, and alpha-amylase. The maximum stimulations measured for alkaline protease and levansucrase were by a factor of 70 and 50, respectively, when the sacQ gene from B. licheniformis was present on a multicopy plasmid in B. subtilis. The sacQ genes from B. subtilis and B. licheniformis, cloned in the same multicopy plasmid, were compared under the same conditions. The sacQ gene from B. licheniformis was more efficient than the sacQ gene from B. subtilis in producing the hypersecretion phenotype. The sacQ structural genes from B. subtilis and B. licheniformis were placed under the control of the same inducible promoter. Hypersecretion was specifically obtained under conditions of full induction of the promoter. The target site of levansucrase regulation by sacQ was identified as a 440-base-pair fragment located in the 5' noncoding region of sacB, suggesting transcriptional control.

Amino Acid Sequence↗
PubMed1978

Degradation by Eco R1 endonuclease of DNA isolated from phages infecting Bacillus licheniformis and Bacillus thuringiensis.

DNA was isolated from lytic phages of two strains, Bacillus licheniformis, a producer of bacitracin, and Bacillus thuringiensis forming protein paracrystals with pronounced insecticidal effects. Its sensitivity to Eco R1 restriction endonuclease was determined. It was the aim of the work to find out whether these phages could serve as vectors in the transfer and possible amplification of genes of the two important industrial species of bacilli. Approximate values of the molecular weight of DNA of the two phages were determined after degradation of the phage DNA by Eco R1, followed by comparison of electrophoretic mobility of individual fragments with that of the Eco R1-degraded DNA of phage lambdab2.

Bacillus↗
PubMed1969

Cell-free amino acid-incorporating systems from Bacillus licheniformis and Bacillus stearothermophilus 10.

Cell-free amino acid-incorporating systems were prepared from log-phase cells of Bacillus licheniformis and B. stearothermophilus 10. No differences were observed between the two systems with respect to the types and relative amounts of the ribosomes, the time dependence of incorporation, and the optimal magnesium ion concentration (4 mm). The B. licheniformis system showed greater dependence on added transfer ribonucleic acid (tRNA) and was less stimulated by polyuridylic acid (poly U) than the B. stearothermophilus 10 system. Neither system was saturated at a level of 450 mug of poly U per incubation mixture. The S-100 fraction and the isolated tRNA inhibited incorporation in the B. stearothermophilus 10 system at 55 C but not at 37 C. No such inhibition was observed in the B. licheniformis system at either temperature. The tRNA prepared from B. subtilis, B. licheniformis, or B. stearothermophilus 10 could be used interchangeably in the two cell-free systems.

Bacillus↗
PubMed1995

Expression of the subtilisin Carlsberg-encoding gene in Bacillus licheniformis and Bacillus subtilis.

The cloning and sequence of the 5' untranslated region (5'-UTR) of the Bacillus licheniformis (Bl) 6816 subtilisin Carlsberg gene (subC) are reported here. The 5' and 3' ends of subC transcripts were characterized, and the promoter identified. Expression was studied using a fused lacZ reporter gene integrated into the chromosome of heterologous host Bacillus subtilis (Bs). beta Gal activities of mutants deleted within the promoter region identified a region which is required for stimulation by the transcriptional activator proteins, DegU and DegQ. This region is close to the transcription start point (tsp), and is adjacent to a sequence homologous to that involved in DegU/Q stimulation of the Bs subtilisin gene, aprE. Expression of subC in Bs was optimized by the use of heterologous promoter and by the deletion of UTR sequences predicted to be involved in secondary structures in the native subC mRNA. Sequence comparison with other subtilisin Carlsberg-type-encoding genes revealed a high degree of conservation of the entire 5'-UTR, including regulatory sequences and promoter, as well as part of the structural gene.

Amino Acid Sequence↗
PubMed2006

Estimating amplification efficiency improves multiplex real-time PCR quantification of Bacillus licheniformis and Bacillus subtilis spores in animal feed.

A multiplex real-time PCR assay was developed for absolute quantification in animal feed of Bacillus subtilis CH201 and Bacillus licheniformis CH200 spores, which constitute the viable component of the microbial growth promoter, BioPlus 2B. Spores were lysed using a bead-beating protocol. DNA was extracted and purified from the lysates with the Qiagen DNeasy Plant Kit. Two standard curves for absolute quantification were made and tested. Standard curve-1 was made from feed samples spiked with BioPlus 2B, while standard curve-2 was made from serially diluted DNA extracted from BioPlus 2B powder. Feed samples supplemented with BioPlus 2B were quantified using both standard curves. The detection limit of the assay was 10(4) CFU g(-1) of feed. The amplification efficiency (Eff) of each PCR was determined using the LinRegPCR software and Eff differences between individual samples and standards were corrected for. When compared to plate counts, standard curve-1 slightly under-estimated the number of spores (mean=-2.47% of plate counts). A spore density-dependent Eff was found, and Eff for standard curve-1 could not be determined. Standard curve-2 over-estimated spore numbers when not corrected for individual Eff (mean=+5.46% of plate counts). Standard curve-2 Eff was independent (Eff(mean)=1.96) of spore density. The assay quantified the numbers of spores in feed samples very similar to plate counts (mean=+0.47% of plate counts), when standard curve-2 was used and individual Eff was accounted for.

Animal Feed↗