Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Acetobacter”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 667 records · Page 37Linked to original sources
PubMed1993

Identification and analysis of the Rhizobium meliloti exoAMONP genes involved in exopolysaccharide biosynthesis and mapping of promoters located on the exoHKLAMONP fragment.

Sequence analysis of a 7.494 kb DNA fragment from megaplasmid 2 of Rhizobium meliloti 2011 involved in exopolysaccharide I (EPS I) biosynthesis revealed the presence of five exo genes designated exoA, exoM, exoN, exoO, and exoP. ExoN was found to show strong homology to a UDP-glucose pyrophosphorylase from Acetobacter xylinum, whereas ExoO displayed weak homologies to the NodC proteins from R. meliloti and R. loti. Surprisingly, different mutations in exoP resulted in divergent phenotypes. One exoP mutant was able to establish an effective symbiosis with alfalfa, although no EPS I polymer could be detected. In contrast, other exoP mutations prevented the formation of an effective symbiosis. The transcriptional organization of the exoA-exoP gene region has been analysed in conjunction with the exoH, exoK and exoL genes. Using exo-lacZ transcription fusions in association with plasmid integration mutagenesis a strong promoter was identified upstream of exoH, which is able to direct transcription of the whole exoHKLAMONP gene cluster. A much weaker promoter upstream of exoL was found to be involved in the transcription of the exoLAMONP genes. In addition, weak promoters were identified upstream of exoK, exoA, exoN and exoP.

Amino Acid Sequence↗
PubMed1981

Gluconobacters from honey bees.

Fifty-six Gluconobacter strains and one Acetobacter strain were isolated from honey bees and their environment in three different regions in Belgium and identified phenotypically. Polyacrylamide gel electrophoresis of the soluble cell proteins showed that two different types exist within the Gluconobacter isolates: strains from type A were found in samples of the three regions, whereas strains from type B were only isolated in two of the three regions. Both types could occur in bees from the same region, from several hives of one bee keeper and from one hive. Strains from type A were almost identical with collection strain G. oxydans subsp. suboxydans NCIB 9018, whereas strains from type B constituted a new protein electrophoretic type within the genus Gluconobacter. Although Gluconobacter is apparently associated with honey bees, it is not known whether it is important or required for the bees or any hive product.

Animals↗
PubMed2003

Composites of bacterial cellulose and paper made with a rotating disk bioreactor.

Suspended solids in the nutrient medium for Acetobacter xylinium in a rotating disk bioreactor become incorporated into the gelatinous mat of bacterial cellulose as it forms. Embedding fibers of ordinary cellulose creates composites with enhanced strength and the toughness of bacterial cellulose. Purified cellulose and elongated fibers from paper are incorporated differently than are spherical particles such as silica gel. About 90% of the final cellulose can come from scrap paper, and dried composite sheets were much stronger than plain bacterial cellulose per unit area.

Bioreactors↗
PubMed2004

Improvement of cotton fiber quality by transforming the acsA and acsB genes into Gossypium hirsutum L. by means of vacuum infiltration.

A novel method for the genetic transformation of cotton pollen by means of vacuum infiltration and Agrobacterium-mediated transformation is reported. The acsA and acsB genes, which are involved in cellulose synthesis in Acetobacter xylinum, were transferred into pollen grains of brown cotton with the aim of improving its fiber quality by incorporating useful prokaryotic features into the colored cotton plants. Transformation was carried out in cotton pollen-germinating medium, and transformation was mediated by vector pCAMBIA1301, which contains a reporter gene beta-glucuronidase (GUS), a selectable marker gene, hpt, for hygromycin resistance and the genes of interest, acsA and acsB. The integration and expression of acsA, acsB and GUS in the genome of transgenic plants were analyzed with Southern blot hybridization, PCR, histochemical GUS assay and Northern blot hybridization. We found that following pollination on the cotton stigma transformed pollen retained its capability of double-fertilization and that normal cotton seeds were produced in the cotton ovary. Of 1,039 seeds from 312 bolls pollinated with transformed pollen grains, 17 were able to germinate and grow into seedlings for more than 3 weeks in a nutrient medium containing 50 mg/l hygromycin; eight of these were transgenic plants integrated with acsA and acsB, yielding a 0.77% transformation rate. Fiber strength and length from the most positive transformants was 15% greater than those of the control (non-transformed), a significant difference, as was cellulose content between the transformed and control plants. Our study suggests that transformation through vacuum infiltration and Agrobacterium mediated transformation can be an efficient way to introduce foreign genes into the cotton pollen grain and that cotton fiber quality can be improved with the incorporation of the prokaryotic genes acsA and acsB.

Agrobacterium tumefaciens↗
PubMed2003

Characterization of a novel cellulose synthesis inhibitor.

The physiological effects of an experimental herbicide and cellulose synthesis inhibitor, N2-(1-ethyl-3-phenylpropyl)-6-(1-fluoro-1-methylethyl)-1,3,5-triazine-2,4-diamine, called AE F150944, are described. In the aminotriazine molecular class, AE F150944 is structurally distinct from other known cellulose synthesis inhibitors. It specifically inhibits crystalline cellulose synthesis in plants without affecting other processes that were tested. The effects of AE F150944 on dicotyledonous plants were tested on cultured mesophyll cells of Zinnia elegans L. cv. Envy, which can be selectively induced to expand via primary wall synthesis or to differentiate into tracheary elements via secondary wall synthesis. The IC50 values during primary and secondary wall synthesis in Z. elegans were 3.91 x 10(-8) M and 3.67 x 10(-9) M, respectively. The IC50 in suspension cultures of the monocot Sorghum halapense (L.) Pers., which were dividing and synthesizing primary walls, was 1.67 x 10(-10) M. At maximally inhibitory concentrations, 18-33% residual crystalline cellulose synthesis activity remained, with the most residual activity observed during primary wall synthesis in Z. elegans. Addition to Z. elegans cells of two other cellulose synthesis inhibitors, 1 microM 2,6-dichlorobenzonitrile and isoxaben, along with AE F150944 did not eliminate the residual cellulose synthesis, indicating little synergy between the three inhibitors. In differentiating tracheary elements, AE F150944 inhibited the deposition of detectable cellulose into patterned secondary wall thickenings, which was correlated with delocalization of lignin as described previously for 2, 6-dichlorobenzonitrile. Freeze-fracture electron microscopy showed that the plasma membrane below the patterned thickenings of AE F150944-treated tracheary elements was depleted of cellulose-synthase-containing rosettes, which appeared to be inserted intact into the plasma membrane followed by their rapid disaggregation. AE F150944 also inhibited cellulose-dependent growth in the rosette-containing alga, Spirogyra pratensis, but it did not inhibit cellulose synthesis in Acetobacter xylinum or Dictyostelium discoideum, both of which synthesize cellulose via linear terminal complexes. Therefore, AE F150944 may inhibit crystalline cellulose synthesis by destabilizing plasma membrane rosettes.

Asteraceae↗
PubMed1999

Cloning of the Escherichia coli endo-1,4-D-glucanase gene and identification of its product.

A plasmid (pYP17) containing a genomic DNA insert from Escherichia coli K-12 that confers the ability to hydrolyze carboxymethylcellulose (CMC) was isolated from a genomic library constructed in the cosmid vector pLAFR3 in E. coli DH5alpha. A small 1.65-kb fragment, designated bcsC (pYP300), was sequenced and found to contain an ORF of 1,104 bp encoding a protein of 368 amino acid residues, with a calculated molecular weight of 41,700 Da. BcsC carries a typical prokaryotic signal peptide of 21 amino acid residues. The predicted amino acid sequence of the BcsC protein is similar to that of CelY of Erwinia chrysanthemi, CMCase of Cellulomonas uda, EngX of Acetobacter xylinum, and CelC of Agrobacterium tumefaciens. Based on these sequence similarities, we propose that the bcsC gene is a member of glycosyl hydrolase family 8. The apparent molecular mass of the protein, when expressed in E. coli, is approximately 40 kDa, and the CMCase activity is found mainly in the extracellular space. The enzyme is optimally active at pH 7 and a temperature of 40 degrees C.

Amino Acid Sequence↗
PubMed1999

Expression and biochemical characterisation of recombinant AceA, a bacterial alpha-mannosyltransferase.

Biosynthesis of repeat-unit polysaccharides and N-linked glycans proceeds by sequential transfer of sugars from the appropriate sugar donor to an activated lipid carrier. The transfer of each sugar is catalysed by a specific glycosyltransferase. The molecular basis of the specificity of sugar addition is not yet well understood, mainly because of the difficulty of isolating these proteins. In this study, the aceA gene product expressed by Acetobacter xylinum, which is involved in the biosynthesis of the exopolysaccharide acetan, was overproduced in Escherichia coli and its function was characterised. The aceA ORF was subcloned into the expression vector pET29 in frame with the S.tag epitope. The recombinant protein was identified, and culture conditions were optimised for production of the soluble protein. The results of test reactions showed that AceA is able to transfer one alpha-mannose residue from GDP-mannose to cellobiose-P-P-lipid to produce alpha-mannose-cellobiose-P-P-lipid. AceA was not able to use free cellobiose as a substrate, indicating that the pyrophosphate-lipid moiety is needed for enzymatic activity.

Amino Acid Sequence↗
PubMed1988

A biochemical chimera suggesting the existence of at least two dolichol-P-glucose:dolichol-P-P-oligosaccharide glucosyltransferases.

As previously reported, incubation of liver dolichol-P, UDP-[14C]Gal, and a particulate preparation of Acetobacter xylinum leads to the synthesis of dolichol-P-[14C]Gal (P. Romero, R. Garcia, and M. Dankert (1977) Mol. Cell. Biochem. 16, 205-212). It is now reported that upon incubation of the latter with rat liver microsomes, [14C-galactose]-Gal1Man9GlcNAc2-P-P-dolichol and [14C-galactose]Gal1Glc1Man9GlcNAc2-P-P-dolichol are formed. The galactosyl residues appeared to be (1,3)-linked in the same positions as the glucose units in the respective physiological compounds. No lipid-linked Gal1Glc2Man9GlcNAc2 was formed, thus strongly suggesting the presence of at least two dolichol-P-Glc:dolichol-P-P-oligosaccharide glucosyltransferases, only one of which is able to use dolichol-P-Gal as substrate. Incubation of the galactosylated dolichol-P-P derivatives with rat liver microsomes led to the transfer of the oligosaccharides to microsomal proteins. No endogenous, membrane-bound glycosidases were able to remove the galactose residues but mannose units were excised by endogenous neutral mannosidases.

Acetylation↗
PubMed1996

Mass spectrometric studies of the thermal decomposition of carbohydrates using 13C-labeled cellulose and glucose.

The mechanism of the thermal decomposition of carbohydrates is very important to the development of fuels, fibers, and paper products. To help gain more insight into the pyrolysis chemistry of cellulose, we have carried out experimental studies using Acetobacter xylinum cellulose grown on D-(1-13C)-glucose medium with incorporation levels of 1-13C of 14%, as determined by 13C NMR analysis. Samples of the labeled cellulose, as well as D-(1-13C)- and D-(2-13C)-glucose, were pyrolyzed under fast-heating conditions and the products analyzed by molecular beam mass spectrometry (MBMS). From the labeled cellulose samples, statistically significant levels of enrichment were observed for the pyrolysis products that occur at m/z 110, 114, 126, 144, and 191, but not at m/z 98, 60, or 31. The lack of enrichment in the latter fragments indicates that they do not incorporate C-1. Samples were treated with 0.1% aqueous KOH to favor the formation of glycolaldehyde, but even in this case this major product was not enriched. These results suggest that the m/z 60 ion is an EI fragment ion of levoglucosan, formed by loss of neutral species containing C-1. However, the m/z 191 ion was found to contain two C-1 carbons. Collision-induced dissociation results for this ion suggest that it consists of a formate group. The structure of this ion is proposed to be the protonated formate of levoglucosan at the C-4 position, derived from either a reverse aldol reaction or a (+/-)-Diels-Alder reaction. The (1-13C)-glucose pyrolysis product distribution is similar to that for (1-13C)-labeled cellulose. The (2-13C)-glucose pyrolysis product distribution shows significant contribution from C-2 at the M + 1 peaks of m/z 32, 43, 60, 73, 85, and 97, indicating major incorporations of C-2 in glycolaldehyde in contrast to the lack of incorporation of the C-1 position in this major product.

Analysis of Variance↗
PubMed1989

The microbial ecology of tape ketan fermentation.

The growth of fungi, yeasts and bacteria was followed during the fermentation of tape ketan. The tape was prepared using samples of Indonesian ragi as inoculum. Fermentation was characterized by the dominant growth of Amylomyces rouxii and Candida pelliculosa (10(5)-10(7) cfu/g), and a lesser contribution from Saccharomyces cerevisiae. Hansenula anomala grew to a limited extent during some fermentations. Bacteria of the genera Bacillus and Acetobacter contributed also to the fermentation, producing populations up to 10(5) cfu/g. Ragi was the main source of microorganisms involved in the fermentation. Tape fermented by inoculating pure cultures of Amylomyces rouxii and the yeasts, either individually or as mixtures, was not of typical quality, indicating the importance of bacteria in the overall fermentation.

Bacteria↗
PubMed1990

Microbial cellulose as a specialty chemical.

Microbial polysaccharides are extensively used commercially as gelling or suspending agents, as protective colloids or as thickening agents. Until recently, microbial cellulose producing systems such as Acetobacter xylinum, had been used largely as model systems for the study of cellulose biosynthesis. Current advances in molecular biology and biochemical engineering promise to usher microbial cellulose into the specialty chemical market. This review will highlight some of the recent progress made in our understanding of microbial cellulose biochemistry and biosynthesis, describe some of its inherent virtues and identify current unique applications of this versatile biopolymer.

Journal Article↗
PubMed2005

Bacterial cellulose as a potential scaffold for tissue engineering of cartilage.

Tissue constructs for cartilage with native mechanical properties have not been described to date. To address this need the bacterial cellulose (BC) secreted by Gluconacetobacter xylinus (= Acetobacter xylinum) was explored as a novel scaffold material due to its unusual material properties and degradability. Native and chemically modified BC materials were evaluated using bovine chondrocytes. The results indicate that unmodified BC supports chondrocyte proliferation at levels of approximately 50% of the collagen type II substrate while providing significant advantages in terms of mechanical properties. Compared to tissue culture plastic and calcium alginate, unmodified BC showed significantly higher levels of chondrocyte growth. Chemical sulfation and phosphorylation of the BC, performed to mimic the glucosaminoglycans of native cartilage, did not enhance chondrocyte growth while the porosity of the material did affect chondrocyte viability. The BC did not induce significant activation of proinflammatory cytokine production during in vitro macrophage screening. Hence, unmodified BC was further explored using human chondrocytes. TEM analysis and RNA expression of the collagen II from human chondrocytes indicated that unmodified BC supports proliferation of chondrocytes. In addition, ingrowth of chondrocytes into the scaffold was verified by TEM. The results suggest the potential for this biomaterial as a scaffold for tissue engineering of cartilage.

Animals↗
PubMed2006

Microbial cellulose--the natural power to heal wounds.

Microbial cellulose (MC) synthesized in abundance by Acetobacter xylinum shows vast potential as a novel wound healing system. The high mechanical strength and remarkable physical properties result from the unique nanostructure of the never-dried membrane. This article attempts to briefly summarize the recent developments and applications of MC in the emerging field of novel wound dressings and skin substitutes. It considers the properties of the synthesized material, its clinical performance, as well as progress in the commercialization of MC for wound care products. Efficient and inexpensive fermentation techniques, not presently available, will be necessary to produce large quantities of the polymer.

Bandages, Hydrocolloid↗
PubMed2004

Synergistic interactions between the genetically modified bacterial polysaccharide P2 and carob or konjac mannan.

Rheological studies have confirmed that the bacterial polysaccharide P2, a genetically modified variant of the Acetobacter xylinum polysaccharide acetan, undergoes synergistic gelation with either of the plant polysaccharides carob or konjac mannan. X-ray fibre diffraction data shows that P2 can form a 5-fold helical structure of pitch 4.7nm and an axial rise per disaccharide repeat of 0.92nm. Optical rotation data demonstrate that P2 undergoes a coil-helix transition in solution and that deacylation enhances the stability of the helical structure in solution. Studies made on mixtures prepared at different temperatures and ionic strengths suggest that denaturation of the P2 helix favours interaction and gelation. Deacetylation of P2 enhances gelation. X-ray diffraction data for oriented fibres prepared from deacetylated P2-konjac mannan mixed films reveal a 6-fold helical structure of pitch 5.54nm with an axial rise per disaccharide repeat also of 0.92nm. This mixed helix provides direct evidence for binding between the two polysaccharides. P2 contains two sites of acetylation: one on the backbone and one on the sidechain. The former site of acetylation inhibits helix formation for P2. It is suggested that this site of acetylation also inhibits formation of the mixed helix, explaining the enhanced gelation of mixtures on deacetylation.

Amorphophallus↗
PubMed2004

An assessment of the genotoxicity and human health risk of topical use of kojic acid [5-hydroxy-2-(hydroxymethyl)-4H-pyran-4-one].

Kojic acid (KA), a natural substance produced by fungi or bacteria, such as Aspergillus, Penicillium or Acetobacter spp, is contained in traditional Japanese fermented foods and is used as a dermatological skin-lightening agent. High concentrations of KA (>or=1000 microg/plate) were mutagenic in S. typhimurium strains TA 98, TA 100, TA 1535, TA102 and E. coli WP2uvrA, but not in TA 1537. An Ames test following the "treat and plate" protocol was negative. A chromosome aberration test in V79 cells following a robust protocol showed only a marginal increase in chromosome aberrations at cytotoxic concentrations after prolonged (>or=18 h) exposure. No genotoxic activity was observed for hprt mutations either in mouse lymphoma or V79 cells, or in in vitro micronucleus tests in human keratinocytes or hepatocytes. All in vivo genotoxicity studies on KA doses were negative, including mouse bone marrow micronucleus tests after single or multiple doses, an in vivo/in vitro unscheduled DNA synthesis (UDS) test, or a study in the liver of the transgenic Muta(TM) Mouse. On the basis of pharmacokinetic studies in rats and in vitro absorption studies in human skin, the systemic exposure of KA in man following its topical application is estimated to be in the range of 0.03-0.06 mg/kg/day. Comparing these values with the NOAEL in oral subchronic animal studies (250 mg/kg/day), the calculated margin of safety would be 4200- to 8900-fold. Comparing human exposure with the doses that were negative for micronuclei, UDS and gene mutations in vivo, the margins of safety are 16000 to 26000-fold. In conclusion, the topical use of KA as a skin lightening agent results in minimal exposure that poses no or negligible risk of genotoxicity or toxicity to the consumer.

Administration, Topical↗
PubMed2006

J1 acylase, a glutaryl-7-aminocephalosporanic acid acylase from Bacillus laterosporus J1, is a member of the alpha/beta-hydrolase fold superfamily.

J1 acylase, a glutaryl-7-aminocephalosporanic acid acylase (GCA) isolated from Bacillus laterosporus J1, has been conventionally grouped as the only member of class V GCA, although its amino acid sequence shares less than 10% identity with members of other classes of GCA. Instead, it shows higher sequence similarities with Rhodococcus sp. strain MB1 cocaine esterase (RhCocE) and Acetobacter turbidans alpha-amino acid ester hydrolase (AtAEH), members of the alpha/beta-hydrolase fold superfamily. Homology modeling and secondary structure prediction indicate that the N-terminal region of J1 acylase has an alpha/beta-hydrolase folding pattern. The catalytic triads in RhCocE and AtAEH were identified in J1 acylase as S125, D264 and H309. Mutations to alanine at these positions were found to completely inactivate the enzyme. These results suggest that J1 acylase is a member of the alpha/beta-hydrolase fold superfamily with a serine-histidine-aspartate catalytic triad.

Amidohydrolases↗
PubMed2004

Characterization of bacterial diversity in pulque, a traditional Mexican alcoholic fermented beverage, as determined by 16S rDNA analysis.

The bacterial diversity in pulque, a traditional Mexican alcoholic fermented beverage, was studied in 16S rDNA clone libraries from three pulque samples. Sequenced clones identified as Lactobacillus acidophilus, Lactobacillus strain ASF360, L. kefir, L. acetotolerans, L. hilgardii, L. plantarum, Leuconostoc pseudomesenteroides, Microbacterium arborescens, Flavobacterium johnsoniae, Acetobacter pomorium, Gluconobacter oxydans, and Hafnia alvei, were detected for the first time in pulque. Identity of 16S rDNA sequenced clones showed that bacterial diversity present among pulque samples is dominated by Lactobacillus species (80.97%). Seventy-eight clones exhibited less than 95% of relatedness to NCBI database sequences, which may indicate the presence of new species in pulque samples.

Agave↗
PubMed2006

Study on the microflora and biochemistry of cocoa fermentation in the Dominican Republic.

Cocoa fermentation was monitored at the IDIAF (Instituto Dominicano de Investigaciones Agropecuarias y Forestales) "Mata Larga" experimental station, in San Francisco de Macoris, Dominican Republic. The maximum average fermentation temperature reached 51 degrees C after 48 h and the pH reached 4.5 after 144 h of fermentation. A significant decrease in glucose, fructose and citric acid was seen in the pulp over the first 48 h. There was a delay of 24 h between maximum microbial growth and maximum concentrations of the respective metabolites, which occurred after 48 h for ethanol and after 72 h for acetic acid. A maximum concentration in lactic acid was found after around 120 h of fermentation. The aerobic mesophilic flora increased from 6.1x10(6) to a maximum of 4.2x10(7) CFU g(-1) of dry matter after 48 h of fermentation. Yeasts displayed maximum development after 24 h (6.1x10(7) CFU g(-1) of dry matter), whilst for lactic and acetic acid bacteria it occurred after 48 h (7.3x10(7) and 1.5x10(8) CFU g(-1) of dry matter respectively). The yeasts isolated belonged to the genera Hanseniaspora and Candida, the lactic acid bacteria to the genus Lactobacillus, and the acetic acid bacteria to the genus Acetobacter. The differences compared to other fermentation trials concerned the micropopulation from a qualitative point of view.

Bacteria, Aerobic↗