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At least 19 recordsLinked to original sources
PubMed2026

A Reduced-Acidification Phenotype Simplifies Strain Engineering in Komagataeibacter and Enables One-Step Production of Melanated Bacterial Cellulose.

Komagataeibacter species are among the highest-yielding bacterial cellulose producers and offer a promising platform for the genetic engineering of functionalized bacterial cellulose. However, routine strain engineering remains limited by inefficient screening of genomic integrants and acidic culture conditions that inhibit acid-sensitive cellulose modifications. Here, we exploited the reduced-acidification phenotype of a Komagataeibacter sucrofermentans glucose dehydrogenase deletion mutant (Δgdh) to overcome both limitations. We developed a simple phenotypic screen based on reduced acidification to identify candidate colonies for subsequent molecular confirmation. We further exploited this phenotype by constructing a Δgdh::tyr1 strain that, after optimizing culture conditions, produced melanated bacterial cellulose in a single step, without the manual pH neutralization required by previous methods. Together, these results establish reduced acidification as a practical engineering phenotype that simplifies strain engineering and enables acid-sensitive modification of bacterial cellulose, thereby expanding the range of bacterial cellulose modifications achievable in Komagataeibacter.

Komagataeibacter sucrofermentans↗
PubMed1992

Susceptibilities of bacterial cellulose containing N-acetylglucosamine residues for cellulolytic and chitinolytic enzymes.

Detailed characterization of enzyme susceptibility of bacterial cellulose containing N-acetylglucosamine (GlcNAc) residues (N-AcGBC) which possess high susceptibility for cellulase and lysozyme and slight susceptibility for chitinase was studied. Turbidimetric lysozyme assay of N-AcGBC showed that (i) the susceptibilities of various N-AcGBCs for lysozyme were proportional to GlcNAc content, and (ii) N-AcGBC homogenates were divided into two groups based on the rate of turbidity reduction (not dependent on GlcNAc content). High reactivity of N-AcGBC for lysozyme would arise from fine microfibrils characteristic of bacterial cellulose (BC) and random distribution of GlcNAc residues in N-AcGBC because water soluble oligomers of N-AcGBC produced by lysozymic hydrolysis did not inhibit lysozyme activity; however, the random distribution of GlcNAc seemed to result in the slight susceptibility of N-AcGBC for chitinase. The rate of cellulolytic turbidity reduction of N-AcGBC was slower than that of BC, which arose from the inhibition for binding of cellulase by GlcNAc residues.

Acetobacter↗
PubMed1975

[Biosynthesis of bacterial cellulose from glucose selectively deuterated in position 6: NMR study].

D-glucose specifically deuterated at C-6 was prepared and used for the biosynthesis of bacterial cellulose with Acetobacter xylinum. The material obtained was converted into glucitol hexaacetate and analyzed by 250 MHz n.m.r. and mass spectrometry. These spectra indicated that about 70% of the starting D-glucose was incorporated without modification of deuteriation at the C-6 position. However an explanation is required of the finding that deuterium was also incorporated at the C-2 and C-1 positions of the cellulose, arising respectively from the 6 pro-R and 6 pro-S positions of the initial D-glucose.

Acetobacter↗
PubMed1976

Diethylaminoethyl-cellulose-bacterial cell immunoadsorbent columns: preparation of serotype-specific globulin and immunofluorescent conjugates for Streptococcus mutans serotypes a and d.

Diethylaminoethyl (DEAE)-cellulose was used as a support material for preparing bacterial cell columns. Pretreatment of the bacterial cells with formalin was essential in obtaining satisfactory adherence of the cells to DEAE-cellulose. Cross-reacting antibodies were removed from antibody preparations against strains of Streptococcus mutans serotypes a and d by adsorption on appropriate bacterial cell columns. S. mutans serotype d was further divided into two subtypes on the basis of immunofluorescent staining with conjugates of immunospecifically adsorbed immunoglobulin G. The DEAE-cellulose-bacterial cell columns were regenerated after use by desorbing the cross-reacting antibodies with low-pH buffer and were used repeatedly over and 18-month period with no detectable loss in effectiveness.

Adsorption↗
PubMed1976

Improvement in specificity of immunofluorescent reagents for identifying Streptococcus mutans by DEAE-cellulose-bacterial cell column immunosorption methods.

We have described a new method for preparing bacterial cell columns, in which DEAE-cellulose is used as the cell support material. The columns can be used to isolate pure antibody or to remove cross-reacting antibodies from immune IgG. The columns are remarkable stable, can be scaled up to any desired dimensions, and should be suitable for large-scale production of highly specific serological reagents. The method is practical for obtaining serotype-specific and polyvalent IF reagents for identifying S. mutans organisms. However, the method could also be used as a tool for sophisticated studies of antigenic relationships that exist among these and other taxonomic groups of microorganisms.

Antibodies, Bacterial↗
PubMed1992

[Food hygienic indexes on biodegradable polymers].

Current specifications for food packaging made of polyolefine plastics were applied to biodegradable plastics. No lead and cadmium were detected in any biodegradable plastic samples with the exception of bacterial cellulose, which contained trace amounts of lead and cadmium. Potassium permanganate consumption amount was less than the current specification level for polyofines. Sugars leached from bacterial cellulose was 22 +/- 1 microgram per 100 cm2 as glucose, and amino acids leached from poly-gamma-methylglutamate films was 8 +/- 3 micrograms per 100 cm2 as glutamic acid.

Amino Acids↗
PubMed1992

Inhibition of lipopolysaccharide synthesis in Agrobacterium tumefaciens and Aeromonas salmonicida.

Lipopolysaccharide (LPS) synthesis was inhibited, new lipid A metabolites accumulated, and growth ceased, when the plant pathogen Agrobacterium tumefaciens and the fish pathogen Aeromonas salmonicida were treated with an antibacterial agent which specifically inhibits CTP:CMP-3-deoxy-manno-octulosonate cytidylyltransferase (CMP-KDO synthase). The new lipid A metabolites were purified by chromatography on DEAE-cellulose and chemically analysed. Metabolites isolated from both bacterial species contained glucosamine and phosphate in a 1:1 molar ratio, and 3-OH-C14:0 was the major fatty acid present (1 mol and 1.4 mol per mol glucosamine for A. tumefaciens and A. salmonicida, respectively). Inhibition of LPS synthesis by CMP-KDO synthase inhibitor had no effect on the initial kinetics of A. tumefaciens attachment to cultured carrot cells, but did inhibit cell aggregation normally induced by bacterial cellulose synthesis. Bacteria treated with inhibitor remained viable and able to synthesize protein at 15% the rate of control cells, indicating that the lack of cellulose-induced aggregation was not due to the inability of bacteria to make protein, but rather the inability to respond normally to the bacterial-plant cell interaction.

Aeromonas↗
PubMed2026

A black soybean yoghurt fermented with a reusable probiotic cellulose gel: beneficial effects and metabolic characteristics.

The demand for plant-based yoghurts is continuously increasing. However, achieving stable physicochemical properties and acceptable flavor of the plant-based yoghurts remains challenging. In our previous work, we encapsulated Lactiplantibacillus plantarum (L. plantarum) LCC-605 biofilm into bacterial cellulose (BC), obtaining a LP605@BC gel. LP605@BC gel exhibited excellent harsh-environment resistance abilities and storage stability, and is very suitable as a starter culture. In this work, we used LP605@BC as a starter culture to prepare the fermented plant-based yoghurt (e.g., black soybean yoghurt, BSY-LP605@BC). After fermentation, the inverted nonflowing yoghurt was formed due to the strong interaction between protein and exopolysaccharide (EPS) produced by LCC-605 during fermentation. In addition, the water holding capacity (67.2%) of BSY-LP605@BC was also greatly improved. The viable bacterial counts in BSY-LP605@BC reached 11.2 log CFU/mL after 21 days of storage. BSY-LP605@BC showed increased antioxidant, cholesterol-lowering abilities, and hypoglycemic potential compared with the unfermented black soybean milk. Interestingly, LP605@BC could be reused at least 5 times, demonstrating excellent sustainability. Significant metabolomic differences between BSY-LP605@BC and the black soybean milk were observed via untargeted metabolomic analysis, further proving the beneficial effects of BSY-LP605@BC. Overall, our work developed an effective reusable starter culture for preparing the plant-based yoghurt in a sustainable manner, providing a new design direction and form of starter culture.

Yogurt↗
PubMed1979

Additional properties of a soluble polymer of glucose from cultures of Acetobacter xylinum.

The results of differential, thermal analysis of a soluble, beta (1 leads to 2)-branched, beta (1 leads to 4)-D-glucan isolated from cultures of Acetobacter xylinum are consistent with previous conclusions about its structure. The O-acetyl content of the polymer is 8.3% which corresponds to a maximum substitution of one acetyl group per three glucose residues. Proton nuclear magnetic resonance spectra confirm that all the glycosidic bonds are beta linkages. Some preparations of the polymer are contaminated by another polymer containing mannose and rhamnose. No evidence was obtained to support a previous suggestion that the branched D-glucan is a precursor of bacterial cellulose and this suggestion is now withdrawn.

Glucans↗
PubMed1992

The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats.

Endoglucanase C (CenC) from Cellulomonas fimi binds to cellulose and to Sephadex. The enzyme has two contiguous 150-amino-acid repeats (N1 and N2) at its N-terminus and two unrelated contiguous 100-amino-acid repeats (C1 and C2) at its C-terminus. Polypeptides corresponding to N1, N1N2, C1, and C1C2 were produced by expression of appropriate cenC gene fragments in Escherichia coli. N1N2, but not N1 alone, binds to Sephadex; both polypeptides bind to Avicel, (a heterogeneous cellulose preparation containing both crystalline and non-crystalline components). Neither C1 nor C1C2 binds to Avicel or Sephadex. N1N2 and N1 bind to regenerated ('amorphous') cellulose but not to bacterial crystalline cellulose; the cellulose-binding domain of C. fimi exoglucanase Cex binds to both of these forms of cellulose. Amino acid sequence comparison reveals that N1 and N2 are distantly related to the cellulose-binding domains of Cex and C. fimi endoglucanases A and B.

Actinomycetales↗
PubMedDate not supplied

[Effect of inorganic electron acceptors on the bacterial formation of methane from cellulose].

The effect of nitrate, nitrogen oxide, sulphate, oxidized iron and manganese on the methane fermentation of cellulose was studied with the enrichment bacterial culture. The action of these oxidants on the enrichment culture growing on cellulose was compared to that on a pure methanosarcina culture in order to find out which stage of methane formation from cellulose was inhibited. Nitrate at the concentration of 2 g NaNO3 and more per litre of the medium inhibited the whole process of fermentation; at the concentration less than 2 g/l the production of methane was inhibited, and cellulose decomposition was accompanied with denitrification. Sulphate at the concentration of 2 g MgSO4 per litre had no effect on the formation of methane but the process was inhibited by the product of its reduction, i. e. sulphiade. Cellulose decomposition could be accompanied with sulphate reduction if sulphide produced in the process of the reduction were removed from the medium. In this case as well as in the presence of ferric iron, the production of methane was inhibited due to competition for the reducing agent.

Cellulose↗
PubMed1976

[Use of Soviet semipermeable acetate-cellulose membranes for concentration and purification of typhoid antigens].

A study was made of a possibility of using Soviet made membranes "Vladipor" with a pore diameter of 16--17 nm for the purpose of concentration and purification of antigenic extracts from stab cultures of S. typhi obtained by the action of typsin, hydrogen peroxide and detergents. Preparations, complete by antigenic structure, were obtained by ultrafiltration, with a good yield. The maximal rate of ultrafiltration was noted in case of "peroxide" antigenic preparations. The use of diafiltration provided a significant reduction of the ash content in the end products.

Acetates↗
PubMed1975

Isolation of bacterial and phage proteins by homopolymer RNA-cellulose chromatography.

Nucleic acid-free extracts of Escherichia coli have been analyzed by chromatography on columns of cellulose, to which poly(A), poly(U), or poly(C) have been attached by ultraviolet irradiation. Proteins are released from the columns by stepwise elution with increasingly higher concentrations of salt, followed by washing with urea to remove very tightly bound molecules. The pattern of protein elution is reproducibly different for each of the homopolymer RNA-cellulose columns used: some proteins bind very tightly to one column, but poorly to others. Analysis by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis, by immunological cross-reactivity in double diffusion tests, and by enzymological assays, has allowed the identification of a number of these proteins. The RNA polymerase core enzyme binds to poly(C)- and to poly(U)-cellulose columns, and can be purified to 20 to 30 percent homogeneity in a single step. Ribosomal protein S1 and the termination factor rho bind very tightly to poly(C)-cellulose, and both can be purified to homogeneity rapidly, in much higher yields than previously reported. Poly(A)-cellulose chromatography allows the isolation of large amounts of an 80,000 molecular weight protein having an as yet unassigned cellular function. The host factor required for RNA phage Qbeta RNA replication in vitro can also be obtained from poly(A)-cellulose, and chromatography of extracts of phage Qbeta-infected E. coli on RNA-cellulose columns results in very rapid isolation of the Qbeta replicase enzyme. Homopolymer RNA-cellulose chromatography thus appears to be a simple, general technique, useful for the efficient isolation of a variety of RNA-binding proteins.

Bacterial Proteins↗
PubMed1992

Optimal chemical control of populations developing drug resistance.

A system of differential equations for the control of the growth of certain populations by the use of chemical treatment is presented. Rather general growth rates and kill rates of drugs, as well as drug resistance, are considered. A class of optimal control problems with a performance criterion depending on a parameter is formulated and shown to admit the same basic optimal strategy. Applications to cycle nonspecific chemotherapy and control of the growth of bacterial populations in cellulose media in paper production plants are described.

Antineoplastic Agents↗