lichenin  (Valiant)


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  • 91
    Name:
    Lichenan
    Description:
    Lichenan
    Catalog Number:
    02155231-cf
    Price:
    None
    Applications:
    Glucose polysaccharide
    Category:
    Life Sciences Biochemicals Carbohydrates Polysaccharides
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    Structured Review

    Valiant lichenin
    Lichenan
    Lichenan
    https://www.bioz.com/result/lichenin/product/Valiant
    Average 91 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    lichenin - by Bioz Stars, 2021-02
    91/100 stars

    Images

    1) Product Images from "β-Glucanase Activity of the Oral Bacterium Tannerella forsythia Contributes to the Growth of a Partner Species, Fusobacterium nucleatum, in Cobiofilms"

    Article Title: β-Glucanase Activity of the Oral Bacterium Tannerella forsythia Contributes to the Growth of a Partner Species, Fusobacterium nucleatum, in Cobiofilms

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.01759-17

    Expression and confirmation of enzyme activity of the recombinant protein. (A) Coomassie-stained 10% SDS-PAGE gel of purified protein fractions (10 μg total protein per lane). Lane 1, glutathione-agarose-purified GST-tagged rTfGlcA; lane 2, recombinant β-glucanase protein (rTfGlcA) after thrombin treatment of fusion protein and glutathione-agarose chromatography; lane 3, GST protein eluted from glutathione agarose column. (B) Detection of glucanase activity by zymography on 10% SDS-PAGE gels containing 0.1% lichenin and stained with Congo red. Lane 1, GST-rTfGlcA; lane 2, GST-released rTfGlcA; lane 3, GST. (C) Detection of glucanase activity by TLC was performed for evaluation of β-glucan hydrolyzation by rTfGlcA. Plate 1, subjected to mobile phase comprising 1-propanol:2% boric acid: acetic acid, 40:5:1; plate 2, subjected to mobile phase comprising chloroform:acetic acid:water, 3:3.5:0.5. Lanes: G, 0.2% glucose; S, 0.2% sucrose; L, 0.2% lichenin; Lβ, commercial β-glucanase treated 0.2% lichenin; LrTfG, rTfGlcA treated with 0.2% lichenin.
    Figure Legend Snippet: Expression and confirmation of enzyme activity of the recombinant protein. (A) Coomassie-stained 10% SDS-PAGE gel of purified protein fractions (10 μg total protein per lane). Lane 1, glutathione-agarose-purified GST-tagged rTfGlcA; lane 2, recombinant β-glucanase protein (rTfGlcA) after thrombin treatment of fusion protein and glutathione-agarose chromatography; lane 3, GST protein eluted from glutathione agarose column. (B) Detection of glucanase activity by zymography on 10% SDS-PAGE gels containing 0.1% lichenin and stained with Congo red. Lane 1, GST-rTfGlcA; lane 2, GST-released rTfGlcA; lane 3, GST. (C) Detection of glucanase activity by TLC was performed for evaluation of β-glucan hydrolyzation by rTfGlcA. Plate 1, subjected to mobile phase comprising 1-propanol:2% boric acid: acetic acid, 40:5:1; plate 2, subjected to mobile phase comprising chloroform:acetic acid:water, 3:3.5:0.5. Lanes: G, 0.2% glucose; S, 0.2% sucrose; L, 0.2% lichenin; Lβ, commercial β-glucanase treated 0.2% lichenin; LrTfG, rTfGlcA treated with 0.2% lichenin.

    Techniques Used: Expressing, Activity Assay, Recombinant, Staining, SDS Page, Purification, Chromatography, Zymography, Thin Layer Chromatography

    T. forsythia glucanase activity promoted T. forsythia - F. nucleatum cobiofilm formation by hydrolyzing lichenin. Monospecies ( T. forsythia or F. nucleatum ) and dual-species ( T. forsythia wild-type or glcA deletion mutant with F. nucleatum ) biofilms were formed in black-well cell culture plate wells under three culture conditions: T, T medium; T-L, T medium with 0.2% lichenin; and T-Lβ, T medium with 0.2% commercial β-glucanase (from Trichoderma longibrachiatum EC 3.2.1.6, Sigma)-treated lichenin. Total biofilm mass was estimated by DAPI staining. Tf WT, T. forsythia wild type; Fn, F. nucleatum . Bars represent mean ± SD. This experiment repeated 3 times yielded similar results. *, P
    Figure Legend Snippet: T. forsythia glucanase activity promoted T. forsythia - F. nucleatum cobiofilm formation by hydrolyzing lichenin. Monospecies ( T. forsythia or F. nucleatum ) and dual-species ( T. forsythia wild-type or glcA deletion mutant with F. nucleatum ) biofilms were formed in black-well cell culture plate wells under three culture conditions: T, T medium; T-L, T medium with 0.2% lichenin; and T-Lβ, T medium with 0.2% commercial β-glucanase (from Trichoderma longibrachiatum EC 3.2.1.6, Sigma)-treated lichenin. Total biofilm mass was estimated by DAPI staining. Tf WT, T. forsythia wild type; Fn, F. nucleatum . Bars represent mean ± SD. This experiment repeated 3 times yielded similar results. *, P

    Techniques Used: Activity Assay, Mutagenesis, Cell Culture, Staining

    Induction of β-glucanase activity in T. forsythia in response to F. nucleatum . T. forsythia wild-type cells were incubated with increasing concentrations of F. nucleatum cell extracts (2.5, 5, and 10 mg/ml) and β-glucanase activity in cell lysates of T. forsythia was assayed by lichenin-agar zymography assay in a 96-well microplate. Untreated lichenin-agar wells were used as background and β-glucanase-enzyme-treated wells were used as positive controls. Bars represent mean ± standard deviation (SD) from a representative experiment repeated 3 times, yielding similar results. *, P
    Figure Legend Snippet: Induction of β-glucanase activity in T. forsythia in response to F. nucleatum . T. forsythia wild-type cells were incubated with increasing concentrations of F. nucleatum cell extracts (2.5, 5, and 10 mg/ml) and β-glucanase activity in cell lysates of T. forsythia was assayed by lichenin-agar zymography assay in a 96-well microplate. Untreated lichenin-agar wells were used as background and β-glucanase-enzyme-treated wells were used as positive controls. Bars represent mean ± standard deviation (SD) from a representative experiment repeated 3 times, yielding similar results. *, P

    Techniques Used: Activity Assay, Incubation, Zymography, Standard Deviation

    T. forsythia glucanase activity in T. forsythia-F . nucleatum cobiofilms specifically promoted F. nucleatum biomass (A and B) Biofilm biomass of T. forsythia and F. nucleatum in cobiofilms in T medium with 0.2% lichenin was calculated by in situ staining using bacterium-specific probes, followed by confocal laser scanning microscopy. F. nucleatum and T. forsythia probes were labeled with Cy5 and FITC, respectively. F. nucleatum (A) and T. forsythia (B) biomass volumes (μm 3 /μm 2 ) were estimated from confocal images with Comstat 2 software. Confocal images of Tf + Fn cobiofilm in the presence of 0.2% lichenin in T medium are shown in (C) and (D). (C) T. forsythia wild-type and F. nucleatum cobiofilm. (D) T. forsythia glcA -deficient strain with F. nucleatum cobiofilm. T. forsythia was stained with FITC-labeled specific DNA probe (green) and F. nucleatum was stained with Cy5-labeled specific DNA probe (red). Both confocal images were taken at 200×. *, P
    Figure Legend Snippet: T. forsythia glucanase activity in T. forsythia-F . nucleatum cobiofilms specifically promoted F. nucleatum biomass (A and B) Biofilm biomass of T. forsythia and F. nucleatum in cobiofilms in T medium with 0.2% lichenin was calculated by in situ staining using bacterium-specific probes, followed by confocal laser scanning microscopy. F. nucleatum and T. forsythia probes were labeled with Cy5 and FITC, respectively. F. nucleatum (A) and T. forsythia (B) biomass volumes (μm 3 /μm 2 ) were estimated from confocal images with Comstat 2 software. Confocal images of Tf + Fn cobiofilm in the presence of 0.2% lichenin in T medium are shown in (C) and (D). (C) T. forsythia wild-type and F. nucleatum cobiofilm. (D) T. forsythia glcA -deficient strain with F. nucleatum cobiofilm. T. forsythia was stained with FITC-labeled specific DNA probe (green) and F. nucleatum was stained with Cy5-labeled specific DNA probe (red). Both confocal images were taken at 200×. *, P

    Techniques Used: Activity Assay, In Situ, Staining, Confocal Laser Scanning Microscopy, Labeling, Software

    Related Articles

    Electrophoresis:

    Article Title: Extracellular Secretion of Noncatalytic Plant Cell Wall-Binding Proteins by the Cellulolytic Thermophile Caldicellulosiruptor bescii
    Article Snippet: .. Each protein (3 μg) was analyzed by electrophoresis under native conditions in a 16% (wt/vol) acrylamide gel (pH 5.4 to 5.6) containing 120 mM potassium acetate and 0.1 mg/ml of one of the following: lichenan, a soluble polysaccharide from Cetraria islandica (MP Biomedicals, Inc., CA); xyloglucan from tamarind (Megazyme); soluble xylan from beechwood (Sigma-Aldrich); glucuronoxylan (4- O -methyl- d -glucurono- d -xylan; Sigma-Aldrich); locust bean gum (galactomannan; Wako, Osaka, Japan); glucomannan from konjac (Megazyme); pectin from citrus (Nacalai Tesque). .. The electrophoresis was conducted at 10 mA and 25°C for 2.5 to 3 h using running buffer (pH 3.8 to 4.0) consisting of 27 mM acetic acid and 70 mM alanine.

    Acrylamide Gel Assay:

    Article Title: Extracellular Secretion of Noncatalytic Plant Cell Wall-Binding Proteins by the Cellulolytic Thermophile Caldicellulosiruptor bescii
    Article Snippet: .. Each protein (3 μg) was analyzed by electrophoresis under native conditions in a 16% (wt/vol) acrylamide gel (pH 5.4 to 5.6) containing 120 mM potassium acetate and 0.1 mg/ml of one of the following: lichenan, a soluble polysaccharide from Cetraria islandica (MP Biomedicals, Inc., CA); xyloglucan from tamarind (Megazyme); soluble xylan from beechwood (Sigma-Aldrich); glucuronoxylan (4- O -methyl- d -glucurono- d -xylan; Sigma-Aldrich); locust bean gum (galactomannan; Wako, Osaka, Japan); glucomannan from konjac (Megazyme); pectin from citrus (Nacalai Tesque). .. The electrophoresis was conducted at 10 mA and 25°C for 2.5 to 3 h using running buffer (pH 3.8 to 4.0) consisting of 27 mM acetic acid and 70 mM alanine.

    Zymography:

    Article Title: β-Glucanase Activity of the Oral Bacterium Tannerella forsythia Contributes to the Growth of a Partner Species, Fusobacterium nucleatum, in Cobiofilms
    Article Snippet: .. Briefly, for agar plate zymography, 10 μl of cell suspension from early-log-phase cultures of E. coli , T. forsythia , and F. nucleatum were spotted on LB agar (for E. coli ) or BF agar (for T. forsythia and F. nucleatum ) plates containing 0.1% lichenin (rich in β-1,3 with few β-1,4 glycosidic bonds; MP Bio, Santa Ana, CA). .. Plates were incubated aerobically overnight at 37°C for E. coli harboring pGEX-rTfGlcA and anaerobically for 1 week for T. forsythia and F. nucleatum strains.

    Activity Assay:

    Article Title: Genome-wide characterization of cellulases from the hemi-biotrophic plant pathogen, Bipolaris sorokiniana, reveals the presence of a highly stable GH7 endoglucanase
    Article Snippet: .. Substrate specificity and kinetic parameters of BsGH7-3 with CMC as a substrate The specificity of BsGH7-3 was determined by measuring specific activity across a range of substrates, namely lichenan (MP Biomedicals, Ohio, USA), β-d -glucan from barley, Avicel PH-101, CMC (Sigma-Aldrich, Saint Louis, USA) and phosphoric acid swollen cellulose (PASC). ..