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Xyloglucan

Xyloglucan is a hemicellulose found in the primary cell walls of most land plants.
It is composed of a glucan backbone with xylose side chains and plays a crucial role in cell wall structure and dynamics.
Xyloglucan is involved in plant growth, development, and responses to environmental stresses.
Understaning the properties and functions of xyloglucan is important for optimizzing plant productivity and adaptability.
PubCompare.ai can help researchers effortlessly locate and compare the most relevant xyloglucan protocols from scientific literature, preprints, and patents to enhance the reproducibilty and accuacy of their studies.

Most cited protocols related to «Xyloglucan»

1
Plant Cell Wall Immunolabeling Protocol
Cited 29 times
Tamarind (Tamarindus indica L.) seeds were obtained from Jungle Seeds, Watlington, UK) and nasturtium (Tropaeolum majus L. cv Tom Thumb) seeds from Mr. Fothergill's Seeds Ltd., Newmarket, UK. Tamarind and nasturtium seeds were imbibed for 24 h and then pieces of cotyledon parenchyma were excised, fixed and prepared for embedding in LR White resin with subsequent sectioning for indirect immunofluorescence analysis as described previously [8 (link)]. Tobacco (Nicotiana tabacum L.) and pea (Pisum sativum L.) plants were grown in a greenhouse with 16 h days and maintained between 19 and 23°C. Regions of second internodes from the top of six-week old plants were fixed, embedded in wax and sectioned as described previously [46 (link)].
In addition to LM15, three further monoclonal antibodies were used in this study using indirect immunofluorescence: CCRCM1, a mouse monoclonal antibody to a fucosylated epitope of xyloglucan [19 (link)], a gift from Dr. Michael Hahn (CCRC, University of Georgia, USA), JIM5, a rat monoclonal antibody to methyl-esterified and unesterified epitopes of HG [32 (link)] and LM6, a rat monoclonal antibody to arabinan [34 (link)]. Section pre-treatment to remove HG from cell walls involved incubation of sections with a recombinant microbial pectate lyase 10A [47 (link)] (a gift from Prof. Harry Gilbert, University of Newcastle-upon-Tyne) at 10 μg/mL for 2 h at room temperature in 50 mM N-cyclohexyl-3-aminopropane sulfonic acid (CAPS), 2 mM CaCl2 buffer at pH 10 as described [10 (link)]. The high pH of the enzyme buffer removes HG methyl esters in cell walls and results in HG being susceptible to pectate lyase degradation and also suitable for recognition by JIM5. Sections not treated with the pectate lyase were incubated for an equivalent time with the high pH buffer without enzyme and imaged as untreated controls. After enzyme or buffer treatment, sections were incubated in phosphate-buffered saline (PBS) containing 5% (w/v) milk protein (MP/PBS) and a 5-fold dilution of antibody hybridoma supernatant for 1.5 h. Samples were then washed in PBS at least 3 times and incubated with a 100-fold dilution of anti-rat IgG (whole molecule), or anti-mouse IgG, linked to fluorescein isothiocyanate (FITC, Sigma, UK) in MP/PBS for 1.5 h in darkness. The samples were washed in PBS at least 3 times and incubated with Calcofluor White (0.2 μg/mL) (Fluorescent Brightner 28, Sigma, UK) for 5 min in darkness. Samples were washed at least 3 times and then mounted in a glycerol-based anti-fade solution (Citifluor AF1, Agar Scientific, UK). Immunofluorescence was observed with a microscope equipped with epifluorescence irradiation and DIC optics (Olympus BX-61). Images were captured with a Hamamatsu ORCA285 camera and Improvision Volocity software.
Marcus S.E., Verhertbruggen Y., Hervé C., Ordaz-Ortiz J.J., Farkas V., Pedersen H.L., Willats W.G, & Knox J.P. (2008). Pectic homogalacturonan masks abundant sets of xyloglucan epitopes in plant cell walls. BMC Plant Biology, 8, 60.
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Publication 2008
2
Genetic Manipulation of B. ovatus
Cited 19 times
The locus tags of the genes involved in the present study and the corresponding DNA primers used for knock-out, sequence alteration and qPCR studies are given in Supplementary Table S1. To construct gene deletions in B. ovatus strain ATCC 8483, a deletion of the gene encoding thymidine kinase (tdk; Bacova_03071) was first constructed using an identical strategy to that used previously for B. thetaiotaomicron.31 (link) All subsequent gene deletions and sequence modifications were conducted in a Δtdk strain background by allelic exchange using the vector pExchange-tdk31 (link) and primers listed in Supplementary Table S1. Wild-type Bacteroides ovatus ATCC 8483, all mutant derivatives and other Bacteroidetes species tested were grown in tryptone-yeast extract-glucose (TYG) medium, brain-heart infusion agar supplemented with 10% horse blood, or minimal media (MM) supplemented with appropriate carbohydrates as previously described.32 (link) Antibiotics were added as needed: gentamicin (200 μg ml−1), erythromycin (25 μg ml−1), and 5-fluoro-2′-deoxyuridine (200 μg ml−1). To prepare cells for exposure to glycans, wild-type and mutant B. ovatus were grown in TYG, subcultured into MM-glucose, grown to mid-exponential phase (OD600 0.6–0.8), then washed and resuspended in 2x MM prior to addition of the appropriate glycan. Xyloglucan substrates are described below and all carbohydrate stocks were prepared at 10 mg/ml in ddH2O and sterilized by autoclaving. All quantitative growth was performed at 37°C in an anaerobic chamber (Coy Manufacturing, Grass Lake, MI; 10 % H2, 5 % CO2 and 85 % N2) in an automated plate reading device as described previously.33 (link) In instances where bacterial growth data are either used to show growth curves or quantify differences in growth ability, strains were grown in 2–3 biological replicates. Fluorescence microscopy was performed on fixed B. ovatus cells grown to early exponential phase (A600 = 0.25–0.35) in minimal medium containing a 9:1 mixture of limit XyG oligosaccharides (XGOs) to slightly longer (average dp = 14) XGOs (see Substrates section below). These conditions circumvented the reduced growth rate of the ΔGH5 mutant on limit XGOs. Cells were fixed in formalin and stained with a polyclonal antibody raised in rabbit against purified recombinant BoGH5A (Cocalico Biologicals, Reamstown, PA), following the method previously reported.34 (link) The same antiserum was used to probe GH5 presence via Western blot.
Larsbrink J., Rogers T.E., Hemsworth G.R., McKee L.S., Tauzin A.S., Spadiut O., Klinter S., Pudlo N.A., Urs K., Koropatkin N.M., Creagh A.L., Haynes C.A., Kelly A.G., Cederholm S.N., Davies G.J., Martens E.C, & Brumer H. (2014). A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes. Nature, 506(7489), 498-502.
Publication 2014
3
Neoglycoprotein Synthesis and Antibody Production
Cited 10 times
A neoglycoprotein (XXXG-BSA) was prepared by coupling a heptasaccharide containing 3 xylosyl and 4 glucosyl residues (XXXG, Megazyme, Bray, Ireland) to BSA by reductive amination [42 (link)]. XXXG (30 mg) was dissolved in 1.0 ml of 0.2 M sodium borate buffer pH 9.0. This was followed by the addition of 20 mg BSA and then 30 mg of sodium cyanoborohydride. The mixture was maintained in a water bath at 50°C with occasional mixing. After 24 h the pH was adjusted to pH 4.0 by the addition of 45 μl of 80% (v/v) acetic acid. The solution was then dialysed extensively against distilled water with several changes over 4 days.
Rat immunization, hybridoma preparation and cloning procedures were performed as described previously [34 (link)]. Two male Wistar rats were injected with 100 μg XXXG-BSA in complete Freund's adjuvant administered subcutaneously on day 0, with the same amount administered with incomplete Freund's adjuvant on days 33 and 71. On day 145, a selected rat was given a prefusion boost of 100 μg XXXG-BSA in 1 ml PBS by intraperitoneal injection. The spleen was isolated three days later for isolation of lymphocytes and fusion with rat myeloma cell line IR983F [43 ]. Antibodies were selected by ELISA using tamarind xyloglucan as antigen. Subsequent characterization was by means of a glycan microarray of cell wall polymers [28 (link)] and competitive inhibition ELISAs using the xyloglucan XXXG heptasaccharide from tamarind xyloglucan and a series of related xyloglucan oligosaccharides. A mixture of the XXLG and XLXG octasaccharide isomers and the XLLG nonasaccharide were derived from tamarind xyloglucan as described [44 (link)] and purified by HPLC using Tosoh TSK Gel Amide column (21.5 × 300 mm) eluted with 65% aqueous acetonitrile. Cellotetraose GGGG was prepared by acetolysis of cellulose [45 ] and separated from the mixture of deacetylated oligosaccharides by HPLC as above. The sample of pea xyloglucan was a gift from Marie-Christine Ralet (INRA, Nantes, France). ELISAs were carried out as described previously [6 (link)] and in all cases immobilised antigens were coated at 50 μg/ml. Mannan, tamarind xyloglucan polymers, isoprimeverose and xylose disaccharide were obtained from Megazyme, Bray, Ireland. The selected antibody, an IgG2c, was designated LM15.
Marcus S.E., Verhertbruggen Y., Hervé C., Ordaz-Ortiz J.J., Farkas V., Pedersen H.L., Willats W.G, & Knox J.P. (2008). Pectic homogalacturonan masks abundant sets of xyloglucan epitopes in plant cell walls. BMC Plant Biology, 8, 60.
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Publication 2008
Acetic Acid acetonitrile Amides Amination Antibodies Antigens Bath Buffers cellotetraose Cellulose Cell Wall Disaccharides Enzyme-Linked Immunosorbent Assay Freund's Adjuvant Fusions, Cell High-Performance Liquid Chromatographies Hybridomas Immunoglobulins incomplete Freund's adjuvant Injections, Intraperitoneal isolation Isomerism isoprimeverose Lymphocyte Males Mannans Microarray Analysis Multiple Myeloma Oligosaccharides Polymers Polysaccharides Psychological Inhibition Rats, Wistar sodium borate sodium cyanoborohydride Spleen Tamarindus indica Vaccination xyloglucan Xylose
4
Enzymatic Cleavage Assays for LPMOs
Cited 10 times
All the cleavage assays (300 μl liquid volume) contained 4.4 μM of PaLPMO9s, 1.2 U.ml−1 of PaCDHB or 1 mM of ascorbate, and 0.1 % (w/v) PASC prepared from Avicel as described by [47 (link)] in 50 mM sodium acetate buffer pH 4.8 or 50 μM of cello-oligosaccharides (Megazyme, Wicklow, Ireland) in 10 mM sodium acetate buffer pH 4.8. The enzyme reactions were performed in 2-ml tubes and incubated in a thermomixer (Eppendorf, Montesson, France) at 50 °C and 850 rpm. After 16 h of incubation, all the samples were boiled at 100 °C for 10 min to stop the enzymatic reaction and then centrifuged at 16,000 rpm for 15 min at 4 °C to separate the soluble fraction from the remaining insoluble fraction before carbohydrate determination. For kinetic experiments, reactions were run as described above and stopped after 1, 2, 3, 5, 7, 9, 24, 30, and 48 h of incubation. Assays were performed as triplicate independent experiments. For XG, the reaction mixture (300 μl liquid volume) contained 4.4 μM of PaLPMO9H, 1 mM of ascorbate, and 0.2 % (w/v) tamarind XG (Megazyme) in 50 mM sodium acetate buffer pH 4.8. The enzyme reactions were performed in 2-ml tubes and proceed as described above. Assays were performed as triplicate independent experiments.
Bennati-Granier C., Garajova S., Champion C., Grisel S., Haon M., Zhou S., Fanuel M., Ropartz D., Rogniaux H., Gimbert I., Record E, & Berrin J.G. (2015). Substrate specificity and regioselectivity of fungal AA9 lytic polysaccharide monooxygenases secreted by Podospora anserina. Biotechnology for Biofuels, 8, 90.
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Publication 2015
Avicel Biological Assay Buffers Carbohydrates Cytokinesis Enzymes Kinetics Oligosaccharides Pancreatic Stellate Cells Sodium Acetate Tamarindus indica
5
Immunohistochemical Analysis of Intestinal Tight Junctions
Cited 9 times
At 8 days after the S. enterica and E. hirae infections, intestinal tissues were fixed in 10% (w/v) PBS-buffered formaldehyde and 7 μm sections were prepared from paraffin embedded tissues. Immunohistochemical localization was performed as previously described [42 (link)]. Sections were incubated overnight with (1) purified goat polyclonal antibody directed towards ZO-1 (Santa Cruz Biotechnology, Santa Cruz, CA, USA, 1:500 in PBS, v/v) or (2) with purified hamster anti-Occludin (Santa Cruz Biotechnology, 1:500 in PBS, w/v). Sections were washed with PBS and incubated with secondary antibody. A biotin-conjugated goat anti-rabbit IgG and avidin–biotin peroxidase complex (Vector Laboratories, Burlingame, CA, USA) detected the specific labeling. The software Optilab Graftek (Graftek, Mirmande, France) assessed densitometry of immunohistochemistry photographs.
Esposito E., Campolo M., Casili G., Lanza M., Franco D., Filippone A., Peritore A.F, & Cuzzocrea S. (2018). Protective Effects of Xyloglucan in Association with the Polysaccharide Gelose in an Experimental Model of Gastroenteritis and Urinary Tract Infections. International Journal of Molecular Sciences, 19(7), 1844.
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Publication 2018
anti-IgG Avidin Biotin Cloning Vectors Densitometry Formaldehyde Goat Hamsters Immunoglobulins Immunohistochemistry Infection Intestines Occludin Paraffin Embedding Peroxidase Rabbits Tissues

Most recents protocols related to «Xyloglucan»

1
Enzymatic Modification of Xanthan Gum
The enzymatic modification of XG was achieved by following the protocol of Brun-Graeppi et al. using β-Galactosidase from Aspergillus oryzae which was purchased from Sigma-Aldrich (Saint Louis, MI, USA) [30 (link)]. Enzymatic modifications were achieved on XG/CNC complexes at 50 °C with an enzyme/substrate ratio of 0.37 U/mg XG. The mixtures were stirred and left to react for 22 h. The mixtures were heated at 90 °C for 5 min to deactivate the enzyme. The mixtures were then cooled and kept at 4 °C.
Rangel G., Moreau C., Villares A., Chassenieux C, & Cathala B. (2024). Xyloglucan–Cellulose Nanocrystals Mixtures: A Case Study of Nanocolloidal Hydrogels and Levers for Tuning Functional Properties. Gels, 10(5), 334.
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Publication 2024
2
Oxidative Activities of TrAA14A on Cellulosic Substrates
The oxidative activities of TrAA14A on various cellulosic substrates including RAC-85, Avicel, mercerized fiber and α-cellulose, or xyloglucan were determined in the reaction mixture (2.0 mL) containing various substrates (5 mg), 1 μM TrAA14A and 1 mM AscA in sodium acetate buffer (pH 5.0, 50 mM) in an incubator at 45 ℃ and 200 rpm for 24 h. The control reaction containing various substrates (5 mg) with AscA (1 mM), or AscA (1 mM) and Cu2+ (1 μM), or inactivated TrAA14A (1 μM, boiled at 99 °C for 15 min) only was also performed in parallel under the same condition. To compare the cellulose-oxidizing activity of TrAA14A with AA9 LPMOs, the oxidative activities on different cellulosic substrates of two previously characterized NcLPMO9C and EpLPMO9A were also determined under the same conditions. After the reaction, all samples were boiled at 99 ℃ for 10 min and centrifuged at 10,000 rpm for 10 min. The nonoxidized and oxidized products in the supernatant were then assayed by HPAEC-PAD [48 (link)]. Briefly, HPAEC analysis was performed on a Dionex ICS-6000 system (Dionex, Sunnyvale, CA, USA) equipped with pulsed amperometric detection (PAD) and a CarboPac PA200 analytical column (3 × 250 mm) with a CarboPac PA200 guard column (3 × 50 mm). Products were separated using 0.1 M NaOH in the mobile phase with the concentration of sodium acetate increasing from 0 to 140 mM (14 min), 140 to 300 mM (8 min), 300 to 400 mM (4 min), and then held constant at 500 mM (3 min) before re-equilibration in 0.1 M NaOH (4 min). The flow rate was set to 0.4 mL/min, the column was maintained at a temperature of 30 °C. The oxidation regioselectivity of TrAA14A was determined by analyzing the products generated from RAC-85 using MALDI-TOF MS as described before [45 (link)]. In all analyses, 2,5-dihydroxybenzoic acid (DHB) in acetonitrile 30% (v/v) was used as the matrix. The synergism of TrAA14A with GHs was performed in a reaction mixture (1 mL) by mixed incubation of TrAA14A (1 μM) with EGI (10 μg), CBHI (20 μg), CBHII (20 μg), or Celluclast®1.5L (0.04 U), and 4 mg/mL RAC-85 or mercerized fiber, with 1 mM AscA in sodium acetate buffer (pH 5.0, 50 mM) at 45 ℃ and 1000 rpm for 1 h in a thermomixer. The control reaction in a reaction mixture (1 mL) containing individual TrAA14A (1 μM), EGI (10 μg), CBHI (20 μg), CBHII (20 μg), or Celluclast®1.5L (0.04 U), and 4 mg/mL RAC-85 or mercerized fiber, with 1 mM AscA was performed under same condition. The reaction was stopped by boiling at 99 ℃ for 10 min and centrifuging at 10,000 rpm for 10 min. The reducing sugar in the supernatant was then assayed by DNS. The degree of synergy (DS) of the coupled enzyme mixtures was calculated by Eq. (1): DS=RS(GH+TrAA14A)/RSGH+RSTrAA14A where RS(GH+ TrAA14A) is the reducing sugar released from the enzyme mixture of GH and TrAA14A, and (RSGH + RSTrAA14A) is the sum of the reducing sugar released from the single GH enzyme and TrAA14A.
Chen K., Zhao X., Zhang P., Long L, & Ding S. (2024). A novel AA14 LPMO from Talaromyces rugulosus with bifunctional cellulolytic/hemicellulolytic activity boosted cellulose hydrolysis. Biotechnology for Biofuels and Bioproducts, 17, 30.
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Publication 2024
3
Quantification of Xyloglucan Hydrolysis
Not available on PMC !
To determine any catalytic effect due to truncation of the full-length enzyme [51] (link), the specific activities of BoGH5A and BoGH5A (cat) endo-xyloglucanases were quantified using a bicinchoninic acid (BCA) reducing sugar assay [67] . Each enzyme was used at 0.5 µg/mL. The reactions were conducted in quadruplet in a final volume of 100 µl in 50 mM sodium phosphate buffer (pH 6.0) at 21 ºC for 10 min with 1 mg/mL tamarind xyloglucan (Megazyme, Lot#100403). Reactions were terminated with the addition of an equal volume of BCA working reagent. Color was developed at 80 ºC for 20 min, and the absorbance was read at 563 nm. A series of glucose concentrations (5 to 100 µM) was included in the assay to quantify the amount of reducing ends released. Blank reactions containing only substrate in assay buffer were used to measure the background absorbance generated by reducing ends present on the undigested tamarind xyloglucan. The enzyme concentration used in this assay was not high enough to contribute significantly to the absorbance at 563 nm.
Rodd A.M., Mawhinney W.M, & Brumer H. (2024). A scalable, chromatography-free, biocatalytic method to produce the xyloglucan heptasaccharide XXXG. Biotechnology for biofuels and bioproducts, 17(1).
Publication 2024
4
Gamma Radiation-Induced Grafting of HEAA onto Xyloglucan
HEAA was grafted onto xyloglucan Xy by gamma radiation-induced graft polymerization using 400 mg of Xy, 2.5 ml of ethanol, and 500 microliters of monomer. Doses from 5 to 25 kGy in increments of 5 kGy (D1, D2, D3, D4, and D5) were used. A Transelektro-LGI-01 60Co-gamma-ray source was used to irradiate the substances in Pyrex tubes (1.52 kGy/h). An Amber 3042 dosimeter (Perspex Harwell) was used to measure the doses accurately. For easy classification of the grafted Xy, the resulting copolymers were denoted according to the dose, namely, XyM2D1, XyM2D2, XyM2D3, XyM2D4, and XyM2D5, where M2 represents HEAA. Soxhlet extraction with acetone (250 ml) was used to purify the Xy-g-PHEAA from HEAA and PHEAA residues for approximately 72 h.
González-Torres M., Martínez-Mata R., Ruvalcaba-Paredes E.K., del Real A., Leyva-Gómez G, & Maciel-Cerda A. (2024). Preparation of xyloglucan-grafted poly(N-hydroxyethyl acrylamide) copolymer by free-radical polymerization for in vitro evaluation of human dermal fibroblasts. Journal of Materials Science. Materials in Medicine, 35(1), 20.
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Publication 2024
5
Optimized Enzymatic Assay for LPMO Turnover
The assay conditions to measure
turnover numbers (TN) were optimized in a series of preliminary experiments.
We used the following standard assay conditions unless otherwise noted:
the optimized assays were performed by operating the amperometric
H2O2 sensor at an applied potential of 100 mV
vs SHE and an angular velocity of the RDE of 50 s–1. Every second, 12.5 data points were collected. The H2O2 sensor was operated in 4 mL of 30 mM sodium acetate
buffer, pH 6.0, containing 100 mM KCl for improved conductivity in
the temperature-controlled (30 °C) electrochemical cell. Substrate
concentrations were 4 g L–1 for hemicelluloses,
cellopentaose, or PASC and 100 g L–1 for CNC and
MCC, and the initial concentration of H2O2 was
100 μM. LPMO concentrations varied according to the studied
substrate and therefore will be indicated in figures and table legends.
Typically, the following concentrations were used: 50 nM LPMO for
hemicellulosic substrates, 100 nM LPMO for cellopentaose and PASC,
and 200 nM LPMO for PASC, CNC, and MCC.
Reaction rates also
depended on the concentration of the reductant, and thus it was important
to determine saturating reductant concentrations. We, therefore, determined
the amount of ascorbate required to achieve saturation for all studied
LPMOs at pH 6.0 (Table S4). Figure S5 shows that saturation is achieved for
all LPMOs acting on xyloglucan or PASC with 500 μM ascorbate
but not for NcAA9F and HjAA9B acting
on PASC and xyloglucan, respectively. For these two LPMOs, 2 mM ascorbate
was used to achieve full saturation. Any deviation from these conditions
is indicated in the figure and table legends. A control experiment
with saturating amounts of cellobiose dehydrogenase from N. crassa (NcCDHIIA) (Figure S6) to reduce NcAA9C
acting on 4 g L–1 of xyloglucan showed that the
measured maximum catalytic rate of 31.9 ± 0.5 s–1 equals the rate obtained when using ascorbate as a reductant (31.6
± 1.5 s–1; averaged over 3 different experiments
using 50–200 nM NcAA9C) (Table S3). This supports the notion that the experimentally
obtained reaction rates are independent of the reductant.
To
study the effect of different substrates, the cosubstrate H2O2, and the reductant ascorbate on catalysis, their
concentrations were varied. The final substrate concentrations in
experiments shown in Figure 2 were 0.125–8 g L–1 (DP5, hemicelluloses,
PASC) and 10–100 g L–1 (CNC). The ascorbate
concentration was varied between 0.005 and 12 mM to determine the
pH-dependent concentration needed to achieve full saturation at pH
4.0–7.0 (Figure 4). To study the influence of pH (5.0–8.0) on catalysis by NcAA9C at varying xyloglucan and H2O2 concentrations, shown in Figure 4, the ascorbate concentration was 3 mM, which is at
least 10 times higher than the highest half-saturating concentration
of ascorbate in the pH 5.0–8.0 range (at pH 5.0; Table S10). The H2O2 concentration
was varied between 25 and 300 μM, while the xyloglucan concentration
was kept constant at 4 g L–1. All measurements were
performed in independent triplicate. The displayed H2O2 time traces were averaged over three independent measurements.
Schwaiger L., Csarman F., Chang H., Golten O., Eijsink V.G, & Ludwig R. (2024). Electrochemical Monitoring of Heterogeneous Peroxygenase Reactions Unravels LPMO Kinetics. ACS Catalysis, 14(2), 1205-1219.
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Publication 2024

Top products related to «Xyloglucan»

1
Tamarind xyloglucan by Megazyme
Sourced in Ireland
Tamarind xyloglucan is a polysaccharide derived from the seeds of the tamarind tree. It is a complex carbohydrate composed of a backbone of glucose units with xylose side chains. Tamarind xyloglucan is commonly used in various laboratory applications due to its unique physical and chemical properties.
2
Xyloglucan by Megazyme
Sourced in Ireland
Xyloglucan is a plant cell wall polysaccharide component that can be extracted and purified for research purposes. It is a complex hetero-polysaccharide composed of a glucose backbone with xylose, galactose, and fucose side chains. Xyloglucan plays a structural role in plant cell walls and is of interest in various research fields.
3
Wheat arabinoxylan by Megazyme
Sourced in Ireland
Wheat arabinoxylan is a polysaccharide extracted from the cell walls of wheat. It is a complex heteropolysaccharide composed of a backbone of xylose units with arabinosyl side chains. This product is suitable for use in research applications involving the study of plant cell wall components.
4
Lichenan by Megazyme
Sourced in Ireland
Lichenan is a laboratory equipment product offered by Megazyme. It is a polysaccharide derived from the lichen Cetraria islandica, commonly known as Iceland moss. Lichenan is used as a substrate in enzymatic assays and other analytical techniques.
5
Avicel ph 101 by Merck Group
Sourced in United States, Germany, China, France, United Kingdom, Sao Tome and Principe, Norway, Macao, Japan
Avicel PH-101 is a microcrystalline cellulose product manufactured by Merck Group. It is a white, odorless, and tasteless powder that is used as an excipient in the pharmaceutical and dietary supplement industries.
6
β glucan by Megazyme
Sourced in Ireland
β-glucan is a lab equipment product used to measure the β-glucan content in various samples. It provides an accurate and reliable method for quantifying the levels of this important polysaccharide.
7
Konjac glucomannan by Megazyme
Sourced in Ireland
Konjac glucomannan is a water-soluble dietary fiber derived from the roots of the konjac plant. It is a neutral polysaccharide composed of glucose and mannose units. Konjac glucomannan is commonly used as a thickening and gelling agent in food and pharmaceutical applications.
8
Glucomannan by Megazyme
Sourced in Ireland
Glucomannan is a polysaccharide that can be extracted from the roots of the konjac plant. It is a high molecular weight, water-soluble dietary fiber with a chemical structure consisting of D-mannose and D-glucose units. Glucomannan is commonly used as a thickening, gelling, and stabilizing agent in various food and industrial applications.
9
Barley β glucan by Megazyme
Sourced in Ireland, United States, Germany
Barley β-glucan is a type of lab equipment used for the analysis of β-glucan content in barley and other cereal samples. It provides a reliable and accurate method for quantifying the amount of β-glucan present in these materials.
10
Curdlan by Megazyme
Sourced in Ireland
Curdlan is a polysaccharide produced by the bacterium Agrobacterium bacteria. It is a neutral, water-insoluble, and linear β-(1→3)-glucan. Curdlan has the ability to form thermally-reversible gels, which is its core function.

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