Dionex carbopac pa200 column

Manufactured by Thermo Fisher Scientific

Sourced in United States

The Dionex Carbopac PA200 column is a high-performance anion-exchange chromatography column designed for the separation and analysis of carbohydrates and related compounds. The column features a polymeric resin substrate with a high-capacity anion-exchange functionality, enabling effective separation and detection of a wide range of carbohydrates.

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Lab products found in correlation

Ics 5000 hplc system, by Thermo Fisher Scientific (2 mentions) Dionex ics 5000, by Thermo Fisher Scientific (2 mentions) Thermomixer, by Eppendorf (2 mentions) Autoflex system, by Bruker (1 mentions)

Spelling variants of this product

CarboPac PA200 column (46 citations) CarboPac PA200 (22 citations) Dionex CarboPac PA200 (8 citations)

4 protocols using dionex carbopac pa200 column

Carbohydrate Analysis by HPAEC-PAD

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HPAEC-PAD carbohydrate analysis was performed on a Dionex ICS-5000 HPLC
system operated by Chromeleon software version 7 (Dionex Corp., Sunnyvale, CA,
USA). The injection volume was 10 μM and a Dionex Carbopac PA200 column
(Thermo Scientific) with a guard column was used for all the samples
separations. Solvent A was ultrapure water, solvent B was 1 M sodium hydroxide,
and solvent C was 1 M sodium acetate prepared from anhydrous Bio Ultra-grade
solid (Sigma). The following gradient was used: 0 – 5 min, 10 % B and 3.5
% solvent C; 5 – 12 min, 10% B and a linear gradient from 3.5–30%
C; 12 –12.1 min, 50 % B, 50 % C; 12.1 – 13 min, exponential
gradient (curve setting 9) of B and C back to initial conditions; 13 – 17
min, initial conditions ^{34 (link)}.
To determine the mode of action of the enzyme, 3 μM of the
recombinant enzyme was incubated with 0.25 mg.mL⁻¹polysaccharide at 37 °C in a 0.5 mL reaction mixture containing 50 mM
HEPES-NaOH buffer (pH 7.0) with 1 mM CaCl₂. The reaction was stopped
at different time points by adding 100 μL of 95 °C water and
heating to 95 °C for 10 min to a 100 μL aliquot of the reaction
mixture. The reaction mixture was then diluted two times prior to product
analysis by HPAEC-PAD.

Foley M.H., Déjean G., Hemsworth G.R., Davies G.J., Brumer H, & Koropatkin N.M. (2019). A cell-surface GH9 endo-glucanase coordinates with surface glycan binding proteins to mediate xyloglucan uptake in the gut symbiont Bacteroides ovatus. Journal of molecular biology, 431(5), 981-995.

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Structural Analysis of Mixed-Linkage Glucans

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High performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) was performed using a Dionex ICS-5000 HPLC system equipped with an AS-AP autosampler in a sequential injection configuration using the Chromeleon software version 7. 10 μl of the samples were injected on a 3 × 250 mm Dionex Carbopac PA200 column (Thermo Scientific, Waltham, United States). 56 μM of the β-1,3/1,4-MLG tetrasaccharide or 45 μM of the β-1,3/1,4-MLG trisaccharide were loaded onto the column. The gradient was used as follows: 0–5 min, 10% B, 3.5% C (initial conditions); 5–12 min 10% B, linear gradient from 0–30% C; 12.0–12.1 min, 50% B, 50% C; 12.1–13.0 min, exponential gradient of B and C, back to initial conditions, 13–17 min initial conditions. Solvent A was ultrapure water, solvent B was 1 M sodium hydroxide and solvent C was 1 M sodium acetate.
Matrix Assisted Laser Desorption Ionization–Time of Flight (MALDI-TOF) analysis of mixed-linkage glucans was performed with a Bruker Autoflex system (Bruker Daltonics) operated in reflectron mode. 10 mg/ml of the oligosaccharide were mixed 1:5 with 2,5-dihiydroxybenzoic acid in 1:1 H₂O:MeOH on a Bruker MTP 384 grounded steel MALDI plate. The samples were allowed to dry and directly analyzed.

Barghahn S., Arnal G., Jain N., Petutschnig E., Brumer H, & Lipka V. (2021). Mixed Linkage β-1,3/1,4-Glucan Oligosaccharides Induce Defense Responses in Hordeum vulgare and Arabidopsis thaliana. Frontiers in Plant Science, 12, 682439.

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Synergistic Corn Cob Xylanase Assay

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The ability of the D. mossii enzymes to boost the activity of the commercially available endo-1,4-β-xylanase Xyn11A (CAS 9025-57-4; Megazyme) was determined on 5% w/v ball milled and freeze-dried corn cob biomass. The reactions were incubated at 1000 rpm and 37 °C in a thermomixer (Eppendorf). The amount of reducing sugars was determined using 3,5-dinitrosalicylic acid (DNSA; (65 )) as described in Kmezik et al. (32 (link)). Xylose was used as standard to translate absorbance values at 575 nm into reducing sugar equivalent concentrations. The xylooligosaccharide product profiles were determined by measuring X₁, X₂, X₃, X₄, X₅, and X₆ concentrations using HPAEC-PAD (high-performance anion-exchange chromatography with pulsed amperometric detection) on a Dionex ICS-5000+ (Thermo Fisher Scientific) equipped with a Dionex CarboPac PA200 column (Thermo Fisher Scientific) (66 (link)).

Kmezik C., Mazurkewich S., Meents T., McKee L.S., Idström A., Armeni M., Savolainen O., Brändén G, & Larsbrink J. (2021). A polysaccharide utilization locus from the gut bacterium Dysgonomonas mossii encodes functionally distinct carbohydrate esterases. The Journal of Biological Chemistry, 296, 100500.

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Enzymatic Hydrolysis of Lignocellulosic Biomass

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Boosting studies were performed with the commercially available endo-1,4-β-xylanase Xyn11A (CAS 9025-57-4; Megazyme), using 5% w/v corn cob or Japanese beechwood (ball milled and freeze-dried) as substrate. Reactions were incubated in a thermomixer (Eppendorf) at 1000 rpm and 37 °C for the B. ovatus enzymes and at 25 °C for the F. johnsoniae enzymes. Time point samples were immediately frozen in liquid nitrogen and kept at − 20 °C until analysis. Prior to analysis the samples were thawed on ice, clarified by centrifugation (4 °C, 2 min, 14,000 rpm), and 15 µL of sample supernatant was mixed with 100 µL of 3,5-dinitrosalicylic acid (DNSA; [44 (link)]) reagent and 85 µL of Milli-Q-water, and the reactions incubated at 80 °C for 20 min. The concentration of reducing sugar equivalents was determined by monitoring the absorbance at 575 nm and comparing the results to a xylose standard curve and control (blank) samples without any added enzymes. X₁–X₄ concentrations were determined using HPAEC-PAD (high-performance anion-exchange chromatography with pulsed amperometric detection) on a Dionex ICS-5000+ (Thermo Fisher Scientific) equipped with a Dionex CarboPac™ PA200 column (Thermo Fisher Scientific) [45 (link)]. Acetate release was investigated by using the RM acetic acid (RM) kit from Megazyme, according to the manufacturer’s instructions.

Kmezik C., Bonzom C., Olsson L., Mazurkewich S, & Larsbrink J. (2020). Multimodular fused acetyl–feruloyl esterases from soil and gut Bacteroidetes improve xylanase depolymerization of recalcitrant biomass. Biotechnology for Biofuels, 13, 60.

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