D9909
Dextran Sucrase from Leuconostoc mesenteroides
lyophilized powder, ≥100 units/mg protein
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10 UNITS
$405.84
$405.84
List Price$456.00Save 11%Web-Only Promotion
Available to ship onApril 29, 2025Details
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10 UNITS
$405.84
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
$405.84
List Price$456.00Save 11%Web-Only Promotion
Available to ship onApril 29, 2025Details
Recommended Products
biological source
bacterial (Leuconostoc mesenteroides)
Quality Level
form
lyophilized powder
specific activity
≥100 units/mg protein
composition
Protein, ~15% Lowry
solubility
H2O: soluble 0.9-1.1 mg/mL, clear to slightly hazy, colorless to light yellow
storage temp.
−20°C
General description
Dextran Sucrase from Leuconostoc mesenteroides belongs to glycoside hydrolase family 70 (GH70). It functions through a retaining mechanism and uses two catalytic acidic residues. Dextran sucrase has a dextran binding site in the C-terminal domain.[1]
Application
Dextran Sucrase from Leuconostoc mesenteroides has been used:
- in immobilization on shirasu porous membrane (SPG) for dextran production[2]
- in the enzymatic synthesis of dextran nanoparticles at various pH range[1]
- in the immobilization with hydroxyapatite for dextran production[3]
Dextran sucrase from Leuconostoc mesenteroides has been used in a study to investigate the functional and structural characterization of α-(1→2) branching sucrase derived from DSR-E glucansucrase. Dextran sucrase from Leuconostoc mesenteroides has also been used in a study to investigate the bioengineering of Leuconostoc mesenteroides glucansucrases.
The enzyme from Sigma has been used to prepare immobilized sphere for the production of dextran from sucrose.[4]
Biochem/physiol Actions
Dextransucrases are glucansucrases that are able to produce dextran, a glucose polymer linked mainly through α1-6 bonds. However, α1-3, α1-6, α1-4 and α1-2 bonds are also found, in both the main chain and the branching linkages.[5] The peptide has approximately 1600 amino acids. The aspartic acid in position 551 is essential for catalytic activity, while glutamic acid 589 and aspartic acid 662 complement the catalytic triad.[6] The activity of dextransucrase is decreased by EDTA, and is restored by the addition of calcium ions. Zinc, cadmium, lead, mercury and copper ions are inhibitory to various degrees.[7]
Quality
Chromatographically purified
Unit Definition
One unit will liberate 1.0 μmole of fructose per min at 37 °C, pH 5.4.
Physical form
Lyophilized powder containing dextran, MES buffer salts and CaCl2
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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M Kobayashi et al.
Biochimica et biophysica acta, 614(1), 46-62 (1980-07-10)
Multiple forms of dextransucrase (sucrose:1.6-alpha-D-glucan 6-alpha-D-glucosyltransferae EC 2.4.1.5) from Leuconostoc mesenteroides NRRL B-512F strain were shown by gel filtraton and electrophoretic analyses. Two components of enzyme, having different affinities for dextran gel, were separated by a column of Sephadex G-100.
Surface Modification of Hydrophobic Sphere with Dextran Generated from Enzymatic Reaction for Adsorption Site.
Nagata, Daiki, et al.
Advanced Chemical Engineering Research, 2(1), 20-25 (2013)
Yoann Brison et al.
The Journal of biological chemistry, 287(11), 7915-7924 (2012-01-21)
ΔN(123)-glucan-binding domain-catalytic domain 2 (ΔN(123)-GBD-CD2) is a truncated form of the bifunctional glucansucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299. It was constructed by rational truncation of GBD-CD2, which harbors the second catalytic domain of DSR-E. Like GBD-CD2, this variant displays
Young-Min Kim et al.
Biotechnology letters, 31(9), 1433-1438 (2009-05-22)
Alkyl glucosides were synthesized by the reaction of Leuconostoc mesenteroides dextransucrase with sucrose and various alcohols. Alkyl alpha-D-glucosides were obtained with a yield of 30% (mol/mol) with primary alcohols, but secondary alcohols or tertiary alcohols gave yields below 5%. The
Pore control with dextran generated from immobilized dextransucrase
Kawakita H, et al.
Biochemical Engineering Journal, 36(2), 190-193 (2007)
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