D9909
Dextran Sucrase from Leuconostoc mesenteroides
lyophilized powder, ≥100 units/mg protein
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About This Item
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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.
Application
Dextran Sucrase from Leuconostoc mesenteroides has been used:
- in immobilization on shirasu porous membrane (SPG) for dextran production
- in the enzymatic synthesis of dextran nanoparticles at various pH range
- in the immobilization with hydroxyapatite for dextran production
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.
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. 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. 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.
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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
Biotechnology and applied biochemistry, 34(Pt 2), 93-97 (2001-10-11)
A newly isolated strain of Leuconostoc mesenteroides (PCSIR-3) produced a different dextran compared with that of L. mesenteroides NRRL B-512F. Different media compositions used for dextran production showed that media containing CaCl(2) produced dextran in higher quantities compared with other
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.
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
Surface Modification of Hydrophobic Sphere with Dextran Generated from Enzymatic Reaction for Adsorption Site.
Advanced Chemical Engineering Research, 2(1), 20-25 (2013)
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