D9909
Dextran Sucrase from Leuconostoc mesenteroides
lyophilized powder, ≥100 units/mg protein
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
bacterial (Leuconostoc mesenteroides)
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥100 units/mg protein
Composition
Protein, ~15% Lowry
Solubilité
H2O: soluble 0.9-1.1 mg/mL, clear to slightly hazy, colorless to light yellow
Température de stockage
−20°C
Description générale
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.
Actions biochimiques/physiologiques
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.
Qualité
Chromatographically purified
Définition de l'unité
One unit will liberate 1.0 μmole of fructose per min at 37 °C, pH 5.4.
Forme physique
Lyophilized powder containing dextran, MES buffer salts and CaCl2
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
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)
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
S A Ul-Qader et al.
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
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.
Pore control with dextran generated from immobilized dextransucrase
Kawakita H, et al.
Biochemical Engineering Journal, 36(2), 190-193 (2007)
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