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D9909

Dextran Sucrase from Leuconostoc mesenteroides

lyophilized powder, ≥100 units/mg protein

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10 units

Fecha estimada de envío06 de agosto de 2026desdeMILWAUKEE

$488.00

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Número CAS:
Número CE:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥100 units/mg protein
Biological source:
bacterial (Leuconostoc mesenteroides)

$488.00


Fecha estimada de envío06 de agosto de 2026Detalles


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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 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.
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

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.[1] 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.[2] 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.[3]

Physical form

Lyophilized powder containing dextran, MES buffer salts and CaCl2

Analysis Note

Chromatographically purified

Other Notes

One unit will liberate 1.0 μmole of fructose per min at 37 °C, pH 5.4.

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Este artículo
D4876D1662D3759
biological source

bacterial (Leuconostoc mesenteroides)

biological source

bacterial (Leuconostoc mesenteroides)

biological source

bacterial (Leuconostoc mesenteroides)

biological source

bacterial (Leuconostoc mesenteroides)

specific activity

≥100 units/mg protein

specific activity

-

specific activity

-

specific activity

-

form

lyophilized powder

form

powder

form

powder

form

powder

solubility

H2O: soluble 0.9-1.1 mg/mL, clear to slightly hazy, colorless to light yellow

solubility

H2O: soluble 20 mg/mL

solubility

H2O: 100 mg/mL, clear, colorless

solubility

H2O: 50 mg/mL, clear to very slightly hazy, colorless to faintly yellow

storage temp.

−20°C

storage temp.

-

storage temp.

-

storage temp.

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200


Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Pore control with dextran generated from immobilized dextransucrase
Kawakita H, et al.
Biochemical Engineering Journal, 36(2), 190-193 (2007)
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)



Número de artículo de comercio global

SKUGTIN
D9909-10UN04061833591352

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