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Merck
CN

D9909

Dextran Sucrase from Leuconostoc mesenteroides

lyophilized powder, ≥100 units/mg protein

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化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
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产品名称

Dextran Sucrase from Leuconostoc mesenteroides, lyophilized powder, ≥100 units/mg protein

biological source

bacterial (Leuconostoc mesenteroides)

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

Quality Level

Analysis Note

Chromatographically purified

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.

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.

Other Notes

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

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

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分析证书(COA)

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J F Robyt et al.
Carbohydrate research, 68(1), 95-111 (1979-01-01)
The production of dextransucrase from Leuconostoc mesenteroides NRRL B-512F was stimulated 2-fold by the addition of 0.005% of calcium chloride to the medium; levansucrase levels were unaffected. Dextransucrase was purified by concentration and dialysis of the culture supernatant with a
Pore control with dextran generated from immobilized dextransucrase
Kawakita H, et al.
Biochemical Engineering Journal, 36(2), 190-193 (2007)
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
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.

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