D9909
Dextran Sucrase from Leuconostoc mesenteroides
lyophilized powder, ≥100 units/mg protein
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10 UNITS
€526.00
€526.00
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10 UNITS
€526.00
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
€526.00
Please contact Customer Service for Availability
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 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
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Ah-Rum Yi et al.
Journal of microbiology and biotechnology, 19(8), 829-835 (2009-09-08)
A dextransucrase (LcDS) gene from Leuconostoc citreum HJ-P4 has been amplified and cloned in E. coli. The LcDS gene consists of 4,431 nucleotides encoding 1,477 amino acid residues sharing 63-98% of amino acid sequence identities with other known dextransucrases from
Enzymatically synthesized dextran nanoparticles and their use as carriers for nutraceuticals
Semyonov D, et al.
Food & Function, 5(10), 2463-2474 (2014)
Marie-Sophie Bounaix et al.
FEMS microbiology letters, 311(1), 18-26 (2010-08-21)
The study of exopolysaccharide production by heterofermentative sourdough lactic acid bacteria has shown that Weissella strains isolated from sourdoughs produce linear dextrans containing α-(1→6) glucose residues with few α-(1→3) linkages from sucrose. In this study, several dextran-producing strains, Weissella cibaria
Bioengineering of Leuconostoc mesenteroides glucansucrases that gives selected bond formation for glucan synthesis and/or acceptor-product synt
Kang, H., et al.
RNA, 59, 4148-4155 (2011)
Hongbin Zhang et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 25(12), 2022-2028 (2010-04-01)
We optimized the medium for recombinant dextransucrase expression in engineering strain Escherichia coli BL21 (DE3)/pET28-dexYG by an Orthogonal experiment. After the medium had been decided, we studied the effect of temperature, sucrose concentration and pH value on the yield. The
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