71238
Alginic acid sodium salt from brown algae
BioReagent, suitable for immobilization of micro-organisms
Synonym(s):
Algin, Sodium alginate
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About This Item
biological source
algae (brown)
Quality Level
product line
BioReagent
form
powder
ign. residue
≤30%
loss
≤15% loss on drying
color
white to light beige
pH
6.0-8.0 (10 mg/mL in H2O)
suitability
in accordance for gelation test, suitable for immobilization of micro-organisms
storage temp.
room temp
SMILES string
[Na+].[O-]C(=O)C1O[C@H]([C@H]([C@H]([C@@H]1O)O)O)O
InChI
1S/C6H10O7.Na/c7-1-2(8)4(5(10)11)13-6(12)3(1)9;/h1-4,6-9,12H,(H,10,11);/q;+1/p-1/t1-,2-,3-,4?,6+;/m0./s1
InChI key
MSXHSNHNTORCAW-MPGIDXPLSA-M
Application
Alginate, a colloidal polyuronic acid structural molecule capable of gelation, is used in the preparation of colloidal biodegradable structures such as gels, biofilms, beads, nanoparticles, and microcapsules suitable for applications that range from gel based separation technologies to drug delivery and cell preservation.
Other Notes
A straight-chain, hydrophilic, colloidal, polyuronic acid composed of guluronic and mannuronic acid residues.
To gain a comprehensive understanding of our extensive range of Polysaccharides for your research, we encourage you to visit our Carbohydrates Category page.
Immobilization of cells; or enzymes; the alginate matrix can be liquefied by the addition of a chelating agent, making possible the recovery of developing colonies without affecting their continued growth.
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Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Related Content
O Smidsrød et al.
Trends in biotechnology, 8(3), 71-78 (1990-03-01)
In recent years, entrapment of cells within spheres of Ca2+ alginate has become the most widely used technique for immobilizing living cells. This versatile method includes applications ranging from immobilization of living or dead cells in bioreactors, immobilization of plant
W.H. Scouten
Solid Phase Biochemistry, 449-449 (1983)
C. Bucke
Methods in Enzymology, 135, 175-175 (1987)