A1603
Alginate Lyase
powder, ≥10,000 units/g solid
Synonym(s):
poly-beta-D-mannuronate lyase
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General description
Alginate lyases is present in several marine algae, marine mollusks and a vast range of marine and terrestrial bacteria.
Application
Alginate Lyase has been used:
- in the pre-processing of enzyme
- to de-encapsulate cells
- to digest Pseudomonas exopolysaccharide to facilitate electroporation
Alginate Lyase is used to break down alginate or alginic acid and to reduce viscosity. It is useful during follicle isolation, encapsulation, and culture .
Biochem/physiol Actions
Alginate lyases actively participates in the saccharification of the acidic polysaccharides for the production of bioethanol.
Breaks down alginate or alginic acid to smaller molecules and reduces viscosity.
Unit Definition
One unit will produce an increase the A235nm of 1.0 per minute per mL of sodium alginate solution at pH 6.3 at 37 °C
Preparation Note
Add 0.15 mI of enzyme solution (1 un/ml) to 4.5 ml of 0.1% sodium alginate (pH 6.3). Incubate at 37 °C for 30 minutes. Terminate reaction by addition of 4.65 ml of 0.1 N NaOH.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Reproduction (Cambridge, England), 142(2), 309-318 (2011-05-26)
Ovarian follicle maturation results from a complex interplay of endocrine, paracrine, and direct cell-cell interactions. This study compared the dynamic expression of key developmental genes during folliculogenesis in vivo and during in vitro culture in a 3D alginate hydrogel system.
Environmental microbiology, 14(9), 2379-2394 (2012-04-20)
Alginate constitutes a significant part of seaweed biomass and thus a crucial nutrient for numerous marine heterotrophic bacteria. However, the mechanisms for alginate assimilation remain largely unknown in marine microorganisms. We show here that the genome of the marine flavobacterium
Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications
Bioengineered, 6(3), 125-131 (2015)
Acta crystallographica. Section D, Biological crystallography, 68(Pt 9), 1207-1216 (2012-09-06)
The structures of two mutants (H192A and Y246F) of a mannuronate-specific alginate lyase, A1-III, from Sphingomonas species A1 complexed with a tetrasaccharide substrate [4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)(2)-mannuronic acid] were determined by X-ray crystallography at around 2.2 Å resolution together with the apo form
Enzyme-assisted extraction of fucoxanthin and lipids containing polyunsaturated fatty acids from Undaria pinnatifida using dimethyl ether and ethanol
Process Biochemistry (Oxford, United Kingdom), 48(12), 1999-2008 (2013)
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