Most information on this enzyme is proprietary. However, it is an endo-type enzyme sourced from Flavobacterium species and functions as an endo-cleaving enzyme.
A1603
Alginate Lyase
powder, ≥10,000 units/g solid
Synonym(s):
poly-beta-D-mannuronate lyase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Pricing and availability is not currently available.
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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.[1]
Application
Alginate Lyase has been used:
- in the pre-processing of enzyme[2]
- to de-encapsulate cells[3]
- to digest Pseudomonas exopolysaccharide to facilitate electroporation[4]
Alginate Lyase is used to break down alginate or alginic acid and to reduce viscosity. It is useful during follicle isolation, encapsulation, and culture [5].
Biochem/physiol Actions
Alginate lyases actively participates in the saccharification of the acidic polysaccharides for the production of bioethanol.[1]
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Customers Also Viewed
Elizabeth M Parrish et al.
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.
Lena C E Lundqvist et al.
Carbohydrate research, 352, 44-50 (2012-03-21)
The gene coding for an alginate lyase from the marine bacteria Pseudomonas alginovora X017 was cloned and heterologously expressed in Escherichia coli strains. The protein was produced in inclusion bodies and the active form was obtained by applying a refolding
Yuya Morimoto et al.
APL bioengineering, 4(2), 026101-026101 (2020-04-09)
Biohybrid robots composed of biological and synthetic components have been introduced to reconstruct biological functions in mechanical systems and obtain better understanding of biological designs. For example, biohybrid robots powered by skeletal muscle tissue have already succeeded in performing various
Adam J Wargacki et al.
Science (New York, N.Y.), 335(6066), 308-313 (2012-01-24)
Prospecting macroalgae (seaweeds) as feedstocks for bioconversion into biofuels and commodity chemical compounds is limited primarily by the availability of tractable microorganisms that can metabolize alginate polysaccharides. Here, we present the discovery of a 36-kilo-base pair DNA fragment from Vibrio
Bacteriophages phi MR299-2 and phi NH-4 Can Eliminate Pseudomonas aeruginosa in the Murine Lung and on Cystic Fibrosis Lung Airway Cells
Alemayehu D, et al.
mBio, 3(2) (2012)
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Hi! What is the PL family, source and structure of this enzyme?
1 answer-
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What are the aminoacid sequence of the enzyme, molecular weight, molar extinction and the original bacterium
1 answer-
The amino acid sequence and molar extinction of this enzyme has not been determined. The molecular weight is approximately 40,000 daltons. The specific species of the bacterium is considered proprietary.
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Hi, could you please tell me the source of the alginate lyase and the strain in which it was expressed? Thank you!
1 answer-
This enzyme is produced by microbial fermentation. The specific species is considered proprietary.
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I was wondering how to prepare the enzyme solution and what does the 1 un/ml mean? Is is 1 unit/mL or what does the un stand for? How do I convert the units to grams?
1 answer-
A1603 should be resuspended at a concentration of 0.05 - 1.5 u/ml in 0.1 mol/L Phosphate buffer (pH 6.3).
The specific activity of each lot (units/gram solid) is provided on the certificate of analysis. The lot specific certificate of analysis can be found here:
https://www.sigmaaldrich.com/product/sigma/a1603#product-documentation
Based on the specific activity (units/gram solid), the researcher can weigh out the appropriate amount of A1603 to achieve a 1 unit/mL solution.
un = unitHelpful?
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Hi, I've ordered this product from here, but it's just saying powder, ≥10,000 units/g solid, can you please tell me the molecular weight of it? in Da or kDa?
1 answer-
The molecular weight this material is approximately 40,000 daltons.
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Do you have any information about solubility, for example in PBS pH 7.2? It would be helpful to know if activity is retained after a single freeze-thaw cycle, so that we could store concentrated aliquots at -20 C.
1 answer-
A pH of 7.2 will cause a decline in activity. Solutions of 0.05 - 1.5 u/ml prepared in 0.1 M Phosphate buffer at pH 6.3 are recommended to maintain optimum activity.
The general recommendations in the literature are as follows:
For long-term storage, store at -20°C or -80°C. Store working aliquots at 4°C for up to one week. Avoid repeated freeze/thaw cycles.
Note that the stability information above has not been validated .Helpful?
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I ordered the alginate lyase from your company. But the information that I received only present >=10,000U/g. And I need the 20U/m in my experiment. Could you give me more information?
1 answer-
The exact specific activity value is specified on the lot specific Certificate of Analysis. Please see this example Certificate of Analysis: https://www.sigmaaldrich.com/certificates/sapfs/PROD/sap/certificate_pdfs/COFA/Q14/A1603-BULKSLCQ2940.pdf.
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