A6306
Agarase from Pseudomonas atlantica
lyophilized powder, ≥5,000 units/mg protein (Lowry)
Synonym(s):
β-Agarase, Agarose 4-glycanohydrolase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
42040102
NACRES:
NA.26
Recommended Products
biological source
bacterial (Pseudomonas atlantica)
Quality Level
form
lyophilized powder
specific activity
≥5,000 units/mg protein (Lowry)
storage temp.
2-8°C
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Unit Definition
One unit will produce 1.0 μg of reducing sugar (measured as D-galactose) from agar per min at pH 6.0 at 40 °C.
Physical form
Product is formulated with phosphate buffered salts, bovine serum albumin and Agarase. Total protein content ranges between 10 – 30% w/w.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Uyangaa Temuujin et al.
Applied microbiology and biotechnology, 92(4), 749-759 (2011-06-10)
The DagA product of Streptomyces coelicolor is an agarase with a primary translation product (35 kDa) of 309 amino acids, including a 30-amino acid signal peptide. Although dagA expression in Streptomyces lividans under the control of its own set of
Yuji Hatada et al.
Marine biotechnology (New York, N.Y.), 13(3), 411-422 (2010-08-06)
A gene of unknown function from the genome of the agar-degrading deep-sea bacterium Microbulbifer thermotolerans JAMB-A94(T) was functionally identified as a ι-carrageenase gene. This gene, designated as cgiA, is located together with two β-agarase genes, agaA and agaO in a
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The effects of short- and long-term freezing on Porphyra umbilicalis Kutzing (Bangiales, Rhodophyta) blade viability
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Seungwoo Lee et al.
Journal of microbiology and biotechnology, 21(11), 1116-1122 (2011-12-01)
In this study, site-directed mutagenesis was performed on the β-agarase AgaA gene from Zobellia galactanivorans to improve its catalytic activity and thermostability. The activities of three mutant enzymes, S63K, C253I, and S63K-C253I, were 126% (1,757.78 U/mg), 2.4% (33.47 U/mg), and
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