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 Code
11 - Combustible Solids
WGK
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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Construction of an expression system for the secretory production of recombinant α-agarase in yeast.
Ji-Hwan Seok et al.
Biotechnology letters, 34(6), 1041-1049 (2012-02-09)
α-Agarase hydrolyzes the α-1,3 linkage of agarose yielding agaro-oligosaccharides. It is less well characterized than β-agarase. AgaA gene (2.3 kb ORF), encoding the α-agarase from Thalassomonas JAMB A33, was subcloned into both a constitutive and an inducible expression vector. Both
Hyeok-Jin Ko et al.
Applied and environmental microbiology, 78(9), 3051-3058 (2012-02-22)
Autotransporters have been employed as the anchoring scaffold for cell surface display by replacing their passenger domains with heterologous proteins to be displayed. We adopted an autotransporter (YfaL) of Escherichia coli for the cell surface display system. The critical regions
Michael-Paul Vockenhuber et al.
Microbiology (Reading, England), 158(Pt 2), 424-435 (2011-11-15)
Transcriptional regulation of primary and secondary metabolism is well-studied in Streptomyces coelicolor, a model organism for antibiotic production and cell differentiation. In contrast, little is known about post-transcriptional regulation and the potential functions of small non-coding RNAs (sRNAs) in this
Young Hoon Oh et al.
Journal of microbiology and biotechnology, 21(8), 818-821 (2011-08-31)
An agar-degrading bacterium was isolated from the guts of spiny turban shells. It was identified as a Pseudoalteromonas species and named Pseudoalteromonas sp. JYBCL 1. The viscosity of the inoculated agar medium decreased by more than 60% after 20 h
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
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