S1629
Sulfatase from Aerobacter aerogenes
Type VI, buffered aqueous glycerol solution, 2-5 units/mg protein (biuret), 10-20 units/mL
Synonym(s):
Aryl-sulfatase, Aryl-sulfate sulfohydrolase, Phenolsulfatase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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type
Type VI
Quality Level
form
buffered aqueous glycerol solution
specific activity
2-5 units/mg protein (biuret)
mol wt
~41 kDa
concentration
10-20 units/mL
foreign activity
β-Glucuronidase ≤10 U/mL
shipped in
wet ice
storage temp.
−20°C
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General description
Sulfatases comprise Cys/Ser-X-Pro-X-Arg motif that is conserved in their active sites.
Application
Sulfatase from Aerobacter aerogenes has been used:
- as a deconjugation enzyme for treating plasma samples for quercetin quantification using liquid chromatography with tandem mass spectrometry (LC/MS/MS) analyses
- in fluorescence intensity-based enzymatic assay with an activity-based probe probe 1
- to treat sulfatide liposomes to remove the 3-O-sulfogalactosyde head from sulfatides
Biochem/physiol Actions
Sulfatases hydrolyze sulfate ester bonds to generate inorganic sulfates. Microbial sulfatases participate in sulfur scavenging and are essential enzymes for the utilization of sulfur. They may be associated with pathogenesis. Commercially available sulfatase from Aerobacter aerogenes is useful as a deconjugation enzyme for the removal of glucuronate and sulfate moieties from conjugates. Sulfatases find application in industry and agriculture.
Unit Definition
One unit will hydrolyze 1.0 μmole of p-nitrophenyl sulfate per min at pH 7.1 at 37 °C.
Physical form
Solution in 50% glycerol containing 0.01 M Tris, pH 7.5.
substrate
Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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β-Glucuronidase and sulfatase are the major deconjugating enzymes used in the cleavage of the glucuronate and sulfate moieties, respectively, from certain conjugated food factors including polyphenols. In the present study, we found that compounds having the same molecular weights as
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Arylsulfatase activity was detected in a bacterial strain, Citrobacter braakii 69-b, isolated from soil by enrichment cultivation using porcine gastric mucin. The production of arylsulfatase was derepressed markedly in a synthetic medium by the addition of tyramine. The purified enzyme
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