|Related Categories||3.1.x.x Acting on esters, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Carbohydrate and PTM Analysis,|
|secondary activity||≥100,000 units/mL β-glucuronidase (at pH 5.0)|
|shipped in||wet ice|
Sequential action of sulfatase from Helix pomatia and β-O-glucosidase from Caldicellulosiruptor saccharolyticus on glucosinolates allows synthesis of thiohydroximates. 2 Sulfatase from Helix pomatia hydrolyzes β-naphthyl sulfate much faster than α-naphthyl sulfate. 3
One unit will hydrolyze 1.0 μmole of p-nitrocatechol sulfate per hour at pH 5.0 at 37 °C (30 min assay).
Sulfatase from Helix pomatia is often used to remove sulfate groups from carbohydrates. 1
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Type HP-2, aqueous solution, ≥100,000 units/mL
Type H-2, aqueous solution, ≥85,000 units/mL
Type VIII, lyophilized powder, 20-40 units/mg solid
Type VI, buffered aqueous glycerol solution, 2-5 units/mg protein (biuret), 10-20 units/mL
Type H-1, lyophilized powder, sulfatase ≥10,000 units/g solid
2. SCOPE This procedure applies to all products that have a specification for Sulfatase activity, except Sulfatase from Aerobacter aerogenes, Sigma-Aldrich Product Number S1629.
Keywords: Extinction coefficient
2. Chemoenzymatic synthesis of diverse thiohydroximates from glucosinolate-utilizing enzymes from Helix pomatia and Caldicellulosiruptor saccharolyticus Kopycki Biotechnol. Lett. 33(5), 1039-46, (2011)
Supplementation of difructose anhydride III enhanced elevation of plasma equol concentrations and lowered plasma total cholesterol in isoflavone-fed rats. Tamura, A., et al. Br. J. Pharmacol. 96, 442-9, (2006)
The pharmacokinetic behavior of the soy isoflavone metabolite S-(-)equol and its diastereoisomer R-(+)equol in healthy adults determined by using stable-isotope-labeled tracers. Kenneth DR Setchell et al Am. J. Clin. Nutr. 90, 1029-37, (2009)
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