BGS™

The enzymatic mix found in BGS™ has been designed such that the β-glucuronidase and Arylsulfatase have overlapping optimum incubation pHs and temperatures. This allows both glucuronide and sulfate conjugates to be hydrolyzed in one efficient step.

Conjugation of xenobiotics represents an important biotransformation reaction in humans and animals. Hydrolysis of glucuronide and sulfate conjugates is especially important in steroid analysis, since many steroids are converted into glucuronidated conjugates, or into the sulfo conjugation via the steroid elimination pathway. Being a high-purity recombinant product, BGS™ avoids conversions and generation of “steroid-like interferences” that frequently occur when using wild-type derived enzymes.

Compared to wild-type species, the stability of the aryl-sulfatase found in BGS™ is substantially improved. This makes it possible to control the proportion of β-glucuronidase to aryl-sulfatase in a predictable, consistent manner, which is simply not feasible when using wild-type enzymes.Specifications

∙ Product form: Solution 10% (v/v) in glycerol

∙ Temperature Range: 50-55°C

∙ Optimum temperature: 52°C

∙ pH Range: 6.8-7.0

∙ Optimum pH: 6.9

∙ Storage/Stability:2-8°C for 12 months

∙ Glucuronidase activity: ≥ 200,000 U/mL

∙ Activity Unit Definition: One unit will liberate 1.0 µg of phenolphthalein from phenolphthalein glucuronide per hour at pH 7.0 and 37°C.

∙ Sulfatase activity: ≥ 250,000 U/mL

∙ Activity Unit Definition: One unit of sulfatase will hydrolyze 1.0 nmol of p-nitrocatechol sulfate per hour at pH 7.0 and 45°C.