β-Glucuronidase from limpets (Patella vulgata)

New Technical Article Comparing Performance of Different Enzymes
Learn more about recent application data generated by Sigma R&D to optimize hydrolysis for different drug classes using enzymes from different sources and the use of a chromatographicaly purified enzyme to reduce the effect of esterase activity resulting in conversion of 6-MAM to Morphine

More on the suitability of this product for hydrolysis of different drug-glucuronide substrates is available at this page.

Poster presentation comparing the hydrolysis efficiency of novel beta-glucuronidase enzymes from recombinant limpet and recombinant E. coli sources, click at the following poster link: Hydrolysis Efficiency Evaluation of Novel Recombinant Limpet and E. coli Beta-Glucuronidase Enzymes

The enzyme from patella vulgata is reported to be more effective in hydrolyzing opioid-glucuronides than the Helix pomatia, bovine liver and E. coli enzymes

Recombinantly expressed and purified to eliminate MAM esterase activity (6-Monoacetylmorphine→morphine). Representative analysis at high enzyme titer (50 un/μL β-glucuronidase) was less than 1% conversion of 6-MAM to morphine after 4 hours at 60 °C.

Supplied as a solution in 100mM potassium acetate pH 5.2. It is free of detergents, carbohydrates or any other components that may interfere with sample preparation and analysis.

One Sigma or modified Fishman unit will liberate 1.0 μg of phenolphthalein from phenolphthalein glucuronide per hr at 37 °C at pH 3.8 (30 min assay).