BETA-GLUCURONIDASE FROM LIMPETS (C005B-307015)

Application

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

Features and Benefits

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.

Unit Definition

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).

Physical form

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.