Contamination of deconjugation enzymes derived from Helix pomatia with the plant bioactive compounds 3,3′-diindolylmethane, 5-methoxypsoralen, and 8-methoxypsoralen

Bioactive compounds from plant foods are intensely investigated for effects on disease prevention. β-Glucuronidase/arylsulfatase from Helix pomatia (snail) is commonly used when quantifying exposure to metabolized dietary components. However, we describe here the contamination of multiple formulations of this enzyme preparation with 3,3′-diindolylmethane (DIM), 8-methoxypsoralen (8-MOP), and 5-methoxypsoralen (5-MOP), bioactives from cruciferous and apiaceous vegetables under investigation as putative cancer chemopreventive agents. We identified an Escherichia coli preparation of β-glucuronidase as free from contamination with any of the compounds tested. results demonstrate the importance of selecting appropriate enzyme preparations when quantifying naturally occurring, trace level compounds in biological fluids.