Property of arylsulfatase and β-glucuronidase extracted from digestive tracts of Cipangopaludina chinensis and their cleavage performance on conjugated natural estrogens.

Arylsulfatase and β-glucuronidase are the two substantial enzymes having a significant role in the cleavage of conjugated natural estrogens (C-NEs). The present study reports that arylsulfatase and β-glucuronidase have been abundantly found in the digestive tracts of Cipangopaludina chinensis; in which, their corresponding activities were 60 and 5 U/g wet waste, respectively. The arylsulfatase from Cipangopaludina chinensis could show high activity at low temperatures.

Activity measurement of arylsulfatase and β-glucuronidase in activated sludge: HPLC-based versus classical spectrophotometric method.

Arylsulfatase and β-glucuronidase are two important enzymes in wastewater and surface water, which play important roles on cleavage of sulfate/glucuronide estrogens. In this work, a high-performance liquid chromatography (HPLC)-based new method was firstly established for arylsulfatase/β-glucuronidase with determination of p-nitrophenyl sulfate (pNPS)/p-nitrophenyl-β-D-glucuronide (pNPG). The limits of detections (LODs) of the developed method for pNPS and pNPG were 0.

Sulfite may disrupt estrogen homeostasis in human via inhibition of steroid arylsulfatase.

Steroid arylsulfatase is an important enzyme in human, which plays an important role in dynamic equilibrium of natural estrogens. On the other hand, sulfite can be endogenously produced as a consequence of human body's metabolism of sulfur-containing amino acids, while its main sources to human are mainly derived from food as it is a widely used additive. Sulfite-sensitivity is a well-known phenomenon to a small proportion of populations.

Inhibition Properties of Arylsulfatase and β-Glucuronidase by Hydrogen Peroxide, Hypochlorite, and Peracetic Acid.

Arylsulfatase and β-glucuronidase are two important enzymes in humans, which play an important role in the dynamic equilibrium of steroidal estrogens. This work probably for the first time reported that hydrogen peroxide (HO), hypochlorite, and peracetic acid (PAA) could effectively inhibit the activities of arylsulfatase and/or β-glucuronidase. The 50% of inhibitions (IC) of HO, hypochlorite, and PAA on arylsulfatase were found to be 142.

Strategy for effective inhibition of arylsulfatase/β-glucuronidase to prevent deconjugation of sulfate and glucuronide conjugates in wastewater during sample collection and storage.

Arylsulfatase and β-glucuronidase are two important enzymes that are responsible for deconjugation of estrogen conjugates. It is important to keep estrogen conjugates intact during sample collection and storage, while the effective inhibition conditions for arylsulfatase and β-glucuronidase remain unknown. To elucidate these conditions, inhibition experiments were performed by adding several inhibitors or by introducing extreme pH conditions.