Characterization of arylsulfatase activity in brine shrimp, Artemia salina

Abstract

Arylsulfatase from Artemia salina exists in at least two forms (AS I and AS II). The paper presents characterization of the AS II form of the arylsulfatase. The enzyme was able to hydrolyze p-nitrocatechol sulfate (pNCS) as well as ascorbate sulfate. It exhibited maximum activity at temperature of 50 °C and was stable for 2 h at 4–10 °C. Optimum pH shifted from 6.2 at 4 mM pNCS (substrate) to 4.8 at 20 mM pNCS. The enzyme displayed linear kinetics. AS II arylsulfatase exists in two molecular forms (349 and 460 kDa) composed of identical subunits with molecular mass of 53 kDa. Sulfite and phosphate ions were the most potent inhibitors of the enzyme. Cyanide proved to be a weak inhibitor. Sulfate and low concentrations of silver ions had no effect on the enzyme activity. Based on the above results, modifications in the assay for determination of enzyme activity are proposed.