Fibrinolytic enzyme from Sand Warm Perinereis nuntia

Abstract

A protease from sandworms (Perinereis nuntia) was purified by using a combination of ammonium sulfate precipitation, DEAE cellulose and Superdex-200, respectively. The enriched preparation had a specific activity of 355.74 U/mg proteins and a yield of 18.5% total protein. The molecular weight of this protease was estimated to be 37.4 kDa by SDS-15% (w/v) PAGE. The pH stability of this protease is between pH 7-8, and it is stable up to 40 °C. The activity of the enzyme was inhibited by Cu2+ and Co2+, but was enhanced by Ca2+ and Mg2+ ions. Furthermore, protease activity was potently inhibited by EDTA.